New Perspectives in Cell Adhesion: RGD and Integrins

Ruoslahti, Erkki, Pierschbacher, Michael D.·1987·Science

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Abstract

Rapid progress has been made in the understanding of the molecular interactions that result in cell adhesion. Many adhesive proteins present in extracellular matrices and in the blood contain the tripeptide arginine-glycine-aspartic acid (RGD) as their cell recognition site. These proteins include fibronectin, vitronectin, osteopontin, collagens, thrombospondin, fibrinogen, and von Willebrand factor. The RGD sequences of each of the adhesive proteins are recognized by at least one member of a family of structurally related receptors, integrins, which are heterodimeric proteins with two membrane-spanning subunits. Some of these receptors bind to the RGD sequence of a single adhesion protein only, whereas others recognize groups of them. The conformation of the RGD sequence in the individual proteins may be critical to this recognition specificity. On the cytoplasmic side of the plasma membrane, the receptors connect the extracellular matrix to the cytoskeleton. More than ten proved or suspected RGD-containing adhesion-promoting proteins have already been identified, and the integrin family includes at least as many receptors recognizing these proteins. Together, the adhesion proteins and their receptors constitute a versatile recognition system providing cells with anchorage, traction for migration, and signals for polarity, position, differentiation, and possibly growth.

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Holohan, C., Van Schaeybroeck, S., Longley, D. B., & Johnston, P. G. (2013) · Nature Reviews Cancer · doi:10.1038/nrc3599 · Cited by 4,681
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Giancotti, F. G., & Ruoslahti, E. (1999) · Science · doi:10.1126/science.285.5430.1028 · Cited by 3,869
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Ruoslahti, E. (1996) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.12.1.697 · Cited by 3,191
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Kloxin, A. M., Kasko, A. M., Salinas, C. N., & Anseth, K. S. (2009) · Science · doi:10.1126/science.1169494 · Cited by 1,748
Bioactive modification of poly (ethylene glycol) hydrogels for tissue engineering
Zhu, J. (2010) · Biomaterials · doi:10.1016/j.biomaterials.2010.02.044 · Cited by 1,457
Physical approaches to biomaterial design
Mitragotri, S., & Lahann, J. (2009) · Nature Materials · doi:10.1038/nmat2344 · Cited by 1,445
Advancing biomaterials of human origin for tissue engineering
Chen, F.-M., & Liu, X. (2016) · Progress in Polymer Science · doi:10.1016/j.progpolymsci.2015.02.004 · Cited by 1,158
Surface chemistry modulates fibronectin conformation and directs integrin binding and specificity to control cell adhesion
Keselowsky, B. G., Collard, D. M., & García, A. J. (2003) · Journal of Biomedical Materials Research Part A · doi:10.1002/jbm.a.10537 · Cited by 949
Molecular mechanisms of glioma invasiveness: the role of proteases
Rao, J. S. (2003) · Nature Reviews Cancer · doi:10.1038/nrc1121 · Cited by 847
Fibrin structure and wound healing
LAURENS, N., KOOLWIJK, P., & DE MAAT, M. P. M. (2006) · Journal of Thrombosis and Haemostasis · doi:10.1111/j.1538-7836.2006.01861.x · Cited by 724
Transforming Growth Factor‐β: Major Role in Regulation of Extracellular Matrix
ROBERTS, A. B., HEINE, U. I., FLANDERS, K. C., & SPORN, M. B. (1990) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1990.tb17931.x · Cited by 696
Atrp in the design of functional materials for biomedical applications
Siegwart, D. J., Oh, J. K., & Matyjaszewski, K. (2012) · Progress in Polymer Science · doi:10.1016/j.progpolymsci.2011.08.001 · Cited by 613
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Ross, F. P., Chappel, J., Alvarez, J. I., Sander, D., Butler, W. T., Farach-Carson, M. C., Mintz, K. A., Robey, P. G., Teitelbaum, S. L., & Cheresh, D. A. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)98430-9 · Cited by 537
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Cesarz, Z., & Tamama, K. (2016) · Stem Cells International · doi:10.1155/2016/9176357 · Cited by 475
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Wylie, R. G., Ahsan, S., Aizawa, Y., Maxwell, K. L., Morshead, C. M., & Shoichet, M. S. (2011) · Nature Materials · doi:10.1038/nmat3101 · Cited by 480
A β 3 Integrin Mutation Abolishes Ligand Binding and Alters Divalent Cation-Dependent Conformation
Loftus, J. C., O'Toole, T. E., Plow, E. F., Glass, A., Frelinger, A. L., & Ginsberg, M. H. (1990) · Science · doi:10.1126/science.2392682 · Cited by 401
The influence of the microenvironment on the malignant phenotype
Park, C. C., Bissell, M. J., & Barcellos-Hoff, M. H. (2000) · Molecular Medicine Today · doi:10.1016/s1357-4310(00)01756-1 · Cited by 398
Selection of peptides binding to the alpha 5 beta 1 integrin from phage display library.
Koivunen, E., Gay, D. A., & Ruoslahti, E. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(20)80715-7 · Cited by 344
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Adams, R. A., Bauer, J., Flick, M. J., Sikorski, S. L., Nuriel, T., Lassmann, H., Degen, J. L., & Akassoglou, K. (2007) · The Journal of Experimental Medicine · doi:10.1084/jem.20061931 · Cited by 335
