Integrin and glycocalyx mediated contributions to cell adhesion identified by single cell force spectroscopy

被引:16
作者
Boettiger, D. [1 ,2 ,3 ,4 ]
Wehrle-Haller, B. [1 ]
机构
[1] Univ Geneva, Dept Physiol & Metab, Geneva, Switzerland
[2] Univ Penn, Dept Microbiol, Philadelphia, PA 19104 USA
[3] Univ Penn, Dept Pharmacol, Philadelphia, PA 19104 USA
[4] Univ Penn, Inst Med & Engn, Philadelphia, PA 19104 USA
关键词
FIBRONECTIN RECEPTOR; QUANTITATIVE MEASUREMENTS; FOCAL CONTACTS; OUTSIDE-IN; DYNAMICS; ALPHA-V-BETA-3; TRANSFORMATION; TRANSMISSION; PROTRUSION; MIGRATION;
D O I
10.1088/0953-8984/22/19/194101
中图分类号
O469 [凝聚态物理学];
学科分类号
070205 ;
摘要
The measurement of cell adhesion using single cell force spectroscopy methods was compared with earlier methods for measuring cell adhesion. This comparison provided a means and rationale for separating components of the measurement retract curve that were due to interactions between the substrate and the glycocalyx, and interactions that were due to cell surface integrins binding to a substrate-bound ligand. The glycocalyx adhesion was characterized by multiple jumps with dispersed jump sizes that extended from 5 to 30 mu m from the origin. The integrin mediated adhesion was represented by the F-max (maximum detachment force), was generally within the first 5 mu m and commonly detached with a single rupture cascade. The integrin peak (F-max) increases with time and the rate of increase shows large cell to cell variability with a peak similar to 50 nN s(-1) and an average rate of increase of 75 pN s(-1). This is a measure of the rate of increase in the number of adhesive integrin-ligand bonds/cell as a function of contact time.
引用
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页数:11
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共 66 条
[1]  
Alberts B., 2002, The shape and structure of proteins, Vfourth, DOI 10.1093/aob/mcg023
[2]   β Integrin Tyrosine Phosphorylation Is a Conserved Mechanism for Regulating Talin-induced Integrin Activation [J].
Anthis, Nicholas J. ;
Haling, Jacob R. ;
Oxley, Camilla L. ;
Memo, Massimiliano ;
Wegener, Kate L. ;
Lim, Chinten J. ;
Ginsberg, Mark H. ;
Campbell, Iain D. .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2009, 284 (52) :36700-36710
[3]   Marching at the front and dragging behind:: differential α-Vβ3-integrin turnover regulates focal adhesion behavior [J].
Ballestrem, C ;
Hinz, B ;
Imhof, BA ;
Wehrle-Haller, B .
JOURNAL OF CELL BIOLOGY, 2001, 155 (07) :1319-1332
[4]   Discrete interactions in cell adhesion measured by single-molecule force spectroscopy [J].
Benoit, M ;
Gabriel, D ;
Gerisch, G ;
Gaub, HE .
NATURE CELL BIOLOGY, 2000, 2 (06) :313-317
[5]   Distinct ligand-binding modes for integrin αvβ3-mediated adhesion to fibronectin versus vitronectin [J].
Boettiger, D ;
Lynch, L ;
Blystone, S ;
Huber, F .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2001, 276 (34) :31684-31690
[6]   Quantitative measurements of integrin-mediated adhesion to extracellular matrix [J].
Boettiger, David .
INTEGRINS, 2007, 426 :1-+
[7]   Rho and Rac take center stage [J].
Burridge, K ;
Wennerberg, K .
CELL, 2004, 116 (02) :167-179
[8]   Focal adhesions, contractility, and signaling [J].
Burridge, K ;
ChrzanowskaWodnicka, M .
ANNUAL REVIEW OF CELL AND DEVELOPMENTAL BIOLOGY, 1996, 12 :463-518
[9]   Cytoskeletal coherence requires myosin-IIA contractility [J].
Cai, Yunfei ;
Rossier, Olivier ;
Gauthier, Nils C. ;
Biais, Nicolas ;
Fardin, Marc-Antoine ;
Zhang, Xian ;
Miller, Lawrence W. ;
Ladoux, Benoit ;
Cornish, Virginia W. ;
Sheetz, Michael P. .
JOURNAL OF CELL SCIENCE, 2010, 123 (03) :413-423
[10]   Competition for talin results in trans-dominant inhibition of integrin activation [J].
Calderwood, DA ;
Tai, V ;
Di Paolo, G ;
De Camilli, P ;
Ginsberg, MH .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2004, 279 (28) :28889-28895