Abstract

We observe adhesion sites of a cell on a substrate with high resolution. Since this observation requires interfacial measurements between the cell and the substrate, we employ scanning localized surface plasmon microscopy. We experimentally show that focal adhesion sites of a mouse muscle cell can be observed without fluorescent labeling. We also show that a non-scanning surface plasmon microscope combined with the scanning localized surface plasmon microscope contributes to observing an entire cell adhesion site and identify regions of interest.

© 2012 OSA

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2010 (2)

2009 (2)

A. Yamada, Y. Katanosaka, S. Mohri, and K. Naruse, “A rapid microfluidic switching system for analysis at the single cellular level,” IEEE Trans. Nanobioscience8(4), 306–311 (2009).
[CrossRef] [PubMed]

A. W. Peterson, M. Halter, A. Tona, K. Bhadriraju, and A. L. Plant, “Surface plasmon resonance imaging of cells and surface-associated fibronectin,” BMC Cell Biol.10(1), 16 (2009).
[CrossRef] [PubMed]

2007 (1)

2005 (1)

L. Formigli, E. Meacci, C. Sassoli, F. Chellini, R. Giannini, F. Quercioli, B. Tiribilli, R. Squecco, P. Bruni, F. Francini, and S. Zecchi-Orlandini, “Sphingosine 1-phosphate induces cytoskeletal reorganization in C2C12 myoblasts: physiological relevance for stress fibres in the modulation of ion current through stretch-activated channels,” J. Cell Sci.118(6), 1161–1171 (2005).
[CrossRef] [PubMed]

2003 (3)

K. M. Yamada, R. Pankov, and E. Cukierman, “Dimensions and dynamics in integrin function,” Braz. J. Med. Biol. Res.36(8), 959–966 (2003).
[CrossRef] [PubMed]

U. S. Schwarz, N. Q. Balaban, D. Riveline, L. Addadi, A. Bershadsky, S. A. Safran, and B. Geiger, “Measurement of cellular force at focal adhesions using elastic micro-patterned substrates,” Mater. Sci. Eng. C23(3), 387–394 (2003).
[CrossRef]

A. J. Ridley, M. A. Schwartz, K. Burridge, R. A. Firtel, M. H. Ginsberg, G. Borisy, J. T. Parsons, and A. R. Horwitz, “Cell migration: integrating signals from front to back,” Science302(5651), 1704–1709 (2003).
[CrossRef] [PubMed]

2001 (2)

N. Q. Balaban, U. S. Schwarz, D. Riveline, P. Goichberg, G. Tzur, I. Sabanay, D. Mahalu, S. Safran, A. Bershadsky, L. Addadi, and B. Geiger, “Force and focal adhesion assembly: a close relationship studied using elastic micropatterned substrates,” Nat. Cell Biol.3(5), 466–472 (2001).
[CrossRef] [PubMed]

H. Y. Li, E. K. O. Ng, S. M. Y. Lee, M. Kotaka, S. K. W. Tsui, C. Y. Lee, K. P. Fung, and M. M. Y. Waye, “Protein-protein interaction of FHL3 with FHL2 and visualization of their interaction by green fluorescent proteins (GFP) two-fusion fluorescence resonance energy transfer (FRET),” J. Cell. Biochem.80(3), 293–303 (2001).
[CrossRef] [PubMed]

2000 (1)

H. Kano and W. Knoll, “A scanning microscope employing localized surface-plasmon-polaritons as a sensing probe,” Opt. Commun.182(1-3), 11–15 (2000).
[CrossRef]

1998 (3)

N. L. Perillo, M. E. Marcus, and L. G. Baum, “Galectins: versatile modulators of cell adhesion, cell proliferation, and cell death,” J. Mol. Med.76(6), 402–412 (1998).
[CrossRef] [PubMed]

M. E. Chicurel, C. S. Chen, and D. E. Ingber, “Cellular control lies in the balance of forces,” Curr. Opin. Cell Biol.10(2), 232–239 (1998).
[CrossRef] [PubMed]

C. Zhong, M. Chrzanowska-Wodnicka, J. Brown, A. Shaub, A. M. Belkin, and K. Burridge, “Rho-mediated contractility exposes a cryptic site in fibronectin and induces fibronectin matrix assembly,” J. Cell Biol.141(2), 539–551 (1998).
[CrossRef] [PubMed]

1996 (1)

B. A. McCool, J.-P. Pin, P. F. Brust, M. M. Harpold, and D. M. Lovinger, “Functional coupling of rat group II metabotropic glutamate receptors to an ω-conotoxin GVIA-sensitive calcium channel in human embryonic kidney 293 cells,” Mol. Pharmacol.50(4), 912–922 (1996).
[PubMed]

1994 (1)

C. E. H. Berger, R. P. H. Kooyman, and J. Greve, “Resolution in surface plasmon microscopy,” Rev. Sci. Instrum.65(9), 2829–2836 (1994).
[CrossRef]

1990 (1)

W. Hickel and W. Knoll, “Surface plasmon microscopy of lipid layers,” Thin Solid Films187(2), 349–356 (1990).
[CrossRef]

1988 (1)

B. Rothenhäusler and W. Knoll, “Surface-plasmon microscopy,” Nature332(6165), 615–617 (1988).
[CrossRef]

1978 (1)

J. Folkman and A. Moscona, “Role of cell shape in growth control,” Nature273(5661), 345–349 (1978).
[CrossRef] [PubMed]

Addadi, L.