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Chen, Y., Yang, J., Fu, S., & Wu, J. (2020) · International Journal of Nanomedicine · doi:10.2147/ijn.s272902 · Cited by 319
Vascular endothelial cell adhesion and spreading promoted by the peptide REDV of the IIICS region of plasma fibronectin is mediated by integrin alpha 4 beta 1.
Massia, S. P., & Hubbell, J. A. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)49672-5 · Cited by 287
Regulation of Cell Adhesion Receptors by Transforming Growth Factor-β
Ignotz, R. A., Heino, J., & Massagué, J. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)31270-x · Cited by 269
Substrates for cardiovascular tissue engineering
Bouten, C. V. C., Dankers, P. Y. W., Driessen-Mol, A., Pedron, S., Brizard, A. M. A., & Baaijens, F. P. T. (2011) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2011.01.007 · Cited by 261
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Ito, M., Yamashita, T., Tsuzuki, H., Takeda, N., & Sakae, K. (2004) · Journal of General Virology · doi:10.1099/vir.0.19456-0 · Cited by 257
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Munarin, F., Guerreiro, S. G., Grellier, M. A., Tanzi, M. C., Barbosa, M. A., Petrini, P., & Granja, P. L. (2011) · Biomacromolecules · doi:10.1021/bm101110x · Cited by 242
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Elangbam, C. S., Qualls, C. W., & Dahlgren, R. R. (1997) · Veterinary Pathology · doi:10.1177/030098589703400113 · Cited by 215
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Peltonen, J., Larjava, H., Jaakkola, S., Gralnick, H., Akiyama, S. K., Yamada, S. S., Yamada, K. M., & Uitto, J. (1989) · Journal of Clinical Investigation · doi:10.1172/jci114379 · Cited by 220
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Kireeva, M. L., Lam, S. C.-T., & Lau, L. F. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.5.3090 · Cited by 203
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Sunderland, C. J., Steiert, M., Talmadge, J. E., Derfus, A. M., & Barry, S. E. (2006) · Drug Development Research · doi:10.1002/ddr.20069 · Cited by 200
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Nickel, J., Ten Dijke, P., & Mueller, T. D. (2018) · Acta Biochimica et Biophysica Sinica · doi:10.1093/abbs/gmx126 · Cited by 198
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Nam, J.-M., Onodera, Y., Bissell, M. J., & Park, C. C. (2010) · Cancer Research · doi:10.1158/0008-5472.can-09-2319 · Cited by 196
Surface strategies for control of neuronal cell adhesion: A review
Roach, P., Parker, T., Gadegaard, N., & Alexander, M. R. (2010) · Surface Science Reports · doi:10.1016/j.surfrep.2010.07.001 · Cited by 180
Vitronectin receptor has a role in bone resorption but does not mediate tight sealing zone attachment of osteoclasts to the bone surface.
Lakkakorpi, P. T., Horton, M. A., Helfrich, M. H., Karhukorpi, E. K., & Väänänen, H. K. (1991) · The Journal of cell biology · doi:10.1083/jcb.115.4.1179 · Cited by 168
Arg-Gly-Asp-Ser-Selective Adhesion and the Stabilization of Long-Term Potentiation: Pharmacological Studies and the Characterization of a Candidate Matrix Receptor
Bahr, B. A., Staubli, U., Xiao, P., Chun, D., Ji, Z.-X., Esteban, E. T., & Lynch, G. (1997) · The Journal of Neuroscience · doi:10.1523/jneurosci.17-04-01320.1997 · Cited by 165
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Expression of intercellular adhesion molecule 1 (ICAM-1) in Alzheimer’s disease
Frohman, E. M., Frohman, T. C., Gupta, S., de Fougerolles, A., & van den Noort, S. (1991) · Journal of the Neurological Sciences · doi:10.1016/0022-510x(91)90202-i · Cited by 120
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Saidak, Z., Le Henaff, C., Azzi, S., Marty, C., Da Nascimento, S., Sonnet, P., & Marie, P. J. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.621219 · Cited by 113
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Katt, M. E., Linville, R. M., Mayo, L. N., Xu, Z. S., & Searson, P. C. (2018) · Fluids and Barriers of the CNS · doi:10.1186/s12987-018-0092-7 · Cited by 102
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Lilja, J., & Ivaska, J. (2018) · Journal of Cell Science · doi:10.1242/jcs.212803 · Cited by 107
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Gpnmb is a melanosome-associated glycoprotein that contributes to melanocyte/keratinocyte adhesion in a RGD-dependent fashion
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Devalliere, J., Chang, W. G., Andrejecsk, J. W., Abrahimi, P., Cheng, C. J., Jane‐wit, D., Saltzman, W. M., & Pober, J. S. (2014) · The FASEB Journal · doi:10.1096/fj.13-238527 · Cited by 83
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Authors: Ruoslahti, E., & Pierschbacher, M. D.
Venue: Science
Publisher: American Association for the Advancement of Science (AAAS)
Published: 1987-10-23
Volume: 238
Issue: 4826
Pages: 491-497
ISSN: 0036-8075 (ISSN-L)
1095-9203
DOI: 10.1126/science.2821619
OpenAlex: W1987568997
Cited by: 4,865
References: 0
FWCI: 77.10
Type: journal article
Language: en
Open access: closed

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New Perspectives in Cell Adhesion: RGD and Integrins

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