Abstract

A surface enhanced Raman spectroscopy (SERS) based platform was developed for sensitive multiplexed detection of matrix metalloproteinases (MMP) (MMP-2 and MMP-7) with low limit of detection and high specificity. Detection is based on the virtue of enzymatic reaction where a peptide can be cleaved only by its corresponding enzyme. The platform comprises two components, a specialized SERS-based bimetallic-film-over-nanosphere (BMFON) substrate and gold nanoparticles (AuNPs). The two components were functionalized such that binding between the two would occur through biotin-avidin-biotin complexation. Binding is hindered by MMP peptide chains conjugated onto the surfaces of the substrate and AuNPs, and can be removed only by cleaving the peptide chains with corresponding enzymes. Since AuNP binding sites become free after the peptides are cleaved, the number of binding sites for AuNPs onto the substrate would increase. By tagging the AuNPs, concentrations of MMP-specific enzymes can be quantified through examining intensities of signature SERS peaks of the tags. This cleave-and-bind mechanism was first validated by individual detection and quantification of MMP-2 and MMP-7. The platform was demonstrated to be able to sensitively detect concentrations of specific enzymes ranging from 1 ng/mL to 40 µg/mL, with close correlation between SERS intensity and concentrations. Finally, the multiplexed detection of MMP-2 and MMP-7 was demonstrated. The multiplexity of this platform provides a robust way to analyze diseases associated with MMP-2 and MMP-7 enzymes. Our work can be further developed as a clinical diagnostic tool to detect other MMP proteinase in bio-fluids samples, widening the number of biomarkers needed to characterize diseases better.

© 2015 Optical Society of America

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  4. H. A. Kenny and E. Lengyel, “MMP-2 functions as an early response protein in ovarian cancer metastasis,” Cell Cycle 8(5), 683–688 (2009).
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    [Crossref] [PubMed]
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    [Crossref] [PubMed]
  7. H. J. Zhang, W. Zhao, S. Venkataraman, M. E. Robbins, G. R. Buettner, K. C. Kregel, and L. W. Oberley, “Activation of matrix metalloproteinase-2 by overexpression of manganese superoxide dismutase in human breast cancer MCF-7 cells involves reactive oxygen species,” J. Biol. Chem. 277(23), 20919–20926 (2002).
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    [Crossref] [PubMed]

2014 (1)

A. Polistena, A. Cucina, S. Dinicola, C. Stene, G. Cavallaro, A. Ciardi, G. Orlando, R. Arena, G. D’Ermo, A. Cavallaro, L. B. Johnson, and G. De Toma, “MMP7 expression in colorectal tumours of different stages,” In Vivo 28(1), 105–110 (2014).
[PubMed]

2013 (1)

P. Chen, R. Selegård, D. Aili, and B. Liedberg, “Peptide functionalized gold nanoparticles for colorimetric detection of matrilysin (MMP-7) activity,” Nanoscale 5(19), 8973–8976 (2013).
[Crossref] [PubMed]

2012 (1)

C. Y. Fu, K. W. Kho, U. S. Dinish, Z. Y. Koh, and O. Malini, “Enhancement in SERS intensity with hierarchical nanostructures by bimetallic deposition approach,” J. Raman Spectrosc. 43(8), 977–985 (2012).
[Crossref]

2011 (1)

C. Gialeli, A. D. Theocharis, and N. K. Karamanos, “Roles of matrix metalloproteinases in cancer progression and their pharmacological targeting,” FEBS J. 278(1), 16–27 (2011).
[Crossref] [PubMed]

2010 (1)

Y. Xu, Q. Cao, F. Svec, and J. M. J. Fréchet, “Porous Polymer Monolithic Column with Surface-Bound Gold Nanoparticles for the Capture and Separation of Cysteine-Containing Peptides,” Anal. Chem. 82(8), 3352–3358 (2010).
[Crossref] [PubMed]

2009 (2)

H. A. Kenny and E. Lengyel, “MMP-2 functions as an early response protein in ovarian cancer metastasis,” Cell Cycle 8(5), 683–688 (2009).
[Crossref] [PubMed]

A. Köhrmann, U. Kammerer, M. Kapp, J. Dietl, and J. Anacker, “Expression of matrix metalloproteinases (MMPs) in primary human breast cancer and breast cancer cell lines: New findings and review of the literature,” BMC Cancer 9(1), 188 (2009).
[Crossref] [PubMed]

2008 (1)

K. Jung, A. Ramankulov, M. Schrader, K. Miller, and M. Lein, “Circulating matrix metalloproteinase-7: an early or metastatic marker for renal cell carcinoma?” Clin. Chem. 54(11), 1927–1929 (2008).
[Crossref] [PubMed]

2007 (3)

S. Eissa, R. Ali-Labib, M. Swellam, M. Bassiony, F. Tash, and T. M. El-Zayat, “Noninvasive Diagnosis of Bladder Cancer by Detection of Matrix Metalloproteinases (MMP-2 and MMP-9) and Their Inhibitor (TIMP-2) in Urine,” Eur. Urol. 52(5), 1388–1397 (2007).
[Crossref] [PubMed]

M. Hilska, P. J. Roberts, Y. U. Collan, V. J. O. Laine, J. Kössi, P. Hirsimäki, O. Rahkonen, and M. Laato, “Prognostic significance of matrix metalloproteinases-1, -2, -7 and -13 and tissue inhibitors of metalloproteinases-1, -2, -3 and -4 in colorectal cancer,” Int. J. Cancer 121(4), 714–723 (2007).
[Crossref] [PubMed]

C.-B. Guo, S. Wang, C. Deng, D.-L. Zhang, F.-L. Wang, and X.-Q. Jin, “Relationship between Matrix Metalloproteinase 2 and Lung Cancer Progression,” Mol. Diagn. Ther. 11(3), 183–192 (2007).
[Crossref] [PubMed]

2006 (1)

L. Shi, V. De Paoli, N. Rosenzweig, and Z. Rosenzweig, “Synthesis and Application of Quantum Dots FRET-Based Protease Sensors,” J. Am. Chem. Soc. 128(32), 10378–10379 (2006).
[Crossref] [PubMed]

2005 (1)

M. Pesta, L. Holubec, O. Topolcan, M. Cerna, K. Rupert, L. S. Holubec, V. Treska, S. Kormunda, L. Elgrova, J. Finek, and R. Cerny, “Quantitative estimation of matrix metalloproteinases 2 and 7 (MMP-2, MMP-7) and tissue inhibitors of matrix metalloproteinases 1 and 2 (TIMP-1, TIMP-2) in colorectal carcinoma tissue samples,” Anticancer Res. 25(5), 3387–3391 (2005).
[PubMed]

2004 (3)

G. La Rocca, I. Pucci-Minafra, A. Marrazzo, P. Taormina, and S. Minafra, “Zymographic detection and clinical correlations of MMP-2 and MMP-9 in breast cancer sera,” Br. J. Cancer 90(7), 1414–1421 (2004).
[Crossref] [PubMed]

R. A. Alvarez-Puebla, S. Dos Santos Júnior, and R. F. Aroca, “Surface-enhanced Raman scattering for ultrasensitive chemical analysis of 1 and 2-naphthalenethiols,” Analyst (Lond.) 129(12), 1251–1256 (2004).
[Crossref] [PubMed]

L. E. Jones, M. J. Humphreys, F. Campbell, J. P. Neoptolemos, and M. T. Boyd, “Comprehensive Analysis of Matrix Metalloproteinase and Tissue Inhibitor Expression in Pancreatic Cancer: Increased Expression of Matrix Metalloproteinase-7 Predicts Poor Survival,” Clin. Cancer Res. 10(8), 2832–2845 (2004).
[Crossref] [PubMed]

2003 (3)

Y. Tanioka, T. Yoshida, T. Yagawa, Y. Saiki, S. Takeo, T. Harada, T. Okazawa, H. Yanai, and K. Okita, “Matrix metalloproteinase-7 and matrix metalloproteinase-9 are associated with unfavourable prognosis in superficial oesophageal cancer,” Br. J. Cancer 89(11), 2116–2121 (2003).
[Crossref] [PubMed]

J. Zheng, Y. Zhou, X. Li, Y. Ji, T. Lu, and R. Gu, “Surface-Enhanced Raman Scattering of 4-Aminothiophenol in Assemblies of Nanosized Particles and the Macroscopic Surface of Silver,” Langmuir 19(3), 632–636 (2003).
[Crossref]

M. G. Tutton, M. L. George, S. A. Eccles, S. Burton, R. I. Swift, and A. M. Abulafi, “Use of plasma MMP-2 and MMP-9 levels as a surrogate for tumour expression in colorectal cancer patients,” Int. J. Cancer 107(4), 541–550 (2003).
[Crossref] [PubMed]

2002 (1)

H. J. Zhang, W. Zhao, S. Venkataraman, M. E. Robbins, G. R. Buettner, K. C. Kregel, and L. W. Oberley, “Activation of matrix metalloproteinase-2 by overexpression of manganese superoxide dismutase in human breast cancer MCF-7 cells involves reactive oxygen species,” J. Biol. Chem. 277(23), 20919–20926 (2002).
[Crossref] [PubMed]

2001 (2)

B. Schmalfeldt, D. Prechtel, K. Härting, K. Späthe, S. Rutke, E. Konik, R. Fridman, U. Berger, M. Schmitt, W. Kuhn, and E. Lengyel, “Increased expression of matrix metalloproteinases (MMP)-2, MMP-9, and the urokinase-type plasminogen activator is associated with progression from benign to advanced ovarian cancer,” Clin. Cancer Res. 7(8), 2396–2404 (2001).
[PubMed]

H. Sasaki, H. Yukiue, S. Moiriyama, Y. Kobayashi, Y. Nakashima, M. Kaji, M. Kiriyama, I. Fukai, Y. Yamakawa, and Y. Fujii, “Clinical significance of matrix metalloproteinase-7 and Ets-1 gene expression in patients with lung cancer,” J. Surg. Res. 101(2), 242–247 (2001).
[Crossref] [PubMed]

2000 (5)

B. Passlick, W. Sienel, R. Seen-Hibler, W. Wöckel, O. Thetter, W. Mutschler, and K. Pantel, “Overexpression of matrix metalloproteinase 2 predicts unfavorable outcome in early-stage non-small cell lung cancer,” Clin. Cancer Res. 6(10), 3944–3948 (2000).
[PubMed]

K. Yamashita, M. Mori, T. Shiraishi, K. Shibuta, and K. Sugimachi, “Clinical Significance of Matrix Metalloproteinase-7 Expression in Esophageal Carcinoma,” Clin. Cancer Res. 6(3), 1169–1174 (2000).
[PubMed]

K. Kanda, M. Takahashi, Y. Murakami, H. Kanayama, and S. Kagawa, “The role of the activated form of matrix metalloproteinase-2 in urothelial cancer,” BJU Int. 86(4), 553–557 (2000).
[Crossref] [PubMed]

K. Ohashi, T. Nemoto, K. Nakamura, and R. Nemori, “Increased expression of matrix metalloproteinase 7 and 9 and membrane type 1-matrix metalloproteinase in esophageal squamous cell carcinomas,” Cancer 88(10), 2201–2209 (2000).
[Crossref] [PubMed]

V. Ellenrieder, B. Alber, U. Lacher, S. F. Hendler, A. Menke, W. Boeck, M. Wagner, M. Wilda, H. Friess, M. Büchler, G. Adler, and T. M. Gress, “Role of MT-MMPs and MMP-2 in pancreatic cancer progression,” Int. J. Cancer 85(1), 14–20 (2000).
[Crossref] [PubMed]

1999 (1)

B. Davidson, I. Goldberg, W. H. Gotlieb, J. Kopolovic, G. Ben-Baruch, J. M. Nesland, A. Berner, M. Bryne, and R. Reich, “High levels of MMP-2, MMP-9, MT1-MMP and TIMP-2 mRNA correlate with poor survival in ovarian carcinoma,” Clin. Exp. Metastasis 17(10), 799–808 (1999).
[Crossref] [PubMed]

1998 (1)

C. Gilles, J. A. Bassuk, H. Pulyaeva, E. H. Sage, J.-M. Foidart, and E. W. Thompson, “SPARC/osteonectin induces matrix metalloproteinase 2 activation in human breast cancer cell lines,” Cancer Res. 58(23), 5529–5536 (1998).
[PubMed]

1996 (2)

K. Gohji, N. Fujimoto, T. Komiyama, A. Fujii, J. Ohkawa, S. Kamidono, and M. Nakajima, “Elevation of serum levels of matrix metalloproteinase-2 and -3 as new predictors of recurrence in patients with urothelial carcinoma,” Cancer 78(11), 2379–2387 (1996).
[Crossref] [PubMed]

C. F. Sier, F. J. Kubben, S. Ganesh, M. M. Heerding, G. Griffioen, R. Hanemaaijer, J. H. van Krieken, C. B. Lamers, and H. W. Verspaget, “Tissue levels of matrix metalloproteinases MMP-2 and MMP-9 are related to the overall survival of patients with gastric carcinoma,” Br. J. Cancer 74(3), 413–417 (1996).
[Crossref] [PubMed]

1994 (1)

H. Sato, T. Takino, Y. Okada, J. Cao, A. Shinagawa, E. Yamamoto, and M. Seiki, “A matrix metalloproteinase expressed on the surface of invasive tumour cells,” Nature 370(6484), 61–65 (1994).
[Crossref] [PubMed]

1991 (1)

S. McDonnell, M. Navre, R. J. Coffey, and L. M. Matrisian, “Expression and localization of the matrix metalloproteinase pump-1 (MMP-7) in human gastric and colon carcinomas,” Mol. Carcinog. 4(6), 527–533 (1991).
[Crossref] [PubMed]

Abulafi, A. M.