U. S. Schwarz, N. Q. Balaban, D. Riveline, L. Addadi, A. Bershadsky, S. A. Safran, and B. Geiger, “Measurement of cellular force at focal adhesions using elastic micro-patterned substrates,” Mater. Sci. Eng. C23(3), 387–394 (2003).
[CrossRef]

N. Q. Balaban, U. S. Schwarz, D. Riveline, P. Goichberg, G. Tzur, I. Sabanay, D. Mahalu, S. Safran, A. Bershadsky, L. Addadi, and B. Geiger, “Force and focal adhesion assembly: a close relationship studied using elastic micropatterned substrates,” Nat. Cell Biol.3(5), 466–472 (2001).
[CrossRef] [PubMed]

Balaban, N. Q.

U. S. Schwarz, N. Q. Balaban, D. Riveline, L. Addadi, A. Bershadsky, S. A. Safran, and B. Geiger, “Measurement of cellular force at focal adhesions using elastic micro-patterned substrates,” Mater. Sci. Eng. C23(3), 387–394 (2003).
[CrossRef]

N. Q. Balaban, U. S. Schwarz, D. Riveline, P. Goichberg, G. Tzur, I. Sabanay, D. Mahalu, S. Safran, A. Bershadsky, L. Addadi, and B. Geiger, “Force and focal adhesion assembly: a close relationship studied using elastic micropatterned substrates,” Nat. Cell Biol.3(5), 466–472 (2001).
[CrossRef] [PubMed]

Baum, L. G.

N. L. Perillo, M. E. Marcus, and L. G. Baum, “Galectins: versatile modulators of cell adhesion, cell proliferation, and cell death,” J. Mol. Med.76(6), 402–412 (1998).
[CrossRef] [PubMed]

Belkin, A. M.

C. Zhong, M. Chrzanowska-Wodnicka, J. Brown, A. Shaub, A. M. Belkin, and K. Burridge, “Rho-mediated contractility exposes a cryptic site in fibronectin and induces fibronectin matrix assembly,” J. Cell Biol.141(2), 539–551 (1998).
[CrossRef] [PubMed]

Berger, C. E. H.

C. E. H. Berger, R. P. H. Kooyman, and J. Greve, “Resolution in surface plasmon microscopy,” Rev. Sci. Instrum.65(9), 2829–2836 (1994).
[CrossRef]

Bershadsky, A.

U. S. Schwarz, N. Q. Balaban, D. Riveline, L. Addadi, A. Bershadsky, S. A. Safran, and B. Geiger, “Measurement of cellular force at focal adhesions using elastic micro-patterned substrates,” Mater. Sci. Eng. C23(3), 387–394 (2003).
[CrossRef]

N. Q. Balaban, U. S. Schwarz, D. Riveline, P. Goichberg, G. Tzur, I. Sabanay, D. Mahalu, S. Safran, A. Bershadsky, L. Addadi, and B. Geiger, “Force and focal adhesion assembly: a close relationship studied using elastic micropatterned substrates,” Nat. Cell Biol.3(5), 466–472 (2001).
[CrossRef] [PubMed]

Bhadriraju, K.

A. W. Peterson, M. Halter, A. Tona, K. Bhadriraju, and A. L. Plant, “Surface plasmon resonance imaging of cells and surface-associated fibronectin,” BMC Cell Biol.10(1), 16 (2009).
[CrossRef] [PubMed]

Borisy, G.

A. J. Ridley, M. A. Schwartz, K. Burridge, R. A. Firtel, M. H. Ginsberg, G. Borisy, J. T. Parsons, and A. R. Horwitz, “Cell migration: integrating signals from front to back,” Science302(5651), 1704–1709 (2003).
[CrossRef] [PubMed]

Brown, J.

C. Zhong, M. Chrzanowska-Wodnicka, J. Brown, A. Shaub, A. M. Belkin, and K. Burridge, “Rho-mediated contractility exposes a cryptic site in fibronectin and induces fibronectin matrix assembly,” J. Cell Biol.141(2), 539–551 (1998).
[CrossRef] [PubMed]

Bruni, P.

L. Formigli, E. Meacci, C. Sassoli, F. Chellini, R. Giannini, F. Quercioli, B. Tiribilli, R. Squecco, P. Bruni, F. Francini, and S. Zecchi-Orlandini, “Sphingosine 1-phosphate induces cytoskeletal reorganization in C2C12 myoblasts: physiological relevance for stress fibres in the modulation of ion current through stretch-activated channels,” J. Cell Sci.118(6), 1161–1171 (2005).
[CrossRef] [PubMed]

Brust, P. F.

B. A. McCool, J.-P. Pin, P. F. Brust, M. M. Harpold, and D. M. Lovinger, “Functional coupling of rat group II metabotropic glutamate receptors to an ω-conotoxin GVIA-sensitive calcium channel in human embryonic kidney 293 cells,” Mol. Pharmacol.50(4), 912–922 (1996).
[PubMed]

Burridge, K.

A. J. Ridley, M. A. Schwartz, K. Burridge, R. A. Firtel, M. H. Ginsberg, G. Borisy, J. T. Parsons, and A. R. Horwitz, “Cell migration: integrating signals from front to back,” Science302(5651), 1704–1709 (2003).
[CrossRef] [PubMed]

C. Zhong, M. Chrzanowska-Wodnicka, J. Brown, A. Shaub, A. M. Belkin, and K. Burridge, “Rho-mediated contractility exposes a cryptic site in fibronectin and induces fibronectin matrix assembly,” J. Cell Biol.141(2), 539–551 (1998).
[CrossRef] [PubMed]

Chellini, F.

