Skip to main content

Abstract

The integrin family of cell adhesion receptors consists of over 20 members, which mediate cell surface interactions with extracellular matrix or (in some cases) with other cells (Akiyama et al., 1990b; Albelda and Buck, 1990; Clark, 1990; Hemler, 1990; Hogg, 1991; Ruoslahti, 1991; Shattil and Brugge, 1991; Yamada, 1991; Damsky and Werb, 1992; Ginsberg et al., 1992; Hynes, 1992; Akiyama and Yamada, 1993; Gailit and Clark, 1993; Glukhova and Thiery, 1993; Gumbiner, 1993; Juliano and Haskill, 1993; Sastry and Horwitz, 1993; Sonnenberg, 1993; Tuckwell et al., 1993; Zetter, 1993; Springer, 1994). Each integrin is a heterodimer, consisting of one a and one β subunit in a noncovalent complex. As summarized in Fig. 1, only certain combinations of integrins are observed: major groupings include integrins of the β1 subfamily and integrins containing the αv subunit. Changes in either the α or the β subunit of integrin heterodimers alter their specificity for ligands, as summarized in Table I.

This is a preview of subscription content, log in via an institution to check access.

Access this chapter

Chapter
USD 29.95
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
eBook
USD 259.00
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
Softcover Book
USD 329.00
Price excludes VAT (USA)
  • Compact, lightweight edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info
Hardcover Book
USD 329.99
Price excludes VAT (USA)
  • Durable hardcover edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info

Tax calculation will be finalised at checkout

Purchases are for personal use only

Institutional subscriptions

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  • Abrams, C., Deng, Y. J., Steiner, B., O’Toole, T., and Shattil, S. J., 1994, Determinants of specificity of a baculovirus-expressed antibody Fab fragment that binds selectively to the activated form of integrin αIIbβ3, J. Biol. Chem. 269:18781–18788.

    PubMed  CAS  Google Scholar 

  • Adams, J. C., and Watt, F. M., 1991, Expression of β1, β3, β4, and β5 integrins by human epidermal keratinocytes and non-differentiating keratinocytes, J. Cell Biol. 115:829–841.

    PubMed  CAS  Google Scholar 

  • Akiyama, S. K., and Yamada, K. M., 1987, Biosynthesis and acquisition of biological activity of the fibronectin receptor, J. Biol. Chem. 262:17536–17542.

    PubMed  CAS  Google Scholar 

  • Akiyama, S. K., and Yamada, K. M., 1993, Introduction: Adhesion molecules in cancer. Part I, Semin. Cancer Biol. 4:215–218.

    PubMed  CAS  Google Scholar 

  • Akiyama, S. K., Yamada, S. S., and Yamada, K. M., 1989, Analysis of the role of glycosylation of the human fibronectin receptor, J. Biol. Chem. 264:18011–18018.

    PubMed  CAS  Google Scholar 

  • Akiyama, S. K., Larjava, H., and Yamada, K. M., 1990a, Differences in the biosynthesis and localization of the fibronectin receptor in normal and transformed cultured human cells, Cancer Res. 50:1601–1607.

    PubMed  CAS  Google Scholar 

  • Akiyama, S. K., Nagata, K., and Yamada, K. M., 1990b, Cell surface receptors for extracellular matrix components, Biochim. Biophys. Acta 1031:91–110.

    PubMed  CAS  Google Scholar 

  • Akiyama, S. K., Yamada, S. S., Yamada, K. M., and LaFlamme, S. E., 1994, Transmembrane signal transduction by integrin cytoplasmic domains expressed in single-subunit chimeras, J. Biol. Chem. 269:15961–15964.

    PubMed  CAS  Google Scholar 

  • Albelda, S. M., and Buck, C. A., 1990, Integrins and other cell adhesion molecules, FASEB J. 4:2868–2880.

    PubMed  CAS  Google Scholar 

  • Albelda, S. M., Mette, S. A., Elder, D. E., Stewart, R., Damjanovich, L., Herlyn, M., and Buck, C. A., 1990, Integrin distribution in malignant melanoma: Association of the β3 subunit with tumor progression, Cancer Res. 50:6757–6764.