M. G. Tutton, M. L. George, S. A. Eccles, S. Burton, R. I. Swift, and A. M. Abulafi, “Use of plasma MMP-2 and MMP-9 levels as a surrogate for tumour expression in colorectal cancer patients,” Int. J. Cancer 107(4), 541–550 (2003).
[Crossref] [PubMed]

Adler, G.

V. Ellenrieder, B. Alber, U. Lacher, S. F. Hendler, A. Menke, W. Boeck, M. Wagner, M. Wilda, H. Friess, M. Büchler, G. Adler, and T. M. Gress, “Role of MT-MMPs and MMP-2 in pancreatic cancer progression,” Int. J. Cancer 85(1), 14–20 (2000).
[Crossref] [PubMed]

Aili, D.

P. Chen, R. Selegård, D. Aili, and B. Liedberg, “Peptide functionalized gold nanoparticles for colorimetric detection of matrilysin (MMP-7) activity,” Nanoscale 5(19), 8973–8976 (2013).
[Crossref] [PubMed]

Alber, B.

V. Ellenrieder, B. Alber, U. Lacher, S. F. Hendler, A. Menke, W. Boeck, M. Wagner, M. Wilda, H. Friess, M. Büchler, G. Adler, and T. M. Gress, “Role of MT-MMPs and MMP-2 in pancreatic cancer progression,” Int. J. Cancer 85(1), 14–20 (2000).
[Crossref] [PubMed]

Ali-Labib, R.

S. Eissa, R. Ali-Labib, M. Swellam, M. Bassiony, F. Tash, and T. M. El-Zayat, “Noninvasive Diagnosis of Bladder Cancer by Detection of Matrix Metalloproteinases (MMP-2 and MMP-9) and Their Inhibitor (TIMP-2) in Urine,” Eur. Urol. 52(5), 1388–1397 (2007).
[Crossref] [PubMed]

Alvarez-Puebla, R. A.

R. A. Alvarez-Puebla, S. Dos Santos Júnior, and R. F. Aroca, “Surface-enhanced Raman scattering for ultrasensitive chemical analysis of 1 and 2-naphthalenethiols,” Analyst (Lond.) 129(12), 1251–1256 (2004).
[Crossref] [PubMed]

Anacker, J.

A. Köhrmann, U. Kammerer, M. Kapp, J. Dietl, and J. Anacker, “Expression of matrix metalloproteinases (MMPs) in primary human breast cancer and breast cancer cell lines: New findings and review of the literature,” BMC Cancer 9(1), 188 (2009).
[Crossref] [PubMed]

Arena, R.

A. Polistena, A. Cucina, S. Dinicola, C. Stene, G. Cavallaro, A. Ciardi, G. Orlando, R. Arena, G. D’Ermo, A. Cavallaro, L. B. Johnson, and G. De Toma, “MMP7 expression in colorectal tumours of different stages,” In Vivo 28(1), 105–110 (2014).
[PubMed]

Aroca, R. F.

R. A. Alvarez-Puebla, S. Dos Santos Júnior, and R. F. Aroca, “Surface-enhanced Raman scattering for ultrasensitive chemical analysis of 1 and 2-naphthalenethiols,” Analyst (Lond.) 129(12), 1251–1256 (2004).
[Crossref] [PubMed]

Bassiony, M.

S. Eissa, R. Ali-Labib, M. Swellam, M. Bassiony, F. Tash, and T. M. El-Zayat, “Noninvasive Diagnosis of Bladder Cancer by Detection of Matrix Metalloproteinases (MMP-2 and MMP-9) and Their Inhibitor (TIMP-2) in Urine,” Eur. Urol. 52(5), 1388–1397 (2007).
[Crossref] [PubMed]

Bassuk, J. A.

C. Gilles, J. A. Bassuk, H. Pulyaeva, E. H. Sage, J.-M. Foidart, and E. W. Thompson, “SPARC/osteonectin induces matrix metalloproteinase 2 activation in human breast cancer cell lines,” Cancer Res. 58(23), 5529–5536 (1998).
[PubMed]

Ben-Baruch, G.

B. Davidson, I. Goldberg, W. H. Gotlieb, J. Kopolovic, G. Ben-Baruch, J. M. Nesland, A. Berner, M. Bryne, and R. Reich, “High levels of MMP-2, MMP-9, MT1-MMP and TIMP-2 mRNA correlate with poor survival in ovarian carcinoma,” Clin. Exp. Metastasis 17(10), 799–808 (1999).
[Crossref] [PubMed]

Berger, U.

B. Schmalfeldt, D. Prechtel, K. Härting, K. Späthe, S. Rutke, E. Konik, R. Fridman, U. Berger, M. Schmitt, W. Kuhn, and E. Lengyel, “Increased expression of matrix metalloproteinases (MMP)-2, MMP-9, and the urokinase-type plasminogen activator is associated with progression from benign to advanced ovarian cancer,” Clin. Cancer Res. 7(8), 2396–2404 (2001).
[PubMed]

Berner, A.

B. Davidson, I. Goldberg, W. H. Gotlieb, J. Kopolovic, G. Ben-Baruch, J. M. Nesland, A. Berner, M. Bryne, and R. Reich, “High levels of MMP-2, MMP-9, MT1-MMP and TIMP-2 mRNA correlate with poor survival in ovarian carcinoma,” Clin. Exp. Metastasis 17(10), 799–808 (1999).
[Crossref] [PubMed]

Boeck, W.

V. Ellenrieder, B. Alber, U. Lacher, S. F. Hendler, A. Menke, W. Boeck, M. Wagner, M. Wilda, H. Friess, M. Büchler, G. Adler, and T. M. Gress, “Role of MT-MMPs and MMP-2 in pancreatic cancer progression,” Int. J. Cancer 85(1), 14–20 (2000).
[Crossref] [PubMed]

Boyd, M. T.

L. E. Jones, M. J. Humphreys, F. Campbell, J. P. Neoptolemos, and M. T. Boyd, “Comprehensive Analysis of Matrix Metalloproteinase and Tissue Inhibitor Expression in Pancreatic Cancer: Increased Expression of Matrix Metalloproteinase-7 Predicts Poor Survival,” Clin. Cancer Res. 10(8), 2832–2845 (2004).
[Crossref] [PubMed]

Bryne, M.

B. Davidson, I. Goldberg, W. H. Gotlieb, J. Kopolovic, G. Ben-Baruch, J. M. Nesland, A. Berner, M. Bryne, and R. Reich, “High levels of MMP-2, MMP-9, MT1-MMP and TIMP-2 mRNA correlate with poor survival in ovarian carcinoma,” Clin. Exp. Metastasis 17(10), 799–808 (1999).
[Crossref] [PubMed]

Büchler, M.

V. Ellenrieder, B. Alber, U. Lacher, S. F. Hendler, A. Menke, W. Boeck, M. Wagner, M. Wilda, H. Friess, M. Büchler, G. Adler, and T. M. Gress, “Role of MT-MMPs and MMP-2 in pancreatic cancer progression,” Int. J. Cancer 85(1), 14–20 (2000).
[Crossref] [PubMed]

Buettner, G. R.

H. J. Zhang, W. Zhao, S. Venkataraman, M. E. Robbins, G. R. Buettner, K. C. Kregel, and L. W. Oberley, “Activation of matrix metalloproteinase-2 by overexpression of manganese superoxide dismutase in human breast cancer MCF-7 cells involves reactive oxygen species,” J. Biol. Chem. 277(23), 20919–20926 (2002).
[Crossref] [PubMed]

Burton, S.

M. G. Tutton, M. L. George, S. A. Eccles, S. Burton, R. I. Swift, and A. M. Abulafi, “Use of plasma MMP-2 and MMP-9 levels as a surrogate for tumour expression in colorectal cancer patients,” Int. J. Cancer 107(4), 541–550 (2003).
[Crossref] [PubMed]

Campbell, F.

L. E. Jones, M. J. Humphreys, F. Campbell, J. P. Neoptolemos, and M. T. Boyd, “Comprehensive Analysis of Matrix Metalloproteinase and Tissue Inhibitor Expression in Pancreatic Cancer: Increased Expression of Matrix Metalloproteinase-7 Predicts Poor Survival,” Clin. Cancer Res. 10(8), 2832–2845 (2004).
[Crossref] [PubMed]

Cao, J.

H. Sato, T. Takino, Y. Okada, J. Cao, A. Shinagawa, E. Yamamoto, and M. Seiki, “A matrix metalloproteinase expressed on the surface of invasive tumour cells,” Nature 370(6484), 61–65 (1994).
[Crossref] [PubMed]

Cao, Q.

Y. Xu, Q. Cao, F. Svec, and J. M. J. Fréchet, “Porous Polymer Monolithic Column with Surface-Bound Gold Nanoparticles for the Capture and Separation of Cysteine-Containing Peptides,” Anal. Chem. 82(8), 3352–3358 (2010).
[Crossref] [PubMed]

Cavallaro, A.

A. Polistena, A. Cucina, S. Dinicola, C. Stene, G. Cavallaro, A. Ciardi, G. Orlando, R. Arena, G. D’Ermo, A. Cavallaro, L. B. Johnson, and G. De Toma, “MMP7 expression in colorectal tumours of different stages,” In Vivo 28(1), 105–110 (2014).
[PubMed]

Cavallaro, G.

A. Polistena, A. Cucina, S. Dinicola, C. Stene, G. Cavallaro, A. Ciardi, G. Orlando, R. Arena, G. D’Ermo, A. Cavallaro, L. B. Johnson, and G. De Toma, “MMP7 expression in colorectal tumours of different stages,” In Vivo 28(1), 105–110 (2014).
[PubMed]

Cerna, M.

M. Pesta, L. Holubec, O. Topolcan, M. Cerna, K. Rupert, L. S. Holubec, V. Treska, S. Kormunda, L. Elgrova, J. Finek, and R. Cerny, “Quantitative estimation of matrix metalloproteinases 2 and 7 (MMP-2, MMP-7) and tissue inhibitors of matrix metalloproteinases 1 and 2 (TIMP-1, TIMP-2) in colorectal carcinoma tissue samples,” Anticancer Res. 25(5), 3387–3391 (2005).
[PubMed]

Cerny, R.

M. Pesta, L. Holubec, O. Topolcan, M. Cerna, K. Rupert, L. S. Holubec, V. Treska, S. Kormunda, L. Elgrova, J. Finek, and R. Cerny, “Quantitative estimation of matrix metalloproteinases 2 and 7 (MMP-2, MMP-7) and tissue inhibitors of matrix metalloproteinases 1 and 2 (TIMP-1, TIMP-2) in colorectal carcinoma tissue samples,” Anticancer Res. 25(5), 3387–3391 (2005).
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Chen, P.

P. Chen, R. Selegård, D. Aili, and B. Liedberg, “Peptide functionalized gold nanoparticles for colorimetric detection of matrilysin (MMP-7) activity,” Nanoscale 5(19), 8973–8976 (2013).
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Ciardi, A.

A. Polistena, A. Cucina, S. Dinicola, C. Stene, G. Cavallaro, A. Ciardi, G. Orlando, R. Arena, G. D’Ermo, A. Cavallaro, L. B. Johnson, and G. De Toma, “MMP7 expression in colorectal tumours of different stages,” In Vivo 28(1), 105–110 (2014).
[PubMed]

Coffey, R. J.

S. McDonnell, M. Navre, R. J. Coffey, and L. M. Matrisian, “Expression and localization of the matrix metalloproteinase pump-1 (MMP-7) in human gastric and colon carcinomas,” Mol. Carcinog. 4(6), 527–533 (1991).
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Collan, Y. U.

M. Hilska, P. J. Roberts, Y. U. Collan, V. J. O. Laine, J. Kössi, P. Hirsimäki, O. Rahkonen, and M. Laato, “Prognostic significance of matrix metalloproteinases-1, -2, -7 and -13 and tissue inhibitors of metalloproteinases-1, -2, -3 and -4 in colorectal cancer,” Int. J. Cancer 121(4), 714–723 (2007).
[Crossref] [PubMed]

Cucina, A.

A. Polistena, A. Cucina, S. Dinicola, C. Stene, G. Cavallaro, A. Ciardi, G. Orlando, R. Arena, G. D’Ermo, A. Cavallaro, L. B. Johnson, and G. De Toma, “MMP7 expression in colorectal tumours of different stages,” In Vivo 28(1), 105–110 (2014).
[PubMed]

D’Ermo, G.