L. Formigli, E. Meacci, C. Sassoli, F. Chellini, R. Giannini, F. Quercioli, B. Tiribilli, R. Squecco, P. Bruni, F. Francini, and S. Zecchi-Orlandini, “Sphingosine 1-phosphate induces cytoskeletal reorganization in C2C12 myoblasts: physiological relevance for stress fibres in the modulation of ion current through stretch-activated channels,” J. Cell Sci.118(6), 1161–1171 (2005).
[CrossRef] [PubMed]

Chen, C. S.

M. E. Chicurel, C. S. Chen, and D. E. Ingber, “Cellular control lies in the balance of forces,” Curr. Opin. Cell Biol.10(2), 232–239 (1998).
[CrossRef] [PubMed]

Chicurel, M. E.

M. E. Chicurel, C. S. Chen, and D. E. Ingber, “Cellular control lies in the balance of forces,” Curr. Opin. Cell Biol.10(2), 232–239 (1998).
[CrossRef] [PubMed]

Chrzanowska-Wodnicka, M.

C. Zhong, M. Chrzanowska-Wodnicka, J. Brown, A. Shaub, A. M. Belkin, and K. Burridge, “Rho-mediated contractility exposes a cryptic site in fibronectin and induces fibronectin matrix assembly,” J. Cell Biol.141(2), 539–551 (1998).
[CrossRef] [PubMed]

Cukierman, E.

K. M. Yamada, R. Pankov, and E. Cukierman, “Dimensions and dynamics in integrin function,” Braz. J. Med. Biol. Res.36(8), 959–966 (2003).
[CrossRef] [PubMed]

Firtel, R. A.

A. J. Ridley, M. A. Schwartz, K. Burridge, R. A. Firtel, M. H. Ginsberg, G. Borisy, J. T. Parsons, and A. R. Horwitz, “Cell migration: integrating signals from front to back,” Science302(5651), 1704–1709 (2003).
[CrossRef] [PubMed]

Folkman, J.

J. Folkman and A. Moscona, “Role of cell shape in growth control,” Nature273(5661), 345–349 (1978).
[CrossRef] [PubMed]

Formigli, L.

L. Formigli, E. Meacci, C. Sassoli, F. Chellini, R. Giannini, F. Quercioli, B. Tiribilli, R. Squecco, P. Bruni, F. Francini, and S. Zecchi-Orlandini, “Sphingosine 1-phosphate induces cytoskeletal reorganization in C2C12 myoblasts: physiological relevance for stress fibres in the modulation of ion current through stretch-activated channels,” J. Cell Sci.118(6), 1161–1171 (2005).
[CrossRef] [PubMed]

Francini, F.

L. Formigli, E. Meacci, C. Sassoli, F. Chellini, R. Giannini, F. Quercioli, B. Tiribilli, R. Squecco, P. Bruni, F. Francini, and S. Zecchi-Orlandini, “Sphingosine 1-phosphate induces cytoskeletal reorganization in C2C12 myoblasts: physiological relevance for stress fibres in the modulation of ion current through stretch-activated channels,” J. Cell Sci.118(6), 1161–1171 (2005).
[CrossRef] [PubMed]

Fung, K. P.

H. Y. Li, E. K. O. Ng, S. M. Y. Lee, M. Kotaka, S. K. W. Tsui, C. Y. Lee, K. P. Fung, and M. M. Y. Waye, “Protein-protein interaction of FHL3 with FHL2 and visualization of their interaction by green fluorescent proteins (GFP) two-fusion fluorescence resonance energy transfer (FRET),” J. Cell. Biochem.80(3), 293–303 (2001).
[CrossRef] [PubMed]

Geiger, B.

O. Medalia and B. Geiger, “Frontiers of microscopy-based research into cell-matrix adhesions,” Curr. Opin. Cell Biol.22(5), 659–668 (2010).
[CrossRef] [PubMed]

U. S. Schwarz, N. Q. Balaban, D. Riveline, L. Addadi, A. Bershadsky, S. A. Safran, and B. Geiger, “Measurement of cellular force at focal adhesions using elastic micro-patterned substrates,” Mater. Sci. Eng. C23(3), 387–394 (2003).
[CrossRef]

N. Q. Balaban, U. S. Schwarz, D. Riveline, P. Goichberg, G. Tzur, I. Sabanay, D. Mahalu, S. Safran, A. Bershadsky, L. Addadi, and B. Geiger, “Force and focal adhesion assembly: a close relationship studied using elastic micropatterned substrates,” Nat. Cell Biol.3(5), 466–472 (2001).
[CrossRef] [PubMed]

Giannini, R.

L. Formigli, E. Meacci, C. Sassoli, F. Chellini, R. Giannini, F. Quercioli, B. Tiribilli, R. Squecco, P. Bruni, F. Francini, and S. Zecchi-Orlandini, “Sphingosine 1-phosphate induces cytoskeletal reorganization in C2C12 myoblasts: physiological relevance for stress fibres in the modulation of ion current through stretch-activated channels,” J. Cell Sci.118(6), 1161–1171 (2005).
[CrossRef] [PubMed]

Ginsberg, M. H.