    PubMed  CAS  Google Scholar 

  • Bajt, M. L., Ginsberg, M. H., Frelinger, A., Berndt, M. C., and Loftus, J. C., 1992, A spontaneous mutation of integrin αIIbβ3 (platelet glycoprotein IIb-IIIa) helps define a ligand binding site, J. Biol. Chem. 267:3789–3794.

    PubMed  CAS  Google Scholar 

  • Balzac, F., Belkin, A. M., Koteliansky, V. E., Balabanov, Y. V., Altruda, F., Silengo, L., and Tarone, G., 1993, Expression and functional analysis of a cytoplasmic domain variant of the β1 integrin subunit, J. Cell Biol. 121:171–178.

    PubMed  CAS  Google Scholar 

  • Barrandon, Y., and Green, H., 1987, Cell migration is essential for sustained growth of keratinocytes colonies: The roles of transforming growth factor-α and epidermal growth factor, Cell 50:1131–1137.

    PubMed  CAS  Google Scholar 

  • Bauer, J., Varner, J., Schreiner, C., Kornberg, L., Nicholas, R., and Juliano, R. L., 1993, Functional role of the cytoplasmic domain of the integrin α5 subunit, J. Cell Biol. 122:209–221.

    PubMed  CAS  Google Scholar 

  • Betz, P., Nerlich, A., Tubel, J., Penning, R., and Eisenmenger, W., 1993, Localization of tenascin in human skin wounds: An immunohistochemical study, Int. J. Legal. Med. 105:325–328.

    PubMed  CAS  Google Scholar 

  • Briesewitz, R., Kern, A., and Marcantonio, E. E., 1993, Ligand-dependent and-independent integrin focal contact localization: The role of the alpha chain cytoplasmic domain, Mol. Biol. Cell. 4:593–604.

    PubMed  CAS  Google Scholar 

  • Brown, C., Stenn, K. S., Falk, R. J., Woodley, D. T., and O’Keefe, E. J., 1991, Vitronectin: Effects on keratinocyte motility and inhibition of collagen-induced motility, J. Invest. Dermatol. 96:724–728.

    PubMed  CAS  Google Scholar 

  • Burns, K., Duggan, B., Atkinson, E. A., Famulski, K. S., Nemer, M., Bleackley, R. C., and Michalak, M., 1994, Modulation of gene expression by calreticulin binding to the glucocorticoid receptor, Nature 367:476–480.

    PubMed  CAS  Google Scholar 

  • Calvete, J. J., Mann, K., Schäfer, W., Fernandez-Lafuente, R., and Guisan, J. M., 1994, Proteolytic degradation of the RGD-binding and non-RGD-binding conformers of human platelet integrin glycoprotein IIb/IIIa: Clues for identification of regions involved in the receptor’s activation, Biochem. J. 298:1–7.

    PubMed  CAS  Google Scholar 

  • Carter, W. G., Kaur, P., Gil, S. G., Gahr, P. J., and Wayner, E. A., 1990a, Distinct functions for integrins α3β1 in focal adhesions and α6β4/bullous pemphigoid antigen in a new stable anchoring contact (SAC) of keratinocytes: Relation to hemidesmosomes, J. Cell Biol. 111:3141–3154.

    PubMed  CAS  Google Scholar 

  • Carter, W. G., Wayner, E. A., Bouchard, T. S., and Kaur, P., 1990b, The role of integrins a2βl and α3βl in cell-cell and cell-substrate adhesion of human epidermal cells, J. Cell Biol. 110:1387–1404.

    PubMed  CAS  Google Scholar 

  • Carter, W. G., Ryan, M. C., and Gahr, P. A., 1991, Epiligrin, a new cell adhesion ligand for integrin α3β1 in epithelial basement membranes, Cell 65:599–610.

    PubMed  CAS  Google Scholar 

  • Cavani, A., Zambruno, G., Marconi, A., Manca, V., Marchetti, M., and Giannetti, A., 1993, Distinctive integrin expression in the newly forming epidermis during wound healing in humans, J. Invest. Der-matol. 101:600–604.