A. Polistena, A. Cucina, S. Dinicola, C. Stene, G. Cavallaro, A. Ciardi, G. Orlando, R. Arena, G. D’Ermo, A. Cavallaro, L. B. Johnson, and G. De Toma, “MMP7 expression in colorectal tumours of different stages,” In Vivo 28(1), 105–110 (2014).
[PubMed]

Davidson, B.

B. Davidson, I. Goldberg, W. H. Gotlieb, J. Kopolovic, G. Ben-Baruch, J. M. Nesland, A. Berner, M. Bryne, and R. Reich, “High levels of MMP-2, MMP-9, MT1-MMP and TIMP-2 mRNA correlate with poor survival in ovarian carcinoma,” Clin. Exp. Metastasis 17(10), 799–808 (1999).
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De Paoli, V.

L. Shi, V. De Paoli, N. Rosenzweig, and Z. Rosenzweig, “Synthesis and Application of Quantum Dots FRET-Based Protease Sensors,” J. Am. Chem. Soc. 128(32), 10378–10379 (2006).
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De Toma, G.

A. Polistena, A. Cucina, S. Dinicola, C. Stene, G. Cavallaro, A. Ciardi, G. Orlando, R. Arena, G. D’Ermo, A. Cavallaro, L. B. Johnson, and G. De Toma, “MMP7 expression in colorectal tumours of different stages,” In Vivo 28(1), 105–110 (2014).
[PubMed]

Deng, C.

C.-B. Guo, S. Wang, C. Deng, D.-L. Zhang, F.-L. Wang, and X.-Q. Jin, “Relationship between Matrix Metalloproteinase 2 and Lung Cancer Progression,” Mol. Diagn. Ther. 11(3), 183–192 (2007).
[Crossref] [PubMed]

Dietl, J.

A. Köhrmann, U. Kammerer, M. Kapp, J. Dietl, and J. Anacker, “Expression of matrix metalloproteinases (MMPs) in primary human breast cancer and breast cancer cell lines: New findings and review of the literature,” BMC Cancer 9(1), 188 (2009).
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Dinicola, S.

A. Polistena, A. Cucina, S. Dinicola, C. Stene, G. Cavallaro, A. Ciardi, G. Orlando, R. Arena, G. D’Ermo, A. Cavallaro, L. B. Johnson, and G. De Toma, “MMP7 expression in colorectal tumours of different stages,” In Vivo 28(1), 105–110 (2014).
[PubMed]

Dinish, U. S.

C. Y. Fu, K. W. Kho, U. S. Dinish, Z. Y. Koh, and O. Malini, “Enhancement in SERS intensity with hierarchical nanostructures by bimetallic deposition approach,” J. Raman Spectrosc. 43(8), 977–985 (2012).
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Dos Santos Júnior, S.

R. A. Alvarez-Puebla, S. Dos Santos Júnior, and R. F. Aroca, “Surface-enhanced Raman scattering for ultrasensitive chemical analysis of 1 and 2-naphthalenethiols,” Analyst (Lond.) 129(12), 1251–1256 (2004).
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Eccles, S. A.

M. G. Tutton, M. L. George, S. A. Eccles, S. Burton, R. I. Swift, and A. M. Abulafi, “Use of plasma MMP-2 and MMP-9 levels as a surrogate for tumour expression in colorectal cancer patients,” Int. J. Cancer 107(4), 541–550 (2003).
[Crossref] [PubMed]

Eissa, S.

S. Eissa, R. Ali-Labib, M. Swellam, M. Bassiony, F. Tash, and T. M. El-Zayat, “Noninvasive Diagnosis of Bladder Cancer by Detection of Matrix Metalloproteinases (MMP-2 and MMP-9) and Their Inhibitor (TIMP-2) in Urine,” Eur. Urol. 52(5), 1388–1397 (2007).
[Crossref] [PubMed]

Elgrova, L.

M. Pesta, L. Holubec, O. Topolcan, M. Cerna, K. Rupert, L. S. Holubec, V. Treska, S. Kormunda, L. Elgrova, J. Finek, and R. Cerny, “Quantitative estimation of matrix metalloproteinases 2 and 7 (MMP-2, MMP-7) and tissue inhibitors of matrix metalloproteinases 1 and 2 (TIMP-1, TIMP-2) in colorectal carcinoma tissue samples,” Anticancer Res. 25(5), 3387–3391 (2005).
[PubMed]

Ellenrieder, V.

V. Ellenrieder, B. Alber, U. Lacher, S. F. Hendler, A. Menke, W. Boeck, M. Wagner, M. Wilda, H. Friess, M. Büchler, G. Adler, and T. M. Gress, “Role of MT-MMPs and MMP-2 in pancreatic cancer progression,” Int. J. Cancer 85(1), 14–20 (2000).
[Crossref] [PubMed]

El-Zayat, T. M.

S. Eissa, R. Ali-Labib, M. Swellam, M. Bassiony, F. Tash, and T. M. El-Zayat, “Noninvasive Diagnosis of Bladder Cancer by Detection of Matrix Metalloproteinases (MMP-2 and MMP-9) and Their Inhibitor (TIMP-2) in Urine,” Eur. Urol. 52(5), 1388–1397 (2007).
[Crossref] [PubMed]

Finek, J.

M. Pesta, L. Holubec, O. Topolcan, M. Cerna, K. Rupert, L. S. Holubec, V. Treska, S. Kormunda, L. Elgrova, J. Finek, and R. Cerny, “Quantitative estimation of matrix metalloproteinases 2 and 7 (MMP-2, MMP-7) and tissue inhibitors of matrix metalloproteinases 1 and 2 (TIMP-1, TIMP-2) in colorectal carcinoma tissue samples,” Anticancer Res. 25(5), 3387–3391 (2005).
[PubMed]

Foidart, J.-M.

C. Gilles, J. A. Bassuk, H. Pulyaeva, E. H. Sage, J.-M. Foidart, and E. W. Thompson, “SPARC/osteonectin induces matrix metalloproteinase 2 activation in human breast cancer cell lines,” Cancer Res. 58(23), 5529–5536 (1998).
[PubMed]

Fréchet, J. M. J.

Y. Xu, Q. Cao, F. Svec, and J. M. J. Fréchet, “Porous Polymer Monolithic Column with Surface-Bound Gold Nanoparticles for the Capture and Separation of Cysteine-Containing Peptides,” Anal. Chem. 82(8), 3352–3358 (2010).
[Crossref] [PubMed]

Fridman, R.

B. Schmalfeldt, D. Prechtel, K. Härting, K. Späthe, S. Rutke, E. Konik, R. Fridman, U. Berger, M. Schmitt, W. Kuhn, and E. Lengyel, “Increased expression of matrix metalloproteinases (MMP)-2, MMP-9, and the urokinase-type plasminogen activator is associated with progression from benign to advanced ovarian cancer,” Clin. Cancer Res. 7(8), 2396–2404 (2001).
[PubMed]

Friess, H.

V. Ellenrieder, B. Alber, U. Lacher, S. F. Hendler, A. Menke, W. Boeck, M. Wagner, M. Wilda, H. Friess, M. Büchler, G. Adler, and T. M. Gress, “Role of MT-MMPs and MMP-2 in pancreatic cancer progression,” Int. J. Cancer 85(1), 14–20 (2000).
[Crossref] [PubMed]

Fu, C. Y.

C. Y. Fu, K. W. Kho, U. S. Dinish, Z. Y. Koh, and O. Malini, “Enhancement in SERS intensity with hierarchical nanostructures by bimetallic deposition approach,” J. Raman Spectrosc. 43(8), 977–985 (2012).
[Crossref]

Fujii, A.

K. Gohji, N. Fujimoto, T. Komiyama, A. Fujii, J. Ohkawa, S. Kamidono, and M. Nakajima, “Elevation of serum levels of matrix metalloproteinase-2 and -3 as new predictors of recurrence in patients with urothelial carcinoma,” Cancer 78(11), 2379–2387 (1996).
[Crossref] [PubMed]

Fujii, Y.

H. Sasaki, H. Yukiue, S. Moiriyama, Y. Kobayashi, Y. Nakashima, M. Kaji, M. Kiriyama, I. Fukai, Y. Yamakawa, and Y. Fujii, “Clinical significance of matrix metalloproteinase-7 and Ets-1 gene expression in patients with lung cancer,” J. Surg. Res. 101(2), 242–247 (2001).
[Crossref] [PubMed]

Fujimoto, N.

K. Gohji, N. Fujimoto, T. Komiyama, A. Fujii, J. Ohkawa, S. Kamidono, and M. Nakajima, “Elevation of serum levels of matrix metalloproteinase-2 and -3 as new predictors of recurrence in patients with urothelial carcinoma,” Cancer 78(11), 2379–2387 (1996).
[Crossref] [PubMed]

Fukai, I.

H. Sasaki, H. Yukiue, S. Moiriyama, Y. Kobayashi, Y. Nakashima, M. Kaji, M. Kiriyama, I. Fukai, Y. Yamakawa, and Y. Fujii, “Clinical significance of matrix metalloproteinase-7 and Ets-1 gene expression in patients with lung cancer,” J. Surg. Res. 101(2), 242–247 (2001).
[Crossref] [PubMed]

Ganesh, S.

C. F. Sier, F. J. Kubben, S. Ganesh, M. M. Heerding, G. Griffioen, R. Hanemaaijer, J. H. van Krieken, C. B. Lamers, and H. W. Verspaget, “Tissue levels of matrix metalloproteinases MMP-2 and MMP-9 are related to the overall survival of patients with gastric carcinoma,” Br. J. Cancer 74(3), 413–417 (1996).
[Crossref] [PubMed]

George, M. L.

M. G. Tutton, M. L. George, S. A. Eccles, S. Burton, R. I. Swift, and A. M. Abulafi, “Use of plasma MMP-2 and MMP-9 levels as a surrogate for tumour expression in colorectal cancer patients,” Int. J. Cancer 107(4), 541–550 (2003).
[Crossref] [PubMed]

Gialeli, C.

C. Gialeli, A. D. Theocharis, and N. K. Karamanos, “Roles of matrix metalloproteinases in cancer progression and their pharmacological targeting,” FEBS J. 278(1), 16–27 (2011).
[Crossref] [PubMed]

Gilles, C.

C. Gilles, J. A. Bassuk, H. Pulyaeva, E. H. Sage, J.-M. Foidart, and E. W. Thompson, “SPARC/osteonectin induces matrix metalloproteinase 2 activation in human breast cancer cell lines,” Cancer Res. 58(23), 5529–5536 (1998).
[PubMed]

Gohji, K.

K. Gohji, N. Fujimoto, T. Komiyama, A. Fujii, J. Ohkawa, S. Kamidono, and M. Nakajima, “Elevation of serum levels of matrix metalloproteinase-2 and -3 as new predictors of recurrence in patients with urothelial carcinoma,” Cancer 78(11), 2379–2387 (1996).
[Crossref] [PubMed]

Goldberg, I.

B. Davidson, I. Goldberg, W. H. Gotlieb, J. Kopolovic, G. Ben-Baruch, J. M. Nesland, A. Berner, M. Bryne, and R. Reich, “High levels of MMP-2, MMP-9, MT1-MMP and TIMP-2 mRNA correlate with poor survival in ovarian carcinoma,” Clin. Exp. Metastasis 17(10), 799–808 (1999).
[Crossref] [PubMed]

Gotlieb, W. H.

B. Davidson, I. Goldberg, W. H. Gotlieb, J. Kopolovic, G. Ben-Baruch, J. M. Nesland, A. Berner, M. Bryne, and R. Reich, “High levels of MMP-2, MMP-9, MT1-MMP and TIMP-2 mRNA correlate with poor survival in ovarian carcinoma,” Clin. Exp. Metastasis 17(10), 799–808 (1999).
[Crossref] [PubMed]

Gress, T. M.

V. Ellenrieder, B. Alber, U. Lacher, S. F. Hendler, A. Menke, W. Boeck, M. Wagner, M. Wilda, H. Friess, M. Büchler, G. Adler, and T. M. Gress, “Role of MT-MMPs and MMP-2 in pancreatic cancer progression,” Int. J. Cancer 85(1), 14–20 (2000).
[Crossref] [PubMed]

Griffioen, G.

C. F. Sier, F. J. Kubben, S. Ganesh, M. M. Heerding, G. Griffioen, R. Hanemaaijer, J. H. van Krieken, C. B. Lamers, and H. W. Verspaget, “Tissue levels of matrix metalloproteinases MMP-2 and MMP-9 are related to the overall survival of patients with gastric carcinoma,” Br. J. Cancer 74(3), 413–417 (1996).
[Crossref] [PubMed]

Gu, R.

J. Zheng, Y. Zhou, X. Li, Y. Ji, T. Lu, and R. Gu, “Surface-Enhanced Raman Scattering of 4-Aminothiophenol in Assemblies of Nanosized Particles and the Macroscopic Surface of Silver,” Langmuir 19(3), 632–636 (2003).
[Crossref]

Guo, C.-B.

C.-B. Guo, S. Wang, C. Deng, D.-L. Zhang, F.-L. Wang, and X.-Q. Jin, “Relationship between Matrix Metalloproteinase 2 and Lung Cancer Progression,” Mol. Diagn. Ther. 11(3), 183–192 (2007).
[Crossref] [PubMed]

Hanemaaijer, R.