A. J. Ridley, M. A. Schwartz, K. Burridge, R. A. Firtel, M. H. Ginsberg, G. Borisy, J. T. Parsons, and A. R. Horwitz, “Cell migration: integrating signals from front to back,” Science302(5651), 1704–1709 (2003).
[CrossRef] [PubMed]

Goichberg, P.

N. Q. Balaban, U. S. Schwarz, D. Riveline, P. Goichberg, G. Tzur, I. Sabanay, D. Mahalu, S. Safran, A. Bershadsky, L. Addadi, and B. Geiger, “Force and focal adhesion assembly: a close relationship studied using elastic micropatterned substrates,” Nat. Cell Biol.3(5), 466–472 (2001).
[CrossRef] [PubMed]

Greve, J.

C. E. H. Berger, R. P. H. Kooyman, and J. Greve, “Resolution in surface plasmon microscopy,” Rev. Sci. Instrum.65(9), 2829–2836 (1994).
[CrossRef]

Halter, M.

A. W. Peterson, M. Halter, A. Tona, K. Bhadriraju, and A. L. Plant, “Surface plasmon resonance imaging of cells and surface-associated fibronectin,” BMC Cell Biol.10(1), 16 (2009).
[CrossRef] [PubMed]

Harpold, M. M.

B. A. McCool, J.-P. Pin, P. F. Brust, M. M. Harpold, and D. M. Lovinger, “Functional coupling of rat group II metabotropic glutamate receptors to an ω-conotoxin GVIA-sensitive calcium channel in human embryonic kidney 293 cells,” Mol. Pharmacol.50(4), 912–922 (1996).
[PubMed]

Hickel, W.

W. Hickel and W. Knoll, “Surface plasmon microscopy of lipid layers,” Thin Solid Films187(2), 349–356 (1990).
[CrossRef]

Horiguchi, N.

Horwitz, A. R.

A. J. Ridley, M. A. Schwartz, K. Burridge, R. A. Firtel, M. H. Ginsberg, G. Borisy, J. T. Parsons, and A. R. Horwitz, “Cell migration: integrating signals from front to back,” Science302(5651), 1704–1709 (2003).
[CrossRef] [PubMed]

Ingber, D. E.

M. E. Chicurel, C. S. Chen, and D. E. Ingber, “Cellular control lies in the balance of forces,” Curr. Opin. Cell Biol.10(2), 232–239 (1998).
[CrossRef] [PubMed]

Kano, H.

Katanosaka, Y.

A. Yamada, Y. Katanosaka, S. Mohri, and K. Naruse, “A rapid microfluidic switching system for analysis at the single cellular level,” IEEE Trans. Nanobioscience8(4), 306–311 (2009).
[CrossRef] [PubMed]

Knoll, W.

H. Kano and W. Knoll, “A scanning microscope employing localized surface-plasmon-polaritons as a sensing probe,” Opt. Commun.182(1-3), 11–15 (2000).
[CrossRef]

W. Hickel and W. Knoll, “Surface plasmon microscopy of lipid layers,” Thin Solid Films187(2), 349–356 (1990).
[CrossRef]

B. Rothenhäusler and W. Knoll, “Surface-plasmon microscopy,” Nature332(6165), 615–617 (1988).
[CrossRef]

Kooyman, R. P. H.

C. E. H. Berger, R. P. H. Kooyman, and J. Greve, “Resolution in surface plasmon microscopy,” Rev. Sci. Instrum.65(9), 2829–2836 (1994).
[CrossRef]

Kotaka, M.

H. Y. Li, E. K. O. Ng, S. M. Y. Lee, M. Kotaka, S. K. W. Tsui, C. Y. Lee, K. P. Fung, and M. M. Y. Waye, “Protein-protein interaction of FHL3 with FHL2 and visualization of their interaction by green fluorescent proteins (GFP) two-fusion fluorescence resonance energy transfer (FRET),” J. Cell. Biochem.80(3), 293–303 (2001).
[CrossRef] [PubMed]

Lee, C. Y.

H. Y. Li, E. K. O. Ng, S. M. Y. Lee, M. Kotaka, S. K. W. Tsui, C. Y. Lee, K. P. Fung, and M. M. Y. Waye, “Protein-protein interaction of FHL3 with FHL2 and visualization of their interaction by green fluorescent proteins (GFP) two-fusion fluorescence resonance energy transfer (FRET),” J. Cell. Biochem.80(3), 293–303 (2001).
[CrossRef] [PubMed]

Lee, S. M. Y.

H. Y. Li, E. K. O. Ng, S. M. Y. Lee, M. Kotaka, S. K. W. Tsui, C. Y. Lee, K. P. Fung, and M. M. Y. Waye, “Protein-protein interaction of FHL3 with FHL2 and visualization of their interaction by green fluorescent proteins (GFP) two-fusion fluorescence resonance energy transfer (FRET),” J. Cell. Biochem.80(3), 293–303 (2001).
[CrossRef] [PubMed]

Li, H. Y.

H. Y. Li, E. K. O. Ng, S. M. Y. Lee, M. Kotaka, S. K. W. Tsui, C. Y. Lee, K. P. Fung, and M. M. Y. Waye, “Protein-protein interaction of FHL3 with FHL2 and visualization of their interaction by green fluorescent proteins (GFP) two-fusion fluorescence resonance energy transfer (FRET),” J. Cell. Biochem.80(3), 293–303 (2001).
[CrossRef] [PubMed]

Lovinger, D. M.