    CAS  Google Scholar 

  • Chan, B. M., Kassner, P. D., Schiro, J. A., Byers, H. R., Kuppe, T. S., and Hemler, M. E., 1992, Distinct cellular functions mediated by different VLA integrin a subunit cytoplasmic domains, Cell 68:1051–1060.

    PubMed  CAS  Google Scholar 

  • Chen, J. D., Kim, J. P., Zhang, K., Sarret, Y., Wynn, K. C., Kramer, R. H., and Woodley, D. T., 1993, Epidermal growth factor (EGF) promotes human keratinocyte locomotion on collagen by increasing the α2 integrin subunit, Exp. Cell Res. 209:216–223.

    PubMed  CAS  Google Scholar 

  • Chen, Q., Kinch, M. S., Lin, T. H., Burridge, K., and Juliano, R. L., 1994, Integrin-mediated cell adhesion activates mitogen-activated protein kinases. Integrin-mediated cell adhesion activates mitogen-activated protein kinases, J. Biol. Chem. 269:26602–26605.

    PubMed  CAS  Google Scholar 

  • Chen, W. T., and Singer, S. J., 1982, Immunoelectron microscopic studies of the sites of cell-substratum and cell-cell contacts in cultured fibroblasts, J. Cell Biol. 95:205–222.

    PubMed  CAS  Google Scholar 

  • Chen, Y. P., O’Toole, T. E., Shipley, T., Forsyth, J., LaFlamme, S. E., Yamada, K. M., Shattil, S. J., and Ginsberg, M. H., 1994, Inside-out signal transduction inhibited by isolated integrin cytoplasmic domains, J. Biol. Chem. 269:18307–18310.

    PubMed  CAS  Google Scholar 

  • Cheresh, D. A., 1991, Structure, function and biological properties of integrin αvβ3 on human melanoma cells, Cancer Metastasis Rev. 10:3–10.

    PubMed  CAS  Google Scholar 

  • Cheresh, D. A., and Spiro, R. C., 1987, Biosynthetic and functional properties of an Arg-Gly-Asp-directed receptor involved in human melanoma cell attachment to vitronectin, fibrinogen, and von Willebrand factor, J. Biol. Chem. 262:17703–17711.

    PubMed  CAS  Google Scholar 

  • Clark, R. A. F., 1990, Fibronectin matrix deposition and fibronectin receptor expression in healing and normal skin, J. Invest. Dermatol. 94:128S–134S.

    PubMed  CAS  Google Scholar 

  • Clark, R. A. F., Lanigan, J. M., DellaPelle, P., Manseau, E., Dvorak, H. F., and Colvin, R. B., 1982, Fibronectin and fibrin provide a provisional matrix for epidermal cell migration during wound reep-ithelialization, J. Invest. Dermatol. 70:264–269.

    Google Scholar 

  • Clark, R. A. F., Wikner, N. E., Doherty, D. E., and Noms, D. A., 1988, Cryptic chemotactic activity of fibronectin for human monocytes resides in the 120-kDa fibroblastic cell-binding fragment, J. Biol. Chem. 263:12115–12123.

    PubMed  CAS  Google Scholar 

  • Clark, R. A. F., Gailit, J., Pierschbacher, M. D., and Ruoslahti, E., 1990, Expression of fibronectin and vitronectin receptors in wound fibroblasts, Clin. Res. 38:630A.

    Google Scholar 

  • Clark, R. A. F., Spencer, J., Larjava, H., and Ferguson, M., 1995a, Reepithelialization of normal human excisional wounds is associated with a switch from αvβ5 to αvβ6 integrins, J. Invest. Dermatol.

    Google Scholar 

  • Clark, R. A. F., Tonnesen, M. G., Gailit, J., and Cheresh, D. A., 1995b, Transient functional expression of αvβ3 on vascular cells during wound repair, Am. J. Path., in press.

    Google Scholar 

  • Collo, G., Starr, L., and Quaranta, V., 1993, A new isoform of the laminin receptor integrin α7β1 is developmentally regulated in skeletal muscle, J. Biol. Chem. 268:19019–19024.