C. F. Sier, F. J. Kubben, S. Ganesh, M. M. Heerding, G. Griffioen, R. Hanemaaijer, J. H. van Krieken, C. B. Lamers, and H. W. Verspaget, “Tissue levels of matrix metalloproteinases MMP-2 and MMP-9 are related to the overall survival of patients with gastric carcinoma,” Br. J. Cancer 74(3), 413–417 (1996).
[Crossref] [PubMed]

Harada, T.

Y. Tanioka, T. Yoshida, T. Yagawa, Y. Saiki, S. Takeo, T. Harada, T. Okazawa, H. Yanai, and K. Okita, “Matrix metalloproteinase-7 and matrix metalloproteinase-9 are associated with unfavourable prognosis in superficial oesophageal cancer,” Br. J. Cancer 89(11), 2116–2121 (2003).
[Crossref] [PubMed]

Härting, K.

B. Schmalfeldt, D. Prechtel, K. Härting, K. Späthe, S. Rutke, E. Konik, R. Fridman, U. Berger, M. Schmitt, W. Kuhn, and E. Lengyel, “Increased expression of matrix metalloproteinases (MMP)-2, MMP-9, and the urokinase-type plasminogen activator is associated with progression from benign to advanced ovarian cancer,” Clin. Cancer Res. 7(8), 2396–2404 (2001).
[PubMed]

Heerding, M. M.

C. F. Sier, F. J. Kubben, S. Ganesh, M. M. Heerding, G. Griffioen, R. Hanemaaijer, J. H. van Krieken, C. B. Lamers, and H. W. Verspaget, “Tissue levels of matrix metalloproteinases MMP-2 and MMP-9 are related to the overall survival of patients with gastric carcinoma,” Br. J. Cancer 74(3), 413–417 (1996).
[Crossref] [PubMed]

Hendler, S. F.

V. Ellenrieder, B. Alber, U. Lacher, S. F. Hendler, A. Menke, W. Boeck, M. Wagner, M. Wilda, H. Friess, M. Büchler, G. Adler, and T. M. Gress, “Role of MT-MMPs and MMP-2 in pancreatic cancer progression,” Int. J. Cancer 85(1), 14–20 (2000).
[Crossref] [PubMed]

Hilska, M.

M. Hilska, P. J. Roberts, Y. U. Collan, V. J. O. Laine, J. Kössi, P. Hirsimäki, O. Rahkonen, and M. Laato, “Prognostic significance of matrix metalloproteinases-1, -2, -7 and -13 and tissue inhibitors of metalloproteinases-1, -2, -3 and -4 in colorectal cancer,” Int. J. Cancer 121(4), 714–723 (2007).
[Crossref] [PubMed]

Hirsimäki, P.

M. Hilska, P. J. Roberts, Y. U. Collan, V. J. O. Laine, J. Kössi, P. Hirsimäki, O. Rahkonen, and M. Laato, “Prognostic significance of matrix metalloproteinases-1, -2, -7 and -13 and tissue inhibitors of metalloproteinases-1, -2, -3 and -4 in colorectal cancer,” Int. J. Cancer 121(4), 714–723 (2007).
[Crossref] [PubMed]

Holubec, L.

M. Pesta, L. Holubec, O. Topolcan, M. Cerna, K. Rupert, L. S. Holubec, V. Treska, S. Kormunda, L. Elgrova, J. Finek, and R. Cerny, “Quantitative estimation of matrix metalloproteinases 2 and 7 (MMP-2, MMP-7) and tissue inhibitors of matrix metalloproteinases 1 and 2 (TIMP-1, TIMP-2) in colorectal carcinoma tissue samples,” Anticancer Res. 25(5), 3387–3391 (2005).
[PubMed]

Holubec, L. S.

M. Pesta, L. Holubec, O. Topolcan, M. Cerna, K. Rupert, L. S. Holubec, V. Treska, S. Kormunda, L. Elgrova, J. Finek, and R. Cerny, “Quantitative estimation of matrix metalloproteinases 2 and 7 (MMP-2, MMP-7) and tissue inhibitors of matrix metalloproteinases 1 and 2 (TIMP-1, TIMP-2) in colorectal carcinoma tissue samples,” Anticancer Res. 25(5), 3387–3391 (2005).
[PubMed]

Humphreys, M. J.

L. E. Jones, M. J. Humphreys, F. Campbell, J. P. Neoptolemos, and M. T. Boyd, “Comprehensive Analysis of Matrix Metalloproteinase and Tissue Inhibitor Expression in Pancreatic Cancer: Increased Expression of Matrix Metalloproteinase-7 Predicts Poor Survival,” Clin. Cancer Res. 10(8), 2832–2845 (2004).
[Crossref] [PubMed]

Ji, Y.

J. Zheng, Y. Zhou, X. Li, Y. Ji, T. Lu, and R. Gu, “Surface-Enhanced Raman Scattering of 4-Aminothiophenol in Assemblies of Nanosized Particles and the Macroscopic Surface of Silver,” Langmuir 19(3), 632–636 (2003).
[Crossref]

Jin, X.-Q.

C.-B. Guo, S. Wang, C. Deng, D.-L. Zhang, F.-L. Wang, and X.-Q. Jin, “Relationship between Matrix Metalloproteinase 2 and Lung Cancer Progression,” Mol. Diagn. Ther. 11(3), 183–192 (2007).
[Crossref] [PubMed]

Johnson, L. B.

A. Polistena, A. Cucina, S. Dinicola, C. Stene, G. Cavallaro, A. Ciardi, G. Orlando, R. Arena, G. D’Ermo, A. Cavallaro, L. B. Johnson, and G. De Toma, “MMP7 expression in colorectal tumours of different stages,” In Vivo 28(1), 105–110 (2014).
[PubMed]

Jones, L. E.

L. E. Jones, M. J. Humphreys, F. Campbell, J. P. Neoptolemos, and M. T. Boyd, “Comprehensive Analysis of Matrix Metalloproteinase and Tissue Inhibitor Expression in Pancreatic Cancer: Increased Expression of Matrix Metalloproteinase-7 Predicts Poor Survival,” Clin. Cancer Res. 10(8), 2832–2845 (2004).
[Crossref] [PubMed]

Jung, K.

K. Jung, A. Ramankulov, M. Schrader, K. Miller, and M. Lein, “Circulating matrix metalloproteinase-7: an early or metastatic marker for renal cell carcinoma?” Clin. Chem. 54(11), 1927–1929 (2008).
[Crossref] [PubMed]

Kagawa, S.

K. Kanda, M. Takahashi, Y. Murakami, H. Kanayama, and S. Kagawa, “The role of the activated form of matrix metalloproteinase-2 in urothelial cancer,” BJU Int. 86(4), 553–557 (2000).
[Crossref] [PubMed]

Kaji, M.

H. Sasaki, H. Yukiue, S. Moiriyama, Y. Kobayashi, Y. Nakashima, M. Kaji, M. Kiriyama, I. Fukai, Y. Yamakawa, and Y. Fujii, “Clinical significance of matrix metalloproteinase-7 and Ets-1 gene expression in patients with lung cancer,” J. Surg. Res. 101(2), 242–247 (2001).
[Crossref] [PubMed]

Kamidono, S.

K. Gohji, N. Fujimoto, T. Komiyama, A. Fujii, J. Ohkawa, S. Kamidono, and M. Nakajima, “Elevation of serum levels of matrix metalloproteinase-2 and -3 as new predictors of recurrence in patients with urothelial carcinoma,” Cancer 78(11), 2379–2387 (1996).
[Crossref] [PubMed]

Kammerer, U.

A. Köhrmann, U. Kammerer, M. Kapp, J. Dietl, and J. Anacker, “Expression of matrix metalloproteinases (MMPs) in primary human breast cancer and breast cancer cell lines: New findings and review of the literature,” BMC Cancer 9(1), 188 (2009).
[Crossref] [PubMed]

Kanayama, H.

K. Kanda, M. Takahashi, Y. Murakami, H. Kanayama, and S. Kagawa, “The role of the activated form of matrix metalloproteinase-2 in urothelial cancer,” BJU Int. 86(4), 553–557 (2000).
[Crossref] [PubMed]

Kanda, K.

K. Kanda, M. Takahashi, Y. Murakami, H. Kanayama, and S. Kagawa, “The role of the activated form of matrix metalloproteinase-2 in urothelial cancer,” BJU Int. 86(4), 553–557 (2000).
[Crossref] [PubMed]

Kapp, M.

A. Köhrmann, U. Kammerer, M. Kapp, J. Dietl, and J. Anacker, “Expression of matrix metalloproteinases (MMPs) in primary human breast cancer and breast cancer cell lines: New findings and review of the literature,” BMC Cancer 9(1), 188 (2009).
[Crossref] [PubMed]

Karamanos, N. K.

C. Gialeli, A. D. Theocharis, and N. K. Karamanos, “Roles of matrix metalloproteinases in cancer progression and their pharmacological targeting,” FEBS J. 278(1), 16–27 (2011).
[Crossref] [PubMed]

Kenny, H. A.

H. A. Kenny and E. Lengyel, “MMP-2 functions as an early response protein in ovarian cancer metastasis,” Cell Cycle 8(5), 683–688 (2009).
[Crossref] [PubMed]

Kho, K. W.

C. Y. Fu, K. W. Kho, U. S. Dinish, Z. Y. Koh, and O. Malini, “Enhancement in SERS intensity with hierarchical nanostructures by bimetallic deposition approach,” J. Raman Spectrosc. 43(8), 977–985 (2012).
[Crossref]

Kiriyama, M.

H. Sasaki, H. Yukiue, S. Moiriyama, Y. Kobayashi, Y. Nakashima, M. Kaji, M. Kiriyama, I. Fukai, Y. Yamakawa, and Y. Fujii, “Clinical significance of matrix metalloproteinase-7 and Ets-1 gene expression in patients with lung cancer,” J. Surg. Res. 101(2), 242–247 (2001).
[Crossref] [PubMed]

Kobayashi, Y.

H. Sasaki, H. Yukiue, S. Moiriyama, Y. Kobayashi, Y. Nakashima, M. Kaji, M. Kiriyama, I. Fukai, Y. Yamakawa, and Y. Fujii, “Clinical significance of matrix metalloproteinase-7 and Ets-1 gene expression in patients with lung cancer,” J. Surg. Res. 101(2), 242–247 (2001).
[Crossref] [PubMed]

Koh, Z. Y.

C. Y. Fu, K. W. Kho, U. S. Dinish, Z. Y. Koh, and O. Malini, “Enhancement in SERS intensity with hierarchical nanostructures by bimetallic deposition approach,” J. Raman Spectrosc. 43(8), 977–985 (2012).
[Crossref]

Köhrmann, A.

A. Köhrmann, U. Kammerer, M. Kapp, J. Dietl, and J. Anacker, “Expression of matrix metalloproteinases (MMPs) in primary human breast cancer and breast cancer cell lines: New findings and review of the literature,” BMC Cancer 9(1), 188 (2009).
[Crossref] [PubMed]

Komiyama, T.

K. Gohji, N. Fujimoto, T. Komiyama, A. Fujii, J. Ohkawa, S. Kamidono, and M. Nakajima, “Elevation of serum levels of matrix metalloproteinase-2 and -3 as new predictors of recurrence in patients with urothelial carcinoma,” Cancer 78(11), 2379–2387 (1996).
[Crossref] [PubMed]

Konik, E.

B. Schmalfeldt, D. Prechtel, K. Härting, K. Späthe, S. Rutke, E. Konik, R. Fridman, U. Berger, M. Schmitt, W. Kuhn, and E. Lengyel, “Increased expression of matrix metalloproteinases (MMP)-2, MMP-9, and the urokinase-type plasminogen activator is associated with progression from benign to advanced ovarian cancer,” Clin. Cancer Res. 7(8), 2396–2404 (2001).
[PubMed]

Kopolovic, J.

B. Davidson, I. Goldberg, W. H. Gotlieb, J. Kopolovic, G. Ben-Baruch, J. M. Nesland, A. Berner, M. Bryne, and R. Reich, “High levels of MMP-2, MMP-9, MT1-MMP and TIMP-2 mRNA correlate with poor survival in ovarian carcinoma,” Clin. Exp. Metastasis 17(10), 799–808 (1999).
[Crossref] [PubMed]

Kormunda, S.

M. Pesta, L. Holubec, O. Topolcan, M. Cerna, K. Rupert, L. S. Holubec, V. Treska, S. Kormunda, L. Elgrova, J. Finek, and R. Cerny, “Quantitative estimation of matrix metalloproteinases 2 and 7 (MMP-2, MMP-7) and tissue inhibitors of matrix metalloproteinases 1 and 2 (TIMP-1, TIMP-2) in colorectal carcinoma tissue samples,” Anticancer Res. 25(5), 3387–3391 (2005).
[PubMed]

Kössi, J.

M. Hilska, P. J. Roberts, Y. U. Collan, V. J. O. Laine, J. Kössi, P. Hirsimäki, O. Rahkonen, and M. Laato, “Prognostic significance of matrix metalloproteinases-1, -2, -7 and -13 and tissue inhibitors of metalloproteinases-1, -2, -3 and -4 in colorectal cancer,” Int. J. Cancer 121(4), 714–723 (2007).
[Crossref] [PubMed]

Kregel, K. C.

