Integrin Catch Bond Kinetics Mediate Mechanosensing during Cell Spreading
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The RGD motif is a cell adhesion sequence that binds to integrins, a receptor family for extracellular matrix proteins. We previously reported that the RGDX1X2 sequence, where X1X2 is VF or NY, is required for integrin αvβ5-mediated cell adhesion. However, the importance and applications of the X1X2 combinations and their surrounding sequences of integrin αvβ5-binding RGDX1X2-containing peptides have not been comprehensively elucidated. Therefore, we aimed to identify an RGD-containing peptide with enhanced integrin αvβ5 binding activity. We synthesized various peptides based on the RGDVF and RGDNY peptides to optimize the N-terminal, C-terminal, and X1X2 combinations of the RGDX1X2 sequence. These peptides were immobilized on maleimide-functionalized bovine serum albumin-coated plates via a thiol-maleimide reaction, and cell adhesion was evaluated using HeLa cells and human dermal fibroblasts. Consequently, CPPP-RGDTF and CPPP-RGDTFI were identified as highly active peptides for integrin αvβ5-mediated cell adhesion. CPPP-RGDTF and CPPP-RGDTFI are expected to serve as cell adhesion molecules for developing culture substrates and biomaterials. Furthermore, these findings provide important novel insights into the interaction between the RGD motifs and integrins.
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Abstract An erratum for this article has been published in Journal of Pathology; 201(4): 632–641. Cell adhesion is indispensable for embryonic development and for proper tissue function. In metazoans, integrins are the major adhesion receptors that connect cells to components of the extracellular matrix. Integrins are implicated in assembly of extracellular matrices, cell adhesion and migration on extracellular matrices, and in vertebrates (in which the integrin family has expanded) they can also mediate cell–cell adhesion. Furthermore, integrin‐mediated adhesion can modulate many different signal transduction cascades and support cell survival, proliferation, and influence the expression of differentiation‐related genes. In this review we briefly explain how integrins can affect so many different aspects of cell behavior and discuss evidence for roles of integrins in tissue development, function, and disease. Copyright © 2003 John Wiley & Sons, Ltd.
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Abstract The original article to which this Erratum refers was published in Journal of Pathology; 200(4): 471–480. It has been brought to the attention of the publishers that there were errors on pages 476, 477 and 480 of the orginally published manuscript. These errors have now been rectified, and to facilitate greater legibility for our readers, the corrected article has been reproduced in its entirety. Cell adhesion is indispensable for embryonic development and for proper tissue function. In metazoans, integrins are the major adhesion receptors that connect cells to components of the extracellular matrix. Integrins are implicated in assembly of extracellular matrices, cell adhesion and migration on extracellular matrices, and in vertebrates (in which the integrin family has expanded) they can also mediate cell–cell adhesion. Furthermore, integrin‐mediated adhesion can modulate many different signal transduction cascades and support cell survival, proliferation, and influence the expression of differentiation‐related genes. In this review we briefly explain how integrins can affect so many different aspects of cell behavior and discuss evidence for roles of integrins in tissue development, function, and disease. Copyright © 2003 John Wiley & Sons, Ltd.
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Integrins and syndecans mediate cell adhesion to extracellular matrix and their synergistic cooperation is implicated in cell adhesion processes. We previously identified two active peptides, AG73 and EF1, from the laminin α1 chain LG4 module, that promote cell attachment through syndecan‐ and α2β1 integrin‐binding, respectively. Here, we examined time‐dependent cell attachment on the mixed peptides AG73/EF1. The AG73/EF1 promoted stronger and more rapid cell attachment, spreading, FAK phosphorylation that reached a maximum at 20 min than that on AG73 (40 min) or EF1 (90 min) supplied singly. Thus, the syndecan‐ and α2β1 integrin‐binding peptides synergistically affect cells and accelerate cell adhesion.
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▪ Abstract Proteins that contain the Arg-Gly-Asp (RGD) attachment site, together with the integrins that serve as receptors for them, constitute a major recognition system for cell adhesion. The RGD sequence is the cell attachment site of a large number of adhesive extracellular matrix, blood, and cell surface proteins, and nearly half of the over 20 known integrins recognize this sequence in their adhesion protein ligands. Some other integrins bind to related sequences in their ligands. The integrin-binding activity of adhesion proteins can be reproduced by short synthetic peptides containing the RGD sequence. Such peptides promote cell adhesion when insolubilized onto a surface, and inhibit it when presented to cells in solution. Reagents that bind selectively to only one or a few of the RGD-directed integrins can be designed by cyclizing peptides with selected sequences around the RGD and by synthesizing RGD mimics. As the integrin-mediated cell attachment influences and regulates cell migration, growth, differentiation, and apoptosis, the RGD peptides and mimics can be used to probe integrin functions in various biological systems. Drug design based on the RGD structure may provide new treatments for diseases such as thrombosis, osteoporosis, and cancer.
RGD motif
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The integrin family represents the largest group of cell surface proteins that mediate cell adhesion in humans [1,2]. Adhesion is of fundamental importance to a cell as it provides anchorage, cues for migration and a signal for growth and differentiation. There are two different types of cell adhesion: cell‐extracellular matrix adhesion and cell‐cell adhesion. Integrins appear to be the major receptors by which cells attach to extracellular matrices. In addition, some integrins also mediate important cell‐cell adhesion events. The term ‘integrin’ was coined in order to signify the presumed role of these proteins in integrating the intracellular cytoskeleton with the extracellular matrix.
Intercellular adhesion molecule
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Objective:The adhesion of cells to cells and cells to stroma play very important role in the cell-cell information exchanges.Methods:The cell adhesion assay based on the 3 H-TdR incorporation assay was introduced. Firstly, coated cells were cultured to confluence in 96 well plate. After incubated with 3 H-TdR for 6h, the isotope labeled cells were added into plate wells and incubated for another 4 h. Then the un-adhered cells were removed by gently washing. The cpm was counted after cell harvest.Results:The cell adhesion assay based on the 3 H-TdR incorporation assay was very sensitive in the detection of cell adhesion. It could reflect the relative of cell to cell adhesion.Conclusion:The cell adhesion assay based on the 3 H-TdR incorporation assay is an useful method in the detection of cell to cell adhesion.
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