    PubMed  CAS  Google Scholar 

  • Conforti, G., Calza, M., and Beltran-Nunez, A., 1994, αvβ5 integrin is localized at focal contacts by HT-1080 fibrosarcoma cells and human skin fibroblasts attached to vitronectin, Cell. Adhesion Commun. 1:279–293.

    CAS  Google Scholar 

  • Couchman, J. R., and Rees, D. A., 1979, The behaviour of fibroblasts migrating from chick heart expiants: Changes in adhesion, locomotion and growth, and in the distribution of actomyosin and fibronectin, J. Cell Sci. 39:149–165.

    PubMed  CAS  Google Scholar 

  • Damsky, C. H., and Werb, Z., 1992, Signal transduction by integrin receptors for extracellular matrix: Cooperative processing of extracellular information, Curr. Opin. Cell Biol. 4:772–781.

    PubMed  CAS  Google Scholar 

  • Davis, E. D., 1992, Affinity of integrins for damaged extracellular matrix: αvβ3 binds to denatured collagen type I through RGD sites, Biochem. Biophys. Res. Commun. 182:1025–1031.

    PubMed  CAS  Google Scholar 

  • Dedhar, S., Ruoslahti, E., and Pierschbacher, M. D., 1987, A cell surface receptor complex for collagen type I recognizes the Arg-Gly-Asp sequence, J. Cell Biol. 104:585–593.

    PubMed  CAS  Google Scholar 

  • Dedhar, S., Rennie, P. S., Shago, M., Hagesteijn, C. Y., Yang, H., Filmus, J., Hawley, R. G., Bruchovsky, N., Cheng, H., and Matusik, R. J., 1994, Inhibition of nuclear hormone receptor activity by calreticulin, Nature 367:480–483.

    PubMed  CAS  Google Scholar 

  • De Luca, M., Tamura, R. N., Kajiji, S., Bondanza, S., Rossino, P., Cancedda, R., Marchisio, P. C., and Quaranta, V., 1990, Polarized integrin mediates human keratinocyte adhesion to basal lamina, Proc. Natl. Acad. Sci. USA 87:6888–6892.

    PubMed  Google Scholar 

  • de Vos, A. M., Ultsch, M., and Kossiakoff, A. A., 1992, Human growth hormone and extracellular domain of its receptor: Crystal structure of the complex, Science 255:306–312.

    PubMed  Google Scholar 

  • DiMilla, P. A., Stone, J. A., Quinn, J. A., Albelda, S. M., and Lauffenburger, D. A., 1993, Maximal migration of human smooth muscle cells on fibronectin and type IV collagen occurs at an intermediate attachment strength, J. Cell Biol. 122:729–737.

    PubMed  CAS  Google Scholar 

  • Donaldson, D. J., Mahan, J. T., Hui, Y., and Yamada, K. M., 1994, Integrin and phosphotyrosine expression in normal and migrating newt keratinocytes, Anat. Rec. 241:49–58.

    Google Scholar 

  • Douglass, G. D., Zhang, K., and Kramer, R. H., 1992, The role of integrin adhesion receptors in gingival wound healing, J. Calif. Dent. Assoc. 20:37–40.

    PubMed  CAS  Google Scholar 

  • D’Souza, S. E., Ginsberg, M. H., Burke, T. A., and Plow, E. F., 1990, The ligand binding site of the platelet integrin receptor GPIIb-IIIa is proximal to the second calcium binding domain of its a subunit, J. Biol. Chem. 265:3440–3446.

    PubMed  Google Scholar 

  • D’Souza, S. E., Ginsberg, M. H., Matsueda, G. R., and Plow, E. F., 1991, A discrete sequence in a platelet integrin is involved in ligand recognition, Nature 350:66–68.

    PubMed  Google Scholar 

  • D’Souza, S. E., Haas, T. A., Piotrowicz, R. S., Byers-Ward, V., McGrath, D. E., Soule, H. R., Cierniewski, C., Plow, E. F., and Smith, J. W., 1994, Ligand and cation binding are dual functions of a discrete segment of the integrin β3 subunit: Cation displacement is involved in ligand binding, Cell 79:659–667.