H. J. Zhang, W. Zhao, S. Venkataraman, M. E. Robbins, G. R. Buettner, K. C. Kregel, and L. W. Oberley, “Activation of matrix metalloproteinase-2 by overexpression of manganese superoxide dismutase in human breast cancer MCF-7 cells involves reactive oxygen species,” J. Biol. Chem. 277(23), 20919–20926 (2002).
[Crossref] [PubMed]

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C. F. Sier, F. J. Kubben, S. Ganesh, M. M. Heerding, G. Griffioen, R. Hanemaaijer, J. H. van Krieken, C. B. Lamers, and H. W. Verspaget, “Tissue levels of matrix metalloproteinases MMP-2 and MMP-9 are related to the overall survival of patients with gastric carcinoma,” Br. J. Cancer 74(3), 413–417 (1996).
[Crossref] [PubMed]

Kuhn, W.

B. Schmalfeldt, D. Prechtel, K. Härting, K. Späthe, S. Rutke, E. Konik, R. Fridman, U. Berger, M. Schmitt, W. Kuhn, and E. Lengyel, “Increased expression of matrix metalloproteinases (MMP)-2, MMP-9, and the urokinase-type plasminogen activator is associated with progression from benign to advanced ovarian cancer,” Clin. Cancer Res. 7(8), 2396–2404 (2001).
[PubMed]

La Rocca, G.

G. La Rocca, I. Pucci-Minafra, A. Marrazzo, P. Taormina, and S. Minafra, “Zymographic detection and clinical correlations of MMP-2 and MMP-9 in breast cancer sera,” Br. J. Cancer 90(7), 1414–1421 (2004).
[Crossref] [PubMed]

Laato, M.

M. Hilska, P. J. Roberts, Y. U. Collan, V. J. O. Laine, J. Kössi, P. Hirsimäki, O. Rahkonen, and M. Laato, “Prognostic significance of matrix metalloproteinases-1, -2, -7 and -13 and tissue inhibitors of metalloproteinases-1, -2, -3 and -4 in colorectal cancer,” Int. J. Cancer 121(4), 714–723 (2007).
[Crossref] [PubMed]

Lacher, U.

V. Ellenrieder, B. Alber, U. Lacher, S. F. Hendler, A. Menke, W. Boeck, M. Wagner, M. Wilda, H. Friess, M. Büchler, G. Adler, and T. M. Gress, “Role of MT-MMPs and MMP-2 in pancreatic cancer progression,” Int. J. Cancer 85(1), 14–20 (2000).
[Crossref] [PubMed]

Laine, V. J. O.

M. Hilska, P. J. Roberts, Y. U. Collan, V. J. O. Laine, J. Kössi, P. Hirsimäki, O. Rahkonen, and M. Laato, “Prognostic significance of matrix metalloproteinases-1, -2, -7 and -13 and tissue inhibitors of metalloproteinases-1, -2, -3 and -4 in colorectal cancer,” Int. J. Cancer 121(4), 714–723 (2007).
[Crossref] [PubMed]

Lamers, C. B.

C. F. Sier, F. J. Kubben, S. Ganesh, M. M. Heerding, G. Griffioen, R. Hanemaaijer, J. H. van Krieken, C. B. Lamers, and H. W. Verspaget, “Tissue levels of matrix metalloproteinases MMP-2 and MMP-9 are related to the overall survival of patients with gastric carcinoma,” Br. J. Cancer 74(3), 413–417 (1996).
[Crossref] [PubMed]

Lein, M.

K. Jung, A. Ramankulov, M. Schrader, K. Miller, and M. Lein, “Circulating matrix metalloproteinase-7: an early or metastatic marker for renal cell carcinoma?” Clin. Chem. 54(11), 1927–1929 (2008).
[Crossref] [PubMed]

Lengyel, E.

H. A. Kenny and E. Lengyel, “MMP-2 functions as an early response protein in ovarian cancer metastasis,” Cell Cycle 8(5), 683–688 (2009).
[Crossref] [PubMed]

B. Schmalfeldt, D. Prechtel, K. Härting, K. Späthe, S. Rutke, E. Konik, R. Fridman, U. Berger, M. Schmitt, W. Kuhn, and E. Lengyel, “Increased expression of matrix metalloproteinases (MMP)-2, MMP-9, and the urokinase-type plasminogen activator is associated with progression from benign to advanced ovarian cancer,” Clin. Cancer Res. 7(8), 2396–2404 (2001).
[PubMed]

Li, X.

J. Zheng, Y. Zhou, X. Li, Y. Ji, T. Lu, and R. Gu, “Surface-Enhanced Raman Scattering of 4-Aminothiophenol in Assemblies of Nanosized Particles and the Macroscopic Surface of Silver,” Langmuir 19(3), 632–636 (2003).
[Crossref]

Liedberg, B.

P. Chen, R. Selegård, D. Aili, and B. Liedberg, “Peptide functionalized gold nanoparticles for colorimetric detection of matrilysin (MMP-7) activity,” Nanoscale 5(19), 8973–8976 (2013).
[Crossref] [PubMed]

Lu, T.

J. Zheng, Y. Zhou, X. Li, Y. Ji, T. Lu, and R. Gu, “Surface-Enhanced Raman Scattering of 4-Aminothiophenol in Assemblies of Nanosized Particles and the Macroscopic Surface of Silver,” Langmuir 19(3), 632–636 (2003).
[Crossref]

Malini, O.

C. Y. Fu, K. W. Kho, U. S. Dinish, Z. Y. Koh, and O. Malini, “Enhancement in SERS intensity with hierarchical nanostructures by bimetallic deposition approach,” J. Raman Spectrosc. 43(8), 977–985 (2012).
[Crossref]

Marrazzo, A.

G. La Rocca, I. Pucci-Minafra, A. Marrazzo, P. Taormina, and S. Minafra, “Zymographic detection and clinical correlations of MMP-2 and MMP-9 in breast cancer sera,” Br. J. Cancer 90(7), 1414–1421 (2004).
[Crossref] [PubMed]

Matrisian, L. M.

S. McDonnell, M. Navre, R. J. Coffey, and L. M. Matrisian, “Expression and localization of the matrix metalloproteinase pump-1 (MMP-7) in human gastric and colon carcinomas,” Mol. Carcinog. 4(6), 527–533 (1991).
[Crossref] [PubMed]

McDonnell, S.

S. McDonnell, M. Navre, R. J. Coffey, and L. M. Matrisian, “Expression and localization of the matrix metalloproteinase pump-1 (MMP-7) in human gastric and colon carcinomas,” Mol. Carcinog. 4(6), 527–533 (1991).
[Crossref] [PubMed]

Menke, A.

V. Ellenrieder, B. Alber, U. Lacher, S. F. Hendler, A. Menke, W. Boeck, M. Wagner, M. Wilda, H. Friess, M. Büchler, G. Adler, and T. M. Gress, “Role of MT-MMPs and MMP-2 in pancreatic cancer progression,” Int. J. Cancer 85(1), 14–20 (2000).
[Crossref] [PubMed]

Miller, K.

K. Jung, A. Ramankulov, M. Schrader, K. Miller, and M. Lein, “Circulating matrix metalloproteinase-7: an early or metastatic marker for renal cell carcinoma?” Clin. Chem. 54(11), 1927–1929 (2008).
[Crossref] [PubMed]

Minafra, S.

G. La Rocca, I. Pucci-Minafra, A. Marrazzo, P. Taormina, and S. Minafra, “Zymographic detection and clinical correlations of MMP-2 and MMP-9 in breast cancer sera,” Br. J. Cancer 90(7), 1414–1421 (2004).
[Crossref] [PubMed]

Moiriyama, S.

H. Sasaki, H. Yukiue, S. Moiriyama, Y. Kobayashi, Y. Nakashima, M. Kaji, M. Kiriyama, I. Fukai, Y. Yamakawa, and Y. Fujii, “Clinical significance of matrix metalloproteinase-7 and Ets-1 gene expression in patients with lung cancer,” J. Surg. Res. 101(2), 242–247 (2001).
[Crossref] [PubMed]

Mori, M.

K. Yamashita, M. Mori, T. Shiraishi, K. Shibuta, and K. Sugimachi, “Clinical Significance of Matrix Metalloproteinase-7 Expression in Esophageal Carcinoma,” Clin. Cancer Res. 6(3), 1169–1174 (2000).
[PubMed]

Murakami, Y.

K. Kanda, M. Takahashi, Y. Murakami, H. Kanayama, and S. Kagawa, “The role of the activated form of matrix metalloproteinase-2 in urothelial cancer,” BJU Int. 86(4), 553–557 (2000).
[Crossref] [PubMed]

Mutschler, W.

B. Passlick, W. Sienel, R. Seen-Hibler, W. Wöckel, O. Thetter, W. Mutschler, and K. Pantel, “Overexpression of matrix metalloproteinase 2 predicts unfavorable outcome in early-stage non-small cell lung cancer,” Clin. Cancer Res. 6(10), 3944–3948 (2000).
[PubMed]

Nakajima, M.

K. Gohji, N. Fujimoto, T. Komiyama, A. Fujii, J. Ohkawa, S. Kamidono, and M. Nakajima, “Elevation of serum levels of matrix metalloproteinase-2 and -3 as new predictors of recurrence in patients with urothelial carcinoma,” Cancer 78(11), 2379–2387 (1996).
[Crossref] [PubMed]

Nakamura, K.

K. Ohashi, T. Nemoto, K. Nakamura, and R. Nemori, “Increased expression of matrix metalloproteinase 7 and 9 and membrane type 1-matrix metalloproteinase in esophageal squamous cell carcinomas,” Cancer 88(10), 2201–2209 (2000).
[Crossref] [PubMed]

Nakashima, Y.

H. Sasaki, H. Yukiue, S. Moiriyama, Y. Kobayashi, Y. Nakashima, M. Kaji, M. Kiriyama, I. Fukai, Y. Yamakawa, and Y. Fujii, “Clinical significance of matrix metalloproteinase-7 and Ets-1 gene expression in patients with lung cancer,” J. Surg. Res. 101(2), 242–247 (2001).
[Crossref] [PubMed]

Navre, M.

S. McDonnell, M. Navre, R. J. Coffey, and L. M. Matrisian, “Expression and localization of the matrix metalloproteinase pump-1 (MMP-7) in human gastric and colon carcinomas,” Mol. Carcinog. 4(6), 527–533 (1991).
[Crossref] [PubMed]

Nemori, R.

K. Ohashi, T. Nemoto, K. Nakamura, and R. Nemori, “Increased expression of matrix metalloproteinase 7 and 9 and membrane type 1-matrix metalloproteinase in esophageal squamous cell carcinomas,” Cancer 88(10), 2201–2209 (2000).
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K. Ohashi, T. Nemoto, K. Nakamura, and R. Nemori, “Increased expression of matrix metalloproteinase 7 and 9 and membrane type 1-matrix metalloproteinase in esophageal squamous cell carcinomas,” Cancer 88(10), 2201–2209 (2000).
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L. E. Jones, M. J. Humphreys, F. Campbell, J. P. Neoptolemos, and M. T. Boyd, “Comprehensive Analysis of Matrix Metalloproteinase and Tissue Inhibitor Expression in Pancreatic Cancer: Increased Expression of Matrix Metalloproteinase-7 Predicts Poor Survival,” Clin. Cancer Res. 10(8), 2832–2845 (2004).
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Nesland, J. M.

B. Davidson, I. Goldberg, W. H. Gotlieb, J. Kopolovic, G. Ben-Baruch, J. M. Nesland, A. Berner, M. Bryne, and R. Reich, “High levels of MMP-2, MMP-9, MT1-MMP and TIMP-2 mRNA correlate with poor survival in ovarian carcinoma,” Clin. Exp. Metastasis 17(10), 799–808 (1999).
[Crossref] [PubMed]

Oberley, L. W.

H. J. Zhang, W. Zhao, S. Venkataraman, M. E. Robbins, G. R. Buettner, K. C. Kregel, and L. W. Oberley, “Activation of matrix metalloproteinase-2 by overexpression of manganese superoxide dismutase in human breast cancer MCF-7 cells involves reactive oxygen species,” J. Biol. Chem. 277(23), 20919–20926 (2002).
[Crossref] [PubMed]

Ohashi, K.

K. Ohashi, T. Nemoto, K. Nakamura, and R. Nemori, “Increased expression of matrix metalloproteinase 7 and 9 and membrane type 1-matrix metalloproteinase in esophageal squamous cell carcinomas,” Cancer 88(10), 2201–2209 (2000).
[Crossref] [PubMed]

Ohkawa, J.