B. A. McCool, J.-P. Pin, P. F. Brust, M. M. Harpold, and D. M. Lovinger, “Functional coupling of rat group II metabotropic glutamate receptors to an ω-conotoxin GVIA-sensitive calcium channel in human embryonic kidney 293 cells,” Mol. Pharmacol.50(4), 912–922 (1996).
[PubMed]

Mahalu, D.

N. Q. Balaban, U. S. Schwarz, D. Riveline, P. Goichberg, G. Tzur, I. Sabanay, D. Mahalu, S. Safran, A. Bershadsky, L. Addadi, and B. Geiger, “Force and focal adhesion assembly: a close relationship studied using elastic micropatterned substrates,” Nat. Cell Biol.3(5), 466–472 (2001).
[CrossRef] [PubMed]

Marcus, M. E.

N. L. Perillo, M. E. Marcus, and L. G. Baum, “Galectins: versatile modulators of cell adhesion, cell proliferation, and cell death,” J. Mol. Med.76(6), 402–412 (1998).
[CrossRef] [PubMed]

McCool, B. A.

B. A. McCool, J.-P. Pin, P. F. Brust, M. M. Harpold, and D. M. Lovinger, “Functional coupling of rat group II metabotropic glutamate receptors to an ω-conotoxin GVIA-sensitive calcium channel in human embryonic kidney 293 cells,” Mol. Pharmacol.50(4), 912–922 (1996).
[PubMed]

Meacci, E.

L. Formigli, E. Meacci, C. Sassoli, F. Chellini, R. Giannini, F. Quercioli, B. Tiribilli, R. Squecco, P. Bruni, F. Francini, and S. Zecchi-Orlandini, “Sphingosine 1-phosphate induces cytoskeletal reorganization in C2C12 myoblasts: physiological relevance for stress fibres in the modulation of ion current through stretch-activated channels,” J. Cell Sci.118(6), 1161–1171 (2005).
[CrossRef] [PubMed]

Medalia, O.

O. Medalia and B. Geiger, “Frontiers of microscopy-based research into cell-matrix adhesions,” Curr. Opin. Cell Biol.22(5), 659–668 (2010).
[CrossRef] [PubMed]

Mohri, S.

A. Yamada, Y. Katanosaka, S. Mohri, and K. Naruse, “A rapid microfluidic switching system for analysis at the single cellular level,” IEEE Trans. Nanobioscience8(4), 306–311 (2009).
[CrossRef] [PubMed]

Morigaki, K.

Moscona, A.

J. Folkman and A. Moscona, “Role of cell shape in growth control,” Nature273(5661), 345–349 (1978).
[CrossRef] [PubMed]

Naruse, K.

A. Yamada, Y. Katanosaka, S. Mohri, and K. Naruse, “A rapid microfluidic switching system for analysis at the single cellular level,” IEEE Trans. Nanobioscience8(4), 306–311 (2009).
[CrossRef] [PubMed]

Ng, E. K. O.

H. Y. Li, E. K. O. Ng, S. M. Y. Lee, M. Kotaka, S. K. W. Tsui, C. Y. Lee, K. P. Fung, and M. M. Y. Waye, “Protein-protein interaction of FHL3 with FHL2 and visualization of their interaction by green fluorescent proteins (GFP) two-fusion fluorescence resonance energy transfer (FRET),” J. Cell. Biochem.80(3), 293–303 (2001).
[CrossRef] [PubMed]

Okazaki, T.

Pankov, R.

K. M. Yamada, R. Pankov, and E. Cukierman, “Dimensions and dynamics in integrin function,” Braz. J. Med. Biol. Res.36(8), 959–966 (2003).
[CrossRef] [PubMed]

Parsons, J. T.

A. J. Ridley, M. A. Schwartz, K. Burridge, R. A. Firtel, M. H. Ginsberg, G. Borisy, J. T. Parsons, and A. R. Horwitz, “Cell migration: integrating signals from front to back,” Science302(5651), 1704–1709 (2003).
[CrossRef] [PubMed]

Perillo, N. L.

N. L. Perillo, M. E. Marcus, and L. G. Baum, “Galectins: versatile modulators of cell adhesion, cell proliferation, and cell death,” J. Mol. Med.76(6), 402–412 (1998).
[CrossRef] [PubMed]

Peterson, A. W.

A. W. Peterson, M. Halter, A. Tona, K. Bhadriraju, and A. L. Plant, “Surface plasmon resonance imaging of cells and surface-associated fibronectin,” BMC Cell Biol.10(1), 16 (2009).
[CrossRef] [PubMed]

Pin, J.-P.

B. A. McCool, J.-P. Pin, P. F. Brust, M. M. Harpold, and D. M. Lovinger, “Functional coupling of rat group II metabotropic glutamate receptors to an ω-conotoxin GVIA-sensitive calcium channel in human embryonic kidney 293 cells,” Mol. Pharmacol.50(4), 912–922 (1996).
[PubMed]

Plant, A. L.

A. W. Peterson, M. Halter, A. Tona, K. Bhadriraju, and A. L. Plant, “Surface plasmon resonance imaging of cells and surface-associated fibronectin,” BMC Cell Biol.10(1), 16 (2009).
[CrossRef] [PubMed]

Quercioli, F.