    PubMed  Google Scholar 

  • Du, X. P., Plow, E. F., Frelinger, A. L., O’Toole, T. E., Loftus, J. C., and Ginsberg, M. H., 1991, Ligands activate integrin αIIbβ3 (platelet GPIIb-IIIa), Cell 65:409–416.

    PubMed  CAS  Google Scholar 

  • Duband, J. L., Nuckolls, G. H., Ishihara, A., Hasegawa, T., Yamada, K. M., Thiery, J. P., and Jacobson, K., 1988a, Fibronectin receptor exhibits high lateral mobility in embryonic locomoting cells but is immobile in focal contacts and fibrillar streaks in stationary cells, J. Cell Biol. 107:1385–1396.

    PubMed  CAS  Google Scholar 

  • Duband, J. L., Dufour, S., Yamada, K. M., and Thiery, J. P., 1988b, The migratory behavior of avian embryonic cells does not require phosphorylation of the fibronectin-receptor complex, FEBS Lett. 230:181–185.

    PubMed  CAS  Google Scholar 

  • Duband, J. L., Dufour, S., Yamada, S. S., Yamada, K. M., and Thiery, J. P., 1991, Neural crest cell locomotion induced by antibodies to β1 integrins. A tool for studying the roles of substratum molecular avidity and density in migration, J. Cell Sci. 98:517–532.

    PubMed  CAS  Google Scholar 

  • Dustin, M. L., and Springer, T. A., 1989, T-cell receptor cross-linking transiently stimulates adhesiveness through LFA-1, Nature 341:619–624.

    PubMed  CAS  Google Scholar 

  • Eble, J. A., Golbik, R., Mann, K., and Kuhn, K., 1993, The α1β1 integrin recognition site of the basement membrane collagen molecule [α1(IV)]2 α2(IV)], EMBO J. 12:4795–4802.

    PubMed  CAS  Google Scholar 

  • Elemer, G. S., and Edgington, T. S., 1994, Microfilament reorganization is associated with functional activation of αMβ2 on monocytic cells, J. Biol. Chem. 269:3159–3166.

    PubMed  CAS  Google Scholar 

  • Elices, M. J., Urry, L. A., and Hemler, M. E., 1991, Receptor functions for the integrin VLA-3: Fibronectin, collagen, and laminin binding are differentially influenced by Arg-Gly-Asp peptide and by divalent cations, J. Cell Biol. 112:169–181.

    PubMed  CAS  Google Scholar 

  • Faull, R. J., Kovach, N. L., Harlan, J. M., and Ginsberg, M. H., 1993, Affinity modulation of integrin α5β1: Regulation of the functional response by soluble fibronectin, J. Cell Biol. 121:155–162.

    PubMed  CAS  Google Scholar 

  • Gailit, J., and Clark, R. A. F., 1993, Integrins in the skin, Adv. Dermatol. 8:129–152.

    PubMed  CAS  Google Scholar 

  • Gailit, J., Welch, M. P., and Clark, R. A. F., 1994, TGF-β 1 stimulates expression of keratinocyte integrins during re-epithelialization of cutaneous wounds, J. Invest. Dermatol. 103:221–227.

    PubMed  CAS  Google Scholar 

  • Gehlsen, K. R., Argraves, W. S., Pierschbacher, M. D., and Ruoslahti, E., 1988, Inhibition of in vitro tumor cell invasion by Arg-Gly-Asp-containing synthetic peptides, J. Cell Biol. 106:925–930.

    PubMed  CAS  Google Scholar 

  • Geiger, B., 1989, Cytoskeleton-associated cell contacts, Curr. Opin. Cell Biol. 1:103–109.

    PubMed  CAS  Google Scholar 

  • Geiger, B., Salomon, D., Takeichi, M., and Hynes, R. O., 1992, A chimeric N-cadherin/β1-integrin receptor which localizes to both cell-cell and cell-matrix adhesions, J. Cell Sci. 103:943–951.

    PubMed  CAS  Google Scholar 

  • Ginsberg, M. H., Du, X., and Plow, E. F., 1992, Inside-out integrin signalling, Curr. Opin. Cell Biol. 4:766–771.