K. Gohji, N. Fujimoto, T. Komiyama, A. Fujii, J. Ohkawa, S. Kamidono, and M. Nakajima, “Elevation of serum levels of matrix metalloproteinase-2 and -3 as new predictors of recurrence in patients with urothelial carcinoma,” Cancer 78(11), 2379–2387 (1996).
[Crossref] [PubMed]

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H. Sato, T. Takino, Y. Okada, J. Cao, A. Shinagawa, E. Yamamoto, and M. Seiki, “A matrix metalloproteinase expressed on the surface of invasive tumour cells,” Nature 370(6484), 61–65 (1994).
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Y. Tanioka, T. Yoshida, T. Yagawa, Y. Saiki, S. Takeo, T. Harada, T. Okazawa, H. Yanai, and K. Okita, “Matrix metalloproteinase-7 and matrix metalloproteinase-9 are associated with unfavourable prognosis in superficial oesophageal cancer,” Br. J. Cancer 89(11), 2116–2121 (2003).
[Crossref] [PubMed]

Okita, K.

Y. Tanioka, T. Yoshida, T. Yagawa, Y. Saiki, S. Takeo, T. Harada, T. Okazawa, H. Yanai, and K. Okita, “Matrix metalloproteinase-7 and matrix metalloproteinase-9 are associated with unfavourable prognosis in superficial oesophageal cancer,” Br. J. Cancer 89(11), 2116–2121 (2003).
[Crossref] [PubMed]

Orlando, G.

A. Polistena, A. Cucina, S. Dinicola, C. Stene, G. Cavallaro, A. Ciardi, G. Orlando, R. Arena, G. D’Ermo, A. Cavallaro, L. B. Johnson, and G. De Toma, “MMP7 expression in colorectal tumours of different stages,” In Vivo 28(1), 105–110 (2014).
[PubMed]

Pantel, K.

B. Passlick, W. Sienel, R. Seen-Hibler, W. Wöckel, O. Thetter, W. Mutschler, and K. Pantel, “Overexpression of matrix metalloproteinase 2 predicts unfavorable outcome in early-stage non-small cell lung cancer,” Clin. Cancer Res. 6(10), 3944–3948 (2000).
[PubMed]

Passlick, B.

B. Passlick, W. Sienel, R. Seen-Hibler, W. Wöckel, O. Thetter, W. Mutschler, and K. Pantel, “Overexpression of matrix metalloproteinase 2 predicts unfavorable outcome in early-stage non-small cell lung cancer,” Clin. Cancer Res. 6(10), 3944–3948 (2000).
[PubMed]

Pesta, M.

M. Pesta, L. Holubec, O. Topolcan, M. Cerna, K. Rupert, L. S. Holubec, V. Treska, S. Kormunda, L. Elgrova, J. Finek, and R. Cerny, “Quantitative estimation of matrix metalloproteinases 2 and 7 (MMP-2, MMP-7) and tissue inhibitors of matrix metalloproteinases 1 and 2 (TIMP-1, TIMP-2) in colorectal carcinoma tissue samples,” Anticancer Res. 25(5), 3387–3391 (2005).
[PubMed]

Polistena, A.

A. Polistena, A. Cucina, S. Dinicola, C. Stene, G. Cavallaro, A. Ciardi, G. Orlando, R. Arena, G. D’Ermo, A. Cavallaro, L. B. Johnson, and G. De Toma, “MMP7 expression in colorectal tumours of different stages,” In Vivo 28(1), 105–110 (2014).
[PubMed]

Prechtel, D.

B. Schmalfeldt, D. Prechtel, K. Härting, K. Späthe, S. Rutke, E. Konik, R. Fridman, U. Berger, M. Schmitt, W. Kuhn, and E. Lengyel, “Increased expression of matrix metalloproteinases (MMP)-2, MMP-9, and the urokinase-type plasminogen activator is associated with progression from benign to advanced ovarian cancer,” Clin. Cancer Res. 7(8), 2396–2404 (2001).
[PubMed]

Pucci-Minafra, I.

G. La Rocca, I. Pucci-Minafra, A. Marrazzo, P. Taormina, and S. Minafra, “Zymographic detection and clinical correlations of MMP-2 and MMP-9 in breast cancer sera,” Br. J. Cancer 90(7), 1414–1421 (2004).
[Crossref] [PubMed]

Pulyaeva, H.

C. Gilles, J. A. Bassuk, H. Pulyaeva, E. H. Sage, J.-M. Foidart, and E. W. Thompson, “SPARC/osteonectin induces matrix metalloproteinase 2 activation in human breast cancer cell lines,” Cancer Res. 58(23), 5529–5536 (1998).
[PubMed]

Rahkonen, O.

M. Hilska, P. J. Roberts, Y. U. Collan, V. J. O. Laine, J. Kössi, P. Hirsimäki, O. Rahkonen, and M. Laato, “Prognostic significance of matrix metalloproteinases-1, -2, -7 and -13 and tissue inhibitors of metalloproteinases-1, -2, -3 and -4 in colorectal cancer,” Int. J. Cancer 121(4), 714–723 (2007).
[Crossref] [PubMed]

Ramankulov, A.

K. Jung, A. Ramankulov, M. Schrader, K. Miller, and M. Lein, “Circulating matrix metalloproteinase-7: an early or metastatic marker for renal cell carcinoma?” Clin. Chem. 54(11), 1927–1929 (2008).
[Crossref] [PubMed]

Reich, R.

B. Davidson, I. Goldberg, W. H. Gotlieb, J. Kopolovic, G. Ben-Baruch, J. M. Nesland, A. Berner, M. Bryne, and R. Reich, “High levels of MMP-2, MMP-9, MT1-MMP and TIMP-2 mRNA correlate with poor survival in ovarian carcinoma,” Clin. Exp. Metastasis 17(10), 799–808 (1999).
[Crossref] [PubMed]

Robbins, M. E.

H. J. Zhang, W. Zhao, S. Venkataraman, M. E. Robbins, G. R. Buettner, K. C. Kregel, and L. W. Oberley, “Activation of matrix metalloproteinase-2 by overexpression of manganese superoxide dismutase in human breast cancer MCF-7 cells involves reactive oxygen species,” J. Biol. Chem. 277(23), 20919–20926 (2002).
[Crossref] [PubMed]

Roberts, P. J.

M. Hilska, P. J. Roberts, Y. U. Collan, V. J. O. Laine, J. Kössi, P. Hirsimäki, O. Rahkonen, and M. Laato, “Prognostic significance of matrix metalloproteinases-1, -2, -7 and -13 and tissue inhibitors of metalloproteinases-1, -2, -3 and -4 in colorectal cancer,” Int. J. Cancer 121(4), 714–723 (2007).
[Crossref] [PubMed]

Rosenzweig, N.

L. Shi, V. De Paoli, N. Rosenzweig, and Z. Rosenzweig, “Synthesis and Application of Quantum Dots FRET-Based Protease Sensors,” J. Am. Chem. Soc. 128(32), 10378–10379 (2006).
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Rosenzweig, Z.

L. Shi, V. De Paoli, N. Rosenzweig, and Z. Rosenzweig, “Synthesis and Application of Quantum Dots FRET-Based Protease Sensors,” J. Am. Chem. Soc. 128(32), 10378–10379 (2006).
[Crossref] [PubMed]

Rupert, K.

M. Pesta, L. Holubec, O. Topolcan, M. Cerna, K. Rupert, L. S. Holubec, V. Treska, S. Kormunda, L. Elgrova, J. Finek, and R. Cerny, “Quantitative estimation of matrix metalloproteinases 2 and 7 (MMP-2, MMP-7) and tissue inhibitors of matrix metalloproteinases 1 and 2 (TIMP-1, TIMP-2) in colorectal carcinoma tissue samples,” Anticancer Res. 25(5), 3387–3391 (2005).
[PubMed]

Rutke, S.

B. Schmalfeldt, D. Prechtel, K. Härting, K. Späthe, S. Rutke, E. Konik, R. Fridman, U. Berger, M. Schmitt, W. Kuhn, and E. Lengyel, “Increased expression of matrix metalloproteinases (MMP)-2, MMP-9, and the urokinase-type plasminogen activator is associated with progression from benign to advanced ovarian cancer,” Clin. Cancer Res. 7(8), 2396–2404 (2001).
[PubMed]

Sage, E. H.

C. Gilles, J. A. Bassuk, H. Pulyaeva, E. H. Sage, J.-M. Foidart, and E. W. Thompson, “SPARC/osteonectin induces matrix metalloproteinase 2 activation in human breast cancer cell lines,” Cancer Res. 58(23), 5529–5536 (1998).
[PubMed]

Saiki, Y.

Y. Tanioka, T. Yoshida, T. Yagawa, Y. Saiki, S. Takeo, T. Harada, T. Okazawa, H. Yanai, and K. Okita, “Matrix metalloproteinase-7 and matrix metalloproteinase-9 are associated with unfavourable prognosis in superficial oesophageal cancer,” Br. J. Cancer 89(11), 2116–2121 (2003).
[Crossref] [PubMed]

Sasaki, H.

H. Sasaki, H. Yukiue, S. Moiriyama, Y. Kobayashi, Y. Nakashima, M. Kaji, M. Kiriyama, I. Fukai, Y. Yamakawa, and Y. Fujii, “Clinical significance of matrix metalloproteinase-7 and Ets-1 gene expression in patients with lung cancer,” J. Surg. Res. 101(2), 242–247 (2001).
[Crossref] [PubMed]

Sato, H.

H. Sato, T. Takino, Y. Okada, J. Cao, A. Shinagawa, E. Yamamoto, and M. Seiki, “A matrix metalloproteinase expressed on the surface of invasive tumour cells,” Nature 370(6484), 61–65 (1994).
[Crossref] [PubMed]

Schmalfeldt, B.

B. Schmalfeldt, D. Prechtel, K. Härting, K. Späthe, S. Rutke, E. Konik, R. Fridman, U. Berger, M. Schmitt, W. Kuhn, and E. Lengyel, “Increased expression of matrix metalloproteinases (MMP)-2, MMP-9, and the urokinase-type plasminogen activator is associated with progression from benign to advanced ovarian cancer,” Clin. Cancer Res. 7(8), 2396–2404 (2001).
[PubMed]

Schmitt, M.

B. Schmalfeldt, D. Prechtel, K. Härting, K. Späthe, S. Rutke, E. Konik, R. Fridman, U. Berger, M. Schmitt, W. Kuhn, and E. Lengyel, “Increased expression of matrix metalloproteinases (MMP)-2, MMP-9, and the urokinase-type plasminogen activator is associated with progression from benign to advanced ovarian cancer,” Clin. Cancer Res. 7(8), 2396–2404 (2001).
[PubMed]

Schrader, M.

K. Jung, A. Ramankulov, M. Schrader, K. Miller, and M. Lein, “Circulating matrix metalloproteinase-7: an early or metastatic marker for renal cell carcinoma?” Clin. Chem. 54(11), 1927–1929 (2008).
[Crossref] [PubMed]

Seen-Hibler, R.

B. Passlick, W. Sienel, R. Seen-Hibler, W. Wöckel, O. Thetter, W. Mutschler, and K. Pantel, “Overexpression of matrix metalloproteinase 2 predicts unfavorable outcome in early-stage non-small cell lung cancer,” Clin. Cancer Res. 6(10), 3944–3948 (2000).
[PubMed]

Seiki, M.

H. Sato, T. Takino, Y. Okada, J. Cao, A. Shinagawa, E. Yamamoto, and M. Seiki, “A matrix metalloproteinase expressed on the surface of invasive tumour cells,” Nature 370(6484), 61–65 (1994).
[Crossref] [PubMed]

Selegård, R.

P. Chen, R. Selegård, D. Aili, and B. Liedberg, “Peptide functionalized gold nanoparticles for colorimetric detection of matrilysin (MMP-7) activity,” Nanoscale 5(19), 8973–8976 (2013).
[Crossref] [PubMed]

Shi, L.

L. Shi, V. De Paoli, N. Rosenzweig, and Z. Rosenzweig, “Synthesis and Application of Quantum Dots FRET-Based Protease Sensors,” J. Am. Chem. Soc. 128(32), 10378–10379 (2006).
[Crossref] [PubMed]

Shibuta, K.

K. Yamashita, M. Mori, T. Shiraishi, K. Shibuta, and K. Sugimachi, “Clinical Significance of Matrix Metalloproteinase-7 Expression in Esophageal Carcinoma,” Clin. Cancer Res. 6(3), 1169–1174 (2000).
[PubMed]

Shinagawa, A.

H. Sato, T. Takino, Y. Okada, J. Cao, A. Shinagawa, E. Yamamoto, and M. Seiki, “A matrix metalloproteinase expressed on the surface of invasive tumour cells,” Nature 370(6484), 61–65 (1994).
[Crossref] [PubMed]

Shiraishi, T.

K. Yamashita, M. Mori, T. Shiraishi, K. Shibuta, and K. Sugimachi, “Clinical Significance of Matrix Metalloproteinase-7 Expression in Esophageal Carcinoma,” Clin. Cancer Res. 6(3), 1169–1174 (2000).
[PubMed]

Sienel, W.

B. Passlick, W. Sienel, R. Seen-Hibler, W. Wöckel, O. Thetter, W. Mutschler, and K. Pantel, “Overexpression of matrix metalloproteinase 2 predicts unfavorable outcome in early-stage non-small cell lung cancer,” Clin. Cancer Res. 6(10), 3944–3948 (2000).
[PubMed]

Sier, C. F.