L. Formigli, E. Meacci, C. Sassoli, F. Chellini, R. Giannini, F. Quercioli, B. Tiribilli, R. Squecco, P. Bruni, F. Francini, and S. Zecchi-Orlandini, “Sphingosine 1-phosphate induces cytoskeletal reorganization in C2C12 myoblasts: physiological relevance for stress fibres in the modulation of ion current through stretch-activated channels,” J. Cell Sci.118(6), 1161–1171 (2005).
[CrossRef] [PubMed]

Ridley, A. J.

A. J. Ridley, M. A. Schwartz, K. Burridge, R. A. Firtel, M. H. Ginsberg, G. Borisy, J. T. Parsons, and A. R. Horwitz, “Cell migration: integrating signals from front to back,” Science302(5651), 1704–1709 (2003).
[CrossRef] [PubMed]

Riveline, D.

U. S. Schwarz, N. Q. Balaban, D. Riveline, L. Addadi, A. Bershadsky, S. A. Safran, and B. Geiger, “Measurement of cellular force at focal adhesions using elastic micro-patterned substrates,” Mater. Sci. Eng. C23(3), 387–394 (2003).
[CrossRef]

N. Q. Balaban, U. S. Schwarz, D. Riveline, P. Goichberg, G. Tzur, I. Sabanay, D. Mahalu, S. Safran, A. Bershadsky, L. Addadi, and B. Geiger, “Force and focal adhesion assembly: a close relationship studied using elastic micropatterned substrates,” Nat. Cell Biol.3(5), 466–472 (2001).
[CrossRef] [PubMed]

Rothenhäusler, B.

B. Rothenhäusler and W. Knoll, “Surface-plasmon microscopy,” Nature332(6165), 615–617 (1988).
[CrossRef]

Ryosuke, M.

Sabanay, I.

N. Q. Balaban, U. S. Schwarz, D. Riveline, P. Goichberg, G. Tzur, I. Sabanay, D. Mahalu, S. Safran, A. Bershadsky, L. Addadi, and B. Geiger, “Force and focal adhesion assembly: a close relationship studied using elastic micropatterned substrates,” Nat. Cell Biol.3(5), 466–472 (2001).
[CrossRef] [PubMed]

Safran, S.

N. Q. Balaban, U. S. Schwarz, D. Riveline, P. Goichberg, G. Tzur, I. Sabanay, D. Mahalu, S. Safran, A. Bershadsky, L. Addadi, and B. Geiger, “Force and focal adhesion assembly: a close relationship studied using elastic micropatterned substrates,” Nat. Cell Biol.3(5), 466–472 (2001).
[CrossRef] [PubMed]

Safran, S. A.

U. S. Schwarz, N. Q. Balaban, D. Riveline, L. Addadi, A. Bershadsky, S. A. Safran, and B. Geiger, “Measurement of cellular force at focal adhesions using elastic micro-patterned substrates,” Mater. Sci. Eng. C23(3), 387–394 (2003).
[CrossRef]

Sassoli, C.

L. Formigli, E. Meacci, C. Sassoli, F. Chellini, R. Giannini, F. Quercioli, B. Tiribilli, R. Squecco, P. Bruni, F. Francini, and S. Zecchi-Orlandini, “Sphingosine 1-phosphate induces cytoskeletal reorganization in C2C12 myoblasts: physiological relevance for stress fibres in the modulation of ion current through stretch-activated channels,” J. Cell Sci.118(6), 1161–1171 (2005).
[CrossRef] [PubMed]

Schwartz, M. A.

A. J. Ridley, M. A. Schwartz, K. Burridge, R. A. Firtel, M. H. Ginsberg, G. Borisy, J. T. Parsons, and A. R. Horwitz, “Cell migration: integrating signals from front to back,” Science302(5651), 1704–1709 (2003).
[CrossRef] [PubMed]

Schwarz, U. S.

U. S. Schwarz, N. Q. Balaban, D. Riveline, L. Addadi, A. Bershadsky, S. A. Safran, and B. Geiger, “Measurement of cellular force at focal adhesions using elastic micro-patterned substrates,” Mater. Sci. Eng. C23(3), 387–394 (2003).
[CrossRef]

N. Q. Balaban, U. S. Schwarz, D. Riveline, P. Goichberg, G. Tzur, I. Sabanay, D. Mahalu, S. Safran, A. Bershadsky, L. Addadi, and B. Geiger, “Force and focal adhesion assembly: a close relationship studied using elastic micropatterned substrates,” Nat. Cell Biol.3(5), 466–472 (2001).
[CrossRef] [PubMed]

Shaub, A.

C. Zhong, M. Chrzanowska-Wodnicka, J. Brown, A. Shaub, A. M. Belkin, and K. Burridge, “Rho-mediated contractility exposes a cryptic site in fibronectin and induces fibronectin matrix assembly,” J. Cell Biol.141(2), 539–551 (1998).
[CrossRef] [PubMed]

Squecco, R.

L. Formigli, E. Meacci, C. Sassoli, F. Chellini, R. Giannini, F. Quercioli, B. Tiribilli, R. Squecco, P. Bruni, F. Francini, and S. Zecchi-Orlandini, “Sphingosine 1-phosphate induces cytoskeletal reorganization in C2C12 myoblasts: physiological relevance for stress fibres in the modulation of ion current through stretch-activated channels,” J. Cell Sci.118(6), 1161–1171 (2005).
[CrossRef] [PubMed]

Terakado, G.