    PubMed  CAS  Google Scholar 

  • Gipson, I. K., Spurr-Michaud, S., Tisdale, A., Elwell, J., and Stepp, M. A., 1993, Redistribution of the hemidesmosome components α6β4 integrin and bullous pemphigoid antigens during epithelial wound healing, Exp. Cell Res. 207:86–98.

    PubMed  CAS  Google Scholar 

  • Glukhova, M. A., and Thiery, J. P., 1993, Fibronectin and integrins in development, Semin. Cancer Biol. 4:241–249.

    PubMed  CAS  Google Scholar 

  • Grinnell, F., 1990, The activated keratinocyte: Up-regulation of cell adhesion and migration during wound healing, J. Trauma 30:S144–S149.

    PubMed  CAS  Google Scholar 

  • Grinnell, F., 1992, Wound repair, keratinocyte activation and integrin modulation, J. Cell Sci. 101:1–5.

    PubMed  CAS  Google Scholar 

  • Grinnell, F., and Geiger, B., 1986, Interaction of fibronectin-coated beads with attached and spread fi-broblasts. Binding, phagocytosis, and cytoskeletal reorganization, Exp. Cell Res. 162:449–461.

    PubMed  CAS  Google Scholar 

  • Grinnell, F., Toda, K.-I., and Takashima, A., 1988, Role of fibronectin in epithelialization and wound healing, in: Growth Factors and Other Aspects of Wound Healing: Biological and Clinical Implications (A. Barbul, E. Pines, M. Caldwell, and T. K. Hunt, eds.), pp. 259–272, Alan R. Liss, New York.

    Google Scholar 

  • Guadagno, T. M., Ohtsubo, M., Roberts, J. M., and Assoian, R. K., 1993, A link between cyclin A expression and adhesion-dependent cell cycle progression, Science 262:1572–1575.

    PubMed  CAS  Google Scholar 

  • Guan, J. L., and Shalloway, D., 1992, Regulation of focal adhesion-associated protein tyrosine kinase by both cellular adhesion and oncogenic transformation, Nature 358:690–692.

    PubMed  CAS  Google Scholar 

  • Guan, J. L., Trevithick, J. E., and Hynes, R. O., 1991, Fibronectin/integrin interaction induces tyrosine phosphorylation of a 120-kDa protein, Cell Regul. 2:951–964.

    PubMed  CAS  Google Scholar 

  • Gumbiner, B. M., 1993, Proteins associated with the cytoplasmic surface of adhesion molecules, Neuron 11:551–564.

    PubMed  CAS  Google Scholar 

  • Guo, M., Toda, K., and Grinnell, F., 1990, Activation of human keratinocyte migration on type I collagen and fibronectin, J. Cell Sci. 96:197–205.

    PubMed  CAS  Google Scholar 

  • Guo, M., Kim, L. T., Akiyama, S. K., Gralnick, H. R., Yamada, K. M., and Grinnell, F., 1991, Altered processing of integrin receptors during keratinocyte activation, Exp. Cell Res. 195:315–322.

    PubMed  CAS  Google Scholar 

  • Haapasalmi, K., Zhang, K., Tonnesen, M. G., Olerud, J., Sheppard, D., Kramer, R., Clark, R. A. F., Uitto, V.-J., and Larjava, H., 1995, Keratinocytes in human wounds express avβ6 integrin, J. Invest. Dermatol. submitted.

    Google Scholar 

  • Han, E. K., Guadagno, T. M., Dalton, S. L., and Assoian, R. K., 1993, A cell cycle and mutational analysis of anchorage-independent growth: Cell adhesion and TGF-β1 control G1/S transit specifically, J. Cell Biol. 122:461–471.

    PubMed  CAS  Google Scholar 

  • Hay, E., 1991, Cell Biology of Extracellular Matrix, Plenum Press, New York.

    Google Scholar 

  • Hayashi, Y., Haimovich, B., Reszka, A., Boettige, D., and Horwitz, A., 1990, Expression and function of chicken integrin β1 subunit and its cytoplasmic domain mutants in mouse NIH 3T3 cells, J. Cell Biol. 110:175–184.