C. F. Sier, F. J. Kubben, S. Ganesh, M. M. Heerding, G. Griffioen, R. Hanemaaijer, J. H. van Krieken, C. B. Lamers, and H. W. Verspaget, “Tissue levels of matrix metalloproteinases MMP-2 and MMP-9 are related to the overall survival of patients with gastric carcinoma,” Br. J. Cancer 74(3), 413–417 (1996).
[Crossref] [PubMed]

Späthe, K.

B. Schmalfeldt, D. Prechtel, K. Härting, K. Späthe, S. Rutke, E. Konik, R. Fridman, U. Berger, M. Schmitt, W. Kuhn, and E. Lengyel, “Increased expression of matrix metalloproteinases (MMP)-2, MMP-9, and the urokinase-type plasminogen activator is associated with progression from benign to advanced ovarian cancer,” Clin. Cancer Res. 7(8), 2396–2404 (2001).
[PubMed]

Stene, C.

A. Polistena, A. Cucina, S. Dinicola, C. Stene, G. Cavallaro, A. Ciardi, G. Orlando, R. Arena, G. D’Ermo, A. Cavallaro, L. B. Johnson, and G. De Toma, “MMP7 expression in colorectal tumours of different stages,” In Vivo 28(1), 105–110 (2014).
[PubMed]

Sugimachi, K.

K. Yamashita, M. Mori, T. Shiraishi, K. Shibuta, and K. Sugimachi, “Clinical Significance of Matrix Metalloproteinase-7 Expression in Esophageal Carcinoma,” Clin. Cancer Res. 6(3), 1169–1174 (2000).
[PubMed]

Svec, F.

Y. Xu, Q. Cao, F. Svec, and J. M. J. Fréchet, “Porous Polymer Monolithic Column with Surface-Bound Gold Nanoparticles for the Capture and Separation of Cysteine-Containing Peptides,” Anal. Chem. 82(8), 3352–3358 (2010).
[Crossref] [PubMed]

Swellam, M.

S. Eissa, R. Ali-Labib, M. Swellam, M. Bassiony, F. Tash, and T. M. El-Zayat, “Noninvasive Diagnosis of Bladder Cancer by Detection of Matrix Metalloproteinases (MMP-2 and MMP-9) and Their Inhibitor (TIMP-2) in Urine,” Eur. Urol. 52(5), 1388–1397 (2007).
[Crossref] [PubMed]

Swift, R. I.

M. G. Tutton, M. L. George, S. A. Eccles, S. Burton, R. I. Swift, and A. M. Abulafi, “Use of plasma MMP-2 and MMP-9 levels as a surrogate for tumour expression in colorectal cancer patients,” Int. J. Cancer 107(4), 541–550 (2003).
[Crossref] [PubMed]

Takahashi, M.

K. Kanda, M. Takahashi, Y. Murakami, H. Kanayama, and S. Kagawa, “The role of the activated form of matrix metalloproteinase-2 in urothelial cancer,” BJU Int. 86(4), 553–557 (2000).
[Crossref] [PubMed]

Takeo, S.

Y. Tanioka, T. Yoshida, T. Yagawa, Y. Saiki, S. Takeo, T. Harada, T. Okazawa, H. Yanai, and K. Okita, “Matrix metalloproteinase-7 and matrix metalloproteinase-9 are associated with unfavourable prognosis in superficial oesophageal cancer,” Br. J. Cancer 89(11), 2116–2121 (2003).
[Crossref] [PubMed]

Takino, T.

H. Sato, T. Takino, Y. Okada, J. Cao, A. Shinagawa, E. Yamamoto, and M. Seiki, “A matrix metalloproteinase expressed on the surface of invasive tumour cells,” Nature 370(6484), 61–65 (1994).
[Crossref] [PubMed]

Tanioka, Y.

Y. Tanioka, T. Yoshida, T. Yagawa, Y. Saiki, S. Takeo, T. Harada, T. Okazawa, H. Yanai, and K. Okita, “Matrix metalloproteinase-7 and matrix metalloproteinase-9 are associated with unfavourable prognosis in superficial oesophageal cancer,” Br. J. Cancer 89(11), 2116–2121 (2003).
[Crossref] [PubMed]

Taormina, P.

G. La Rocca, I. Pucci-Minafra, A. Marrazzo, P. Taormina, and S. Minafra, “Zymographic detection and clinical correlations of MMP-2 and MMP-9 in breast cancer sera,” Br. J. Cancer 90(7), 1414–1421 (2004).
[Crossref] [PubMed]

Tash, F.

S. Eissa, R. Ali-Labib, M. Swellam, M. Bassiony, F. Tash, and T. M. El-Zayat, “Noninvasive Diagnosis of Bladder Cancer by Detection of Matrix Metalloproteinases (MMP-2 and MMP-9) and Their Inhibitor (TIMP-2) in Urine,” Eur. Urol. 52(5), 1388–1397 (2007).
[Crossref] [PubMed]

Theocharis, A. D.

C. Gialeli, A. D. Theocharis, and N. K. Karamanos, “Roles of matrix metalloproteinases in cancer progression and their pharmacological targeting,” FEBS J. 278(1), 16–27 (2011).
[Crossref] [PubMed]

Thetter, O.

B. Passlick, W. Sienel, R. Seen-Hibler, W. Wöckel, O. Thetter, W. Mutschler, and K. Pantel, “Overexpression of matrix metalloproteinase 2 predicts unfavorable outcome in early-stage non-small cell lung cancer,” Clin. Cancer Res. 6(10), 3944–3948 (2000).
[PubMed]

Thompson, E. W.

C. Gilles, J. A. Bassuk, H. Pulyaeva, E. H. Sage, J.-M. Foidart, and E. W. Thompson, “SPARC/osteonectin induces matrix metalloproteinase 2 activation in human breast cancer cell lines,” Cancer Res. 58(23), 5529–5536 (1998).
[PubMed]

Topolcan, O.

M. Pesta, L. Holubec, O. Topolcan, M. Cerna, K. Rupert, L. S. Holubec, V. Treska, S. Kormunda, L. Elgrova, J. Finek, and R. Cerny, “Quantitative estimation of matrix metalloproteinases 2 and 7 (MMP-2, MMP-7) and tissue inhibitors of matrix metalloproteinases 1 and 2 (TIMP-1, TIMP-2) in colorectal carcinoma tissue samples,” Anticancer Res. 25(5), 3387–3391 (2005).
[PubMed]

Treska, V.

M. Pesta, L. Holubec, O. Topolcan, M. Cerna, K. Rupert, L. S. Holubec, V. Treska, S. Kormunda, L. Elgrova, J. Finek, and R. Cerny, “Quantitative estimation of matrix metalloproteinases 2 and 7 (MMP-2, MMP-7) and tissue inhibitors of matrix metalloproteinases 1 and 2 (TIMP-1, TIMP-2) in colorectal carcinoma tissue samples,” Anticancer Res. 25(5), 3387–3391 (2005).
[PubMed]

Tutton, M. G.

M. G. Tutton, M. L. George, S. A. Eccles, S. Burton, R. I. Swift, and A. M. Abulafi, “Use of plasma MMP-2 and MMP-9 levels as a surrogate for tumour expression in colorectal cancer patients,” Int. J. Cancer 107(4), 541–550 (2003).
[Crossref] [PubMed]

van Krieken, J. H.

C. F. Sier, F. J. Kubben, S. Ganesh, M. M. Heerding, G. Griffioen, R. Hanemaaijer, J. H. van Krieken, C. B. Lamers, and H. W. Verspaget, “Tissue levels of matrix metalloproteinases MMP-2 and MMP-9 are related to the overall survival of patients with gastric carcinoma,” Br. J. Cancer 74(3), 413–417 (1996).
[Crossref] [PubMed]

Venkataraman, S.

H. J. Zhang, W. Zhao, S. Venkataraman, M. E. Robbins, G. R. Buettner, K. C. Kregel, and L. W. Oberley, “Activation of matrix metalloproteinase-2 by overexpression of manganese superoxide dismutase in human breast cancer MCF-7 cells involves reactive oxygen species,” J. Biol. Chem. 277(23), 20919–20926 (2002).
[Crossref] [PubMed]

Verspaget, H. W.

C. F. Sier, F. J. Kubben, S. Ganesh, M. M. Heerding, G. Griffioen, R. Hanemaaijer, J. H. van Krieken, C. B. Lamers, and H. W. Verspaget, “Tissue levels of matrix metalloproteinases MMP-2 and MMP-9 are related to the overall survival of patients with gastric carcinoma,” Br. J. Cancer 74(3), 413–417 (1996).
[Crossref] [PubMed]

Wagner, M.

V. Ellenrieder, B. Alber, U. Lacher, S. F. Hendler, A. Menke, W. Boeck, M. Wagner, M. Wilda, H. Friess, M. Büchler, G. Adler, and T. M. Gress, “Role of MT-MMPs and MMP-2 in pancreatic cancer progression,” Int. J. Cancer 85(1), 14–20 (2000).
[Crossref] [PubMed]

Wang, F.-L.

C.-B. Guo, S. Wang, C. Deng, D.-L. Zhang, F.-L. Wang, and X.-Q. Jin, “Relationship between Matrix Metalloproteinase 2 and Lung Cancer Progression,” Mol. Diagn. Ther. 11(3), 183–192 (2007).
[Crossref] [PubMed]

Wang, S.

C.-B. Guo, S. Wang, C. Deng, D.-L. Zhang, F.-L. Wang, and X.-Q. Jin, “Relationship between Matrix Metalloproteinase 2 and Lung Cancer Progression,” Mol. Diagn. Ther. 11(3), 183–192 (2007).
[Crossref] [PubMed]

Wilda, M.

V. Ellenrieder, B. Alber, U. Lacher, S. F. Hendler, A. Menke, W. Boeck, M. Wagner, M. Wilda, H. Friess, M. Büchler, G. Adler, and T. M. Gress, “Role of MT-MMPs and MMP-2 in pancreatic cancer progression,” Int. J. Cancer 85(1), 14–20 (2000).
[Crossref] [PubMed]

Wöckel, W.

B. Passlick, W. Sienel, R. Seen-Hibler, W. Wöckel, O. Thetter, W. Mutschler, and K. Pantel, “Overexpression of matrix metalloproteinase 2 predicts unfavorable outcome in early-stage non-small cell lung cancer,” Clin. Cancer Res. 6(10), 3944–3948 (2000).
[PubMed]

Xu, Y.

Y. Xu, Q. Cao, F. Svec, and J. M. J. Fréchet, “Porous Polymer Monolithic Column with Surface-Bound Gold Nanoparticles for the Capture and Separation of Cysteine-Containing Peptides,” Anal. Chem. 82(8), 3352–3358 (2010).
[Crossref] [PubMed]

Yagawa, T.

Y. Tanioka, T. Yoshida, T. Yagawa, Y. Saiki, S. Takeo, T. Harada, T. Okazawa, H. Yanai, and K. Okita, “Matrix metalloproteinase-7 and matrix metalloproteinase-9 are associated with unfavourable prognosis in superficial oesophageal cancer,” Br. J. Cancer 89(11), 2116–2121 (2003).
[Crossref] [PubMed]

Yamakawa, Y.

H. Sasaki, H. Yukiue, S. Moiriyama, Y. Kobayashi, Y. Nakashima, M. Kaji, M. Kiriyama, I. Fukai, Y. Yamakawa, and Y. Fujii, “Clinical significance of matrix metalloproteinase-7 and Ets-1 gene expression in patients with lung cancer,” J. Surg. Res. 101(2), 242–247 (2001).
[Crossref] [PubMed]

Yamamoto, E.

H. Sato, T. Takino, Y. Okada, J. Cao, A. Shinagawa, E. Yamamoto, and M. Seiki, “A matrix metalloproteinase expressed on the surface of invasive tumour cells,” Nature 370(6484), 61–65 (1994).
[Crossref] [PubMed]

Yamashita, K.

K. Yamashita, M. Mori, T. Shiraishi, K. Shibuta, and K. Sugimachi, “Clinical Significance of Matrix Metalloproteinase-7 Expression in Esophageal Carcinoma,” Clin. Cancer Res. 6(3), 1169–1174 (2000).
[PubMed]

Yanai, H.

Y. Tanioka, T. Yoshida, T. Yagawa, Y. Saiki, S. Takeo, T. Harada, T. Okazawa, H. Yanai, and K. Okita, “Matrix metalloproteinase-7 and matrix metalloproteinase-9 are associated with unfavourable prognosis in superficial oesophageal cancer,” Br. J. Cancer 89(11), 2116–2121 (2003).
[Crossref] [PubMed]

Yoshida, T.

Y. Tanioka, T. Yoshida, T. Yagawa, Y. Saiki, S. Takeo, T. Harada, T. Okazawa, H. Yanai, and K. Okita, “Matrix metalloproteinase-7 and matrix metalloproteinase-9 are associated with unfavourable prognosis in superficial oesophageal cancer,” Br. J. Cancer 89(11), 2116–2121 (2003).
[Crossref] [PubMed]

Yukiue, H.

H. Sasaki, H. Yukiue, S. Moiriyama, Y. Kobayashi, Y. Nakashima, M. Kaji, M. Kiriyama, I. Fukai, Y. Yamakawa, and Y. Fujii, “Clinical significance of matrix metalloproteinase-7 and Ets-1 gene expression in patients with lung cancer,” J. Surg. Res. 101(2), 242–247 (2001).
[Crossref] [PubMed]

Zhang, D.-L.