Tiribilli, B.

L. Formigli, E. Meacci, C. Sassoli, F. Chellini, R. Giannini, F. Quercioli, B. Tiribilli, R. Squecco, P. Bruni, F. Francini, and S. Zecchi-Orlandini, “Sphingosine 1-phosphate induces cytoskeletal reorganization in C2C12 myoblasts: physiological relevance for stress fibres in the modulation of ion current through stretch-activated channels,” J. Cell Sci.118(6), 1161–1171 (2005).
[CrossRef] [PubMed]

Tona, A.

A. W. Peterson, M. Halter, A. Tona, K. Bhadriraju, and A. L. Plant, “Surface plasmon resonance imaging of cells and surface-associated fibronectin,” BMC Cell Biol.10(1), 16 (2009).
[CrossRef] [PubMed]

Tsui, S. K. W.

H. Y. Li, E. K. O. Ng, S. M. Y. Lee, M. Kotaka, S. K. W. Tsui, C. Y. Lee, K. P. Fung, and M. M. Y. Waye, “Protein-protein interaction of FHL3 with FHL2 and visualization of their interaction by green fluorescent proteins (GFP) two-fusion fluorescence resonance energy transfer (FRET),” J. Cell. Biochem.80(3), 293–303 (2001).
[CrossRef] [PubMed]

Tzur, G.

N. Q. Balaban, U. S. Schwarz, D. Riveline, P. Goichberg, G. Tzur, I. Sabanay, D. Mahalu, S. Safran, A. Bershadsky, L. Addadi, and B. Geiger, “Force and focal adhesion assembly: a close relationship studied using elastic micropatterned substrates,” Nat. Cell Biol.3(5), 466–472 (2001).
[CrossRef] [PubMed]

Watanabe, K.

Waye, M. M. Y.

H. Y. Li, E. K. O. Ng, S. M. Y. Lee, M. Kotaka, S. K. W. Tsui, C. Y. Lee, K. P. Fung, and M. M. Y. Waye, “Protein-protein interaction of FHL3 with FHL2 and visualization of their interaction by green fluorescent proteins (GFP) two-fusion fluorescence resonance energy transfer (FRET),” J. Cell. Biochem.80(3), 293–303 (2001).
[CrossRef] [PubMed]

Yamada, A.

A. Yamada, Y. Katanosaka, S. Mohri, and K. Naruse, “A rapid microfluidic switching system for analysis at the single cellular level,” IEEE Trans. Nanobioscience8(4), 306–311 (2009).
[CrossRef] [PubMed]

Yamada, K. M.

K. M. Yamada, R. Pankov, and E. Cukierman, “Dimensions and dynamics in integrin function,” Braz. J. Med. Biol. Res.36(8), 959–966 (2003).
[CrossRef] [PubMed]

Zecchi-Orlandini, S.

L. Formigli, E. Meacci, C. Sassoli, F. Chellini, R. Giannini, F. Quercioli, B. Tiribilli, R. Squecco, P. Bruni, F. Francini, and S. Zecchi-Orlandini, “Sphingosine 1-phosphate induces cytoskeletal reorganization in C2C12 myoblasts: physiological relevance for stress fibres in the modulation of ion current through stretch-activated channels,” J. Cell Sci.118(6), 1161–1171 (2005).
[CrossRef] [PubMed]

Zhong, C.

C. Zhong, M. Chrzanowska-Wodnicka, J. Brown, A. Shaub, A. M. Belkin, and K. Burridge, “Rho-mediated contractility exposes a cryptic site in fibronectin and induces fibronectin matrix assembly,” J. Cell Biol.141(2), 539–551 (1998).
[CrossRef] [PubMed]

Appl. Opt. (2)

BMC Cell Biol. (1)

A. W. Peterson, M. Halter, A. Tona, K. Bhadriraju, and A. L. Plant, “Surface plasmon resonance imaging of cells and surface-associated fibronectin,” BMC Cell Biol.10(1), 16 (2009).
[CrossRef] [PubMed]

Braz. J. Med. Biol. Res. (1)

K. M. Yamada, R. Pankov, and E. Cukierman, “Dimensions and dynamics in integrin function,” Braz. J. Med. Biol. Res.36(8), 959–966 (2003).
[CrossRef] [PubMed]

Curr. Opin. Cell Biol. (2)

O. Medalia and B. Geiger, “Frontiers of microscopy-based research into cell-matrix adhesions,” Curr. Opin. Cell Biol.22(5), 659–668 (2010).
[CrossRef] [PubMed]

M. E. Chicurel, C. S. Chen, and D. E. Ingber, “Cellular control lies in the balance of forces,” Curr. Opin. Cell Biol.10(2), 232–239 (1998).
[CrossRef] [PubMed]

IEEE Trans. Nanobioscience (1)

A. Yamada, Y. Katanosaka, S. Mohri, and K. Naruse, “A rapid microfluidic switching system for analysis at the single cellular level,” IEEE Trans. Nanobioscience8(4), 306–311 (2009).
[CrossRef] [PubMed]

J. Cell Biol. (1)

C. Zhong, M. Chrzanowska-Wodnicka, J. Brown, A. Shaub, A. M. Belkin, and K. Burridge, “Rho-mediated contractility exposes a cryptic site in fibronectin and induces fibronectin matrix assembly,” J. Cell Biol.141(2), 539–551 (1998).
[CrossRef] [PubMed]