    PubMed  CAS  Google Scholar 

  • Heino, J., Ignotz, R. A., Hemler, M. E., Crouse, C., and Massague, J., 1989, Regulation of cell adhesion receptors by transforming growth factor-β. Concomitant regulation of integrins that share a common β1 subunit, J. Biol. Chem. 264:380–388.

    PubMed  CAS  Google Scholar 

  • Hemler, M. E., 1990, VLA proteins in the integrin family: Structures, functions, and their role on leukocytes, Annu. Rev. Immunol. 8:365–400.

    PubMed  CAS  Google Scholar 

  • Hergott, G. J., Nagai, H., and Kalnins, V. I., 1993, Inhibition of retinal pigment epithelial cell migration and proliferation with monoclonal antibodies against the β1 integrin subunit during wound healing in organ culture, Invest. Ophthalmol. Vis. Sci. 34:2761–2768.

    PubMed  CAS  Google Scholar 

  • Hertle, M. D., Kubier, M. D., Leigh, I. M., and Watt, F. M., 1992, Aberrant integrin expression during epidermal wound healing and in psoriatic epidermis, J. Clin. Invest. 89:1892–1901.

    PubMed  CAS  Google Scholar 

  • Hogg, N., 1991, An integrin overview, Chem. Immunol. 50:1–12.

    PubMed  CAS  Google Scholar 

  • Horton, M., 1990, Vitronectin receptor: Tissue specific expression or adaptation to culture? Int. J. Exp. Pathol. 71:741–759.

    PubMed  CAS  Google Scholar 

  • Horwitz, A., Duggan, K., Buck, C., Beckerle, M. C., and Burridge, K., 1986, Interaction of plasma membrane fibronectin receptor with talin—A transmembrane linkage, Nature 320:531–533.

    PubMed  CAS  Google Scholar 

  • Howlett, A. R., and Bissell, M. J., 1993, The influence of tissue microenvironment (stroma and extracellular matrix) on the development and function of mammary epithelium, Epithelial Cell. Biol. 2:79–89.

    PubMed  CAS  Google Scholar 

  • Huhtala, P., Humphries, M. J., McCarthy, J. B., Tremble, P. M., Werb, Z., and Damsky, C. H., 1995, Cooperative signaling by α5β1 and α4β1 integrins regulates metalloproteinase gene expression in fibroblasts adhering to fibronectin, J. Cell Biol 129:867–879.

    PubMed  CAS  Google Scholar 

  • Hyatt, S. L., Klauck, T., and Jaken, S., 1990, Protein kinase C is localized in focal contacts of normal but not transformed fibroblasts, Mol. Carcinog. 3:45–53.

    PubMed  CAS  Google Scholar 

  • Hynes, R. O., 1992, Integrins: Versatility, modulation, and signaling in cell adhesion, Cell 69:11–25.

    PubMed  CAS  Google Scholar 

  • Jones, J. C. R., Kurpakus, M. A., Cooper, H. M., and Quaranta, V., 1991, A function for the integrin α6β4 in the hemidesmosome, Cell Regul. 2:427–438.

    PubMed  CAS  Google Scholar 

  • Juhasz, I., Murphy, G. F., Yan, H. C., Herlyn, M., and Albelda, S. M., 1993. Regulation of extracellular matrix proteins and integrin cell substratum adhesion receptors on epithelium during cutaneous human wound healing in vivo, Am. J. Pathol. 143(5): 1458–1469.

    PubMed  CAS  Google Scholar 

  • Juliano, R. L., and Haskill, S., 1993, Signal transduction from the extracellular matrix, J. Cell Biol. 120:577–585.

    PubMed  CAS  Google Scholar 

  • Kamata, T., and Takada, Y., 1994, Direct binding of collagen to the I domain of integrin α2βl (VLA-2, CD49b/CD29) in a divalent cation-independent manner, J. Biol. Chem. 269(42):26006–26010.

    PubMed  CAS  Google Scholar 

  • Kapron-Bras, C., Fitz-Gibbon, L., Jeevaratnam, P., Wilkins, J., and Dedhar, S., 1993, Stimulation of tyrosine phosphorylation and accumulation of GTP-bound p21