C.-B. Guo, S. Wang, C. Deng, D.-L. Zhang, F.-L. Wang, and X.-Q. Jin, “Relationship between Matrix Metalloproteinase 2 and Lung Cancer Progression,” Mol. Diagn. Ther. 11(3), 183–192 (2007).
[Crossref] [PubMed]

Zhang, H. J.

H. J. Zhang, W. Zhao, S. Venkataraman, M. E. Robbins, G. R. Buettner, K. C. Kregel, and L. W. Oberley, “Activation of matrix metalloproteinase-2 by overexpression of manganese superoxide dismutase in human breast cancer MCF-7 cells involves reactive oxygen species,” J. Biol. Chem. 277(23), 20919–20926 (2002).
[Crossref] [PubMed]

Zhao, W.

H. J. Zhang, W. Zhao, S. Venkataraman, M. E. Robbins, G. R. Buettner, K. C. Kregel, and L. W. Oberley, “Activation of matrix metalloproteinase-2 by overexpression of manganese superoxide dismutase in human breast cancer MCF-7 cells involves reactive oxygen species,” J. Biol. Chem. 277(23), 20919–20926 (2002).
[Crossref] [PubMed]

Zheng, J.

J. Zheng, Y. Zhou, X. Li, Y. Ji, T. Lu, and R. Gu, “Surface-Enhanced Raman Scattering of 4-Aminothiophenol in Assemblies of Nanosized Particles and the Macroscopic Surface of Silver,” Langmuir 19(3), 632–636 (2003).
[Crossref]

Zhou, Y.

J. Zheng, Y. Zhou, X. Li, Y. Ji, T. Lu, and R. Gu, “Surface-Enhanced Raman Scattering of 4-Aminothiophenol in Assemblies of Nanosized Particles and the Macroscopic Surface of Silver,” Langmuir 19(3), 632–636 (2003).
[Crossref]

Anal. Chem. (1)

Y. Xu, Q. Cao, F. Svec, and J. M. J. Fréchet, “Porous Polymer Monolithic Column with Surface-Bound Gold Nanoparticles for the Capture and Separation of Cysteine-Containing Peptides,” Anal. Chem. 82(8), 3352–3358 (2010).
[Crossref] [PubMed]

Analyst (Lond.) (1)

R. A. Alvarez-Puebla, S. Dos Santos Júnior, and R. F. Aroca, “Surface-enhanced Raman scattering for ultrasensitive chemical analysis of 1 and 2-naphthalenethiols,” Analyst (Lond.) 129(12), 1251–1256 (2004).
[Crossref] [PubMed]

Anticancer Res. (1)

M. Pesta, L. Holubec, O. Topolcan, M. Cerna, K. Rupert, L. S. Holubec, V. Treska, S. Kormunda, L. Elgrova, J. Finek, and R. Cerny, “Quantitative estimation of matrix metalloproteinases 2 and 7 (MMP-2, MMP-7) and tissue inhibitors of matrix metalloproteinases 1 and 2 (TIMP-1, TIMP-2) in colorectal carcinoma tissue samples,” Anticancer Res. 25(5), 3387–3391 (2005).
[PubMed]

BJU Int. (1)

K. Kanda, M. Takahashi, Y. Murakami, H. Kanayama, and S. Kagawa, “The role of the activated form of matrix metalloproteinase-2 in urothelial cancer,” BJU Int. 86(4), 553–557 (2000).
[Crossref] [PubMed]

BMC Cancer (1)

A. Köhrmann, U. Kammerer, M. Kapp, J. Dietl, and J. Anacker, “Expression of matrix metalloproteinases (MMPs) in primary human breast cancer and breast cancer cell lines: New findings and review of the literature,” BMC Cancer 9(1), 188 (2009).
[Crossref] [PubMed]

Br. J. Cancer (3)

Y. Tanioka, T. Yoshida, T. Yagawa, Y. Saiki, S. Takeo, T. Harada, T. Okazawa, H. Yanai, and K. Okita, “Matrix metalloproteinase-7 and matrix metalloproteinase-9 are associated with unfavourable prognosis in superficial oesophageal cancer,” Br. J. Cancer 89(11), 2116–2121 (2003).
[Crossref] [PubMed]

C. F. Sier, F. J. Kubben, S. Ganesh, M. M. Heerding, G. Griffioen, R. Hanemaaijer, J. H. van Krieken, C. B. Lamers, and H. W. Verspaget, “Tissue levels of matrix metalloproteinases MMP-2 and MMP-9 are related to the overall survival of patients with gastric carcinoma,” Br. J. Cancer 74(3), 413–417 (1996).
[Crossref] [PubMed]

G. La Rocca, I. Pucci-Minafra, A. Marrazzo, P. Taormina, and S. Minafra, “Zymographic detection and clinical correlations of MMP-2 and MMP-9 in breast cancer sera,” Br. J. Cancer 90(7), 1414–1421 (2004).
[Crossref] [PubMed]

Cancer (2)

K. Gohji, N. Fujimoto, T. Komiyama, A. Fujii, J. Ohkawa, S. Kamidono, and M. Nakajima, “Elevation of serum levels of matrix metalloproteinase-2 and -3 as new predictors of recurrence in patients with urothelial carcinoma,” Cancer 78(11), 2379–2387 (1996).
[Crossref] [PubMed]

K. Ohashi, T. Nemoto, K. Nakamura, and R. Nemori, “Increased expression of matrix metalloproteinase 7 and 9 and membrane type 1-matrix metalloproteinase in esophageal squamous cell carcinomas,” Cancer 88(10), 2201–2209 (2000).
[Crossref] [PubMed]

Cancer Res. (1)

C. Gilles, J. A. Bassuk, H. Pulyaeva, E. H. Sage, J.-M. Foidart, and E. W. Thompson, “SPARC/osteonectin induces matrix metalloproteinase 2 activation in human breast cancer cell lines,” Cancer Res. 58(23), 5529–5536 (1998).
[PubMed]

Cell Cycle (1)

H. A. Kenny and E. Lengyel, “MMP-2 functions as an early response protein in ovarian cancer metastasis,” Cell Cycle 8(5), 683–688 (2009).
[Crossref] [PubMed]

Clin. Cancer Res. (4)

B. Schmalfeldt, D. Prechtel, K. Härting, K. Späthe, S. Rutke, E. Konik, R. Fridman, U. Berger, M. Schmitt, W. Kuhn, and E. Lengyel, “Increased expression of matrix metalloproteinases (MMP)-2, MMP-9, and the urokinase-type plasminogen activator is associated with progression from benign to advanced ovarian cancer,” Clin. Cancer Res. 7(8), 2396–2404 (2001).
[PubMed]

K. Yamashita, M. Mori, T. Shiraishi, K. Shibuta, and K. Sugimachi, “Clinical Significance of Matrix Metalloproteinase-7 Expression in Esophageal Carcinoma,” Clin. Cancer Res. 6(3), 1169–1174 (2000).
[PubMed]

B. Passlick, W. Sienel, R. Seen-Hibler, W. Wöckel, O. Thetter, W. Mutschler, and K. Pantel, “Overexpression of matrix metalloproteinase 2 predicts unfavorable outcome in early-stage non-small cell lung cancer,” Clin. Cancer Res. 6(10), 3944–3948 (2000).
[PubMed]

L. E. Jones, M. J. Humphreys, F. Campbell, J. P. Neoptolemos, and M. T. Boyd, “Comprehensive Analysis of Matrix Metalloproteinase and Tissue Inhibitor Expression in Pancreatic Cancer: Increased Expression of Matrix Metalloproteinase-7 Predicts Poor Survival,” Clin. Cancer Res. 10(8), 2832–2845 (2004).
[Crossref] [PubMed]

Clin. Chem. (1)

K. Jung, A. Ramankulov, M. Schrader, K. Miller, and M. Lein, “Circulating matrix metalloproteinase-7: an early or metastatic marker for renal cell carcinoma?” Clin. Chem. 54(11), 1927–1929 (2008).
[Crossref] [PubMed]

Clin. Exp. Metastasis (1)

B. Davidson, I. Goldberg, W. H. Gotlieb, J. Kopolovic, G. Ben-Baruch, J. M. Nesland, A. Berner, M. Bryne, and R. Reich, “High levels of MMP-2, MMP-9, MT1-MMP and TIMP-2 mRNA correlate with poor survival in ovarian carcinoma,” Clin. Exp. Metastasis 17(10), 799–808 (1999).
[Crossref] [PubMed]

Eur. Urol. (1)

S. Eissa, R. Ali-Labib, M. Swellam, M. Bassiony, F. Tash, and T. M. El-Zayat, “Noninvasive Diagnosis of Bladder Cancer by Detection of Matrix Metalloproteinases (MMP-2 and MMP-9) and Their Inhibitor (TIMP-2) in Urine,” Eur. Urol. 52(5), 1388–1397 (2007).
[Crossref] [PubMed]

FEBS J. (1)

C. Gialeli, A. D. Theocharis, and N. K. Karamanos, “Roles of matrix metalloproteinases in cancer progression and their pharmacological targeting,” FEBS J. 278(1), 16–27 (2011).
[Crossref] [PubMed]

In Vivo (1)

A. Polistena, A. Cucina, S. Dinicola, C. Stene, G. Cavallaro, A. Ciardi, G. Orlando, R. Arena, G. D’Ermo, A. Cavallaro, L. B. Johnson, and G. De Toma, “MMP7 expression in colorectal tumours of different stages,” In Vivo 28(1), 105–110 (2014).
[PubMed]

Int. J. Cancer (3)

M. Hilska, P. J. Roberts, Y. U. Collan, V. J. O. Laine, J. Kössi, P. Hirsimäki, O. Rahkonen, and M. Laato, “Prognostic significance of matrix metalloproteinases-1, -2, -7 and -13 and tissue inhibitors of metalloproteinases-1, -2, -3 and -4 in colorectal cancer,” Int. J. Cancer 121(4), 714–723 (2007).
[Crossref] [PubMed]

M. G. Tutton, M. L. George, S. A. Eccles, S. Burton, R. I. Swift, and A. M. Abulafi, “Use of plasma MMP-2 and MMP-9 levels as a surrogate for tumour expression in colorectal cancer patients,” Int. J. Cancer 107(4), 541–550 (2003).
[Crossref] [PubMed]

V. Ellenrieder, B. Alber, U. Lacher, S. F. Hendler, A. Menke, W. Boeck, M. Wagner, M. Wilda, H. Friess, M. Büchler, G. Adler, and T. M. Gress, “Role of MT-MMPs and MMP-2 in pancreatic cancer progression,” Int. J. Cancer 85(1), 14–20 (2000).
[Crossref] [PubMed]

J. Am. Chem. Soc. (1)

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H. J. Zhang, W. Zhao, S. Venkataraman, M. E. Robbins, G. R. Buettner, K. C. Kregel, and L. W. Oberley, “Activation of matrix metalloproteinase-2 by overexpression of manganese superoxide dismutase in human breast cancer MCF-7 cells involves reactive oxygen species,” J. Biol. Chem. 277(23), 20919–20926 (2002).
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Figures (4)

Fig. 1
Fig. 1 Schematic illustration of tagged AuNPs biding on BMFON after MMP-2/MMP-7 enzyme cleaving of peptides on BMFON and AuNPs.
Fig. 2
Fig. 2 BMFON characterization. SEM imaging of (a) clean BMFON substrate (b) peptide shielded biotin-avidin conjugated BMFON and (c) AuNPs bond BMFON after enzyme cleaving. (d)(e)(f) Enlargement of images from the area (area within white squares) in (a)(b)(c), respectively.(g) SERS mapping of peptide conjugated BMFON. (h) SERS mapping of peptide conjugated BMFON after enzyme cleavage. (e) Raman spectra of MMP peptide bound BMFON substrate before and after enzyme cleaving.
Fig. 3
Fig. 3 Detection of individual MMP enzymes. Chemical structure and Raman spectra of (a) ATP and (b) NT. SERS spectra of (c) biotin-PEG–SH bound BMFON and (d) NeutrAvidin-biotin-PEG–SH bound BMFON. (e) SERS spectra of ATP tagged AuNPs bound MMP-7 conjugated BMFON after incubated with different concentrations of MMP-7 enzyme. (f) SERS spectra of NT tagged AuNPs bound MMP-2 conjugated BMFON after incubation with different concentrations of MMP-2 enzyme. (g) Intensity curve of the ATP Raman peak at 1584 cm-1 (x-axis is log10 scaled). (h) Intensity curve of the NT Raman peak at 1377cm-1 (x-axis is log10 scaled).
Fig. 4
Fig. 4 Multiplexed detection of MMP-2 and MMP-7 enzymes. Raman spectrum of MMP-2 and MMP-7 shielded BMFON substrate samples in the presence of (a) control solution contain no enzyme (b) MMP-2 enzyme (c) MMP-7 enzyme (d) both MMP-2 and MMP-7 enzyme.

Tables (1)

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Table 1 Peak Assignment of Raman Spectra

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