J. Cell Sci. (1)

L. Formigli, E. Meacci, C. Sassoli, F. Chellini, R. Giannini, F. Quercioli, B. Tiribilli, R. Squecco, P. Bruni, F. Francini, and S. Zecchi-Orlandini, “Sphingosine 1-phosphate induces cytoskeletal reorganization in C2C12 myoblasts: physiological relevance for stress fibres in the modulation of ion current through stretch-activated channels,” J. Cell Sci.118(6), 1161–1171 (2005).
[CrossRef] [PubMed]

J. Cell. Biochem. (1)

H. Y. Li, E. K. O. Ng, S. M. Y. Lee, M. Kotaka, S. K. W. Tsui, C. Y. Lee, K. P. Fung, and M. M. Y. Waye, “Protein-protein interaction of FHL3 with FHL2 and visualization of their interaction by green fluorescent proteins (GFP) two-fusion fluorescence resonance energy transfer (FRET),” J. Cell. Biochem.80(3), 293–303 (2001).
[CrossRef] [PubMed]

J. Mol. Med. (1)

N. L. Perillo, M. E. Marcus, and L. G. Baum, “Galectins: versatile modulators of cell adhesion, cell proliferation, and cell death,” J. Mol. Med.76(6), 402–412 (1998).
[CrossRef] [PubMed]

Mater. Sci. Eng. C (1)

U. S. Schwarz, N. Q. Balaban, D. Riveline, L. Addadi, A. Bershadsky, S. A. Safran, and B. Geiger, “Measurement of cellular force at focal adhesions using elastic micro-patterned substrates,” Mater. Sci. Eng. C23(3), 387–394 (2003).
[CrossRef]

Mol. Pharmacol. (1)

B. A. McCool, J.-P. Pin, P. F. Brust, M. M. Harpold, and D. M. Lovinger, “Functional coupling of rat group II metabotropic glutamate receptors to an ω-conotoxin GVIA-sensitive calcium channel in human embryonic kidney 293 cells,” Mol. Pharmacol.50(4), 912–922 (1996).
[PubMed]

Nat. Cell Biol. (1)

N. Q. Balaban, U. S. Schwarz, D. Riveline, P. Goichberg, G. Tzur, I. Sabanay, D. Mahalu, S. Safran, A. Bershadsky, L. Addadi, and B. Geiger, “Force and focal adhesion assembly: a close relationship studied using elastic micropatterned substrates,” Nat. Cell Biol.3(5), 466–472 (2001).
[CrossRef] [PubMed]

Nature (2)

J. Folkman and A. Moscona, “Role of cell shape in growth control,” Nature273(5661), 345–349 (1978).
[CrossRef] [PubMed]

B. Rothenhäusler and W. Knoll, “Surface-plasmon microscopy,” Nature332(6165), 615–617 (1988).
[CrossRef]

Opt. Commun. (1)

H. Kano and W. Knoll, “A scanning microscope employing localized surface-plasmon-polaritons as a sensing probe,” Opt. Commun.182(1-3), 11–15 (2000).
[CrossRef]

Rev. Sci. Instrum. (1)

C. E. H. Berger, R. P. H. Kooyman, and J. Greve, “Resolution in surface plasmon microscopy,” Rev. Sci. Instrum.65(9), 2829–2836 (1994).
[CrossRef]

Science (1)

A. J. Ridley, M. A. Schwartz, K. Burridge, R. A. Firtel, M. H. Ginsberg, G. Borisy, J. T. Parsons, and A. R. Horwitz, “Cell migration: integrating signals from front to back,” Science302(5651), 1704–1709 (2003).
[CrossRef] [PubMed]

Thin Solid Films (1)

W. Hickel and W. Knoll, “Surface plasmon microscopy of lipid layers,” Thin Solid Films187(2), 349–356 (1990).
[CrossRef]

Other (3)

H. Raether, Surface Plasmons on Smooth and Rough Surfaces and on Gratings (Springer, 1988).

F. Kawata, R. Miyazaki, G. Terakado, K. Watanabe, and H. Kano, “Scanning and non-scanning surface plasmon microscopy of refractive index distribution on a metal surface,” in Focus on Microscopy (Focus on Microscopy Society, 2011), abstract 269.

J. Homola, Surface Plasmon Resonance Based Sensors (Springer, 2006).

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Figures (6)

Fig. 1
Fig. 1

The optical systems of (a) the lens imaging surface plasmon microscope (LISPM) and (b) the scanning localized surface plasmon microscope (SLSPM). The optical paths can be switched using the flipper mirrors FM1 and FM2.

Fig. 2
Fig. 2

(a) Reflected light intensity distribution in the pupil plane. (b) Magnified image of squared area shown in (a). The pixels that overlapped with a ring (white line) were highlighted using semitransparent white shading.

Fig. 3
Fig. 3

LISPM image of latex particles with a diameter of 1.053 µm. The arrow A shows the propagation direction of surface plamons.

Fig. 4
Fig. 4

SLSPM image of latex particles with a diameter of 1.053 µm. The observed area corresponds to the framed area shown in Fig. 3.

Fig. 5
Fig. 5

Observed LISPM image of the underlying supports of a mouse muscle cell. The white arrows indicate the C2C12 cell and the cellular divergence point. The framed area is the section observed by SLSPM as shown in Fig. 6.

Fig. 6
Fig. 6

SLSPM image observed at divergence point of the C2C12 cell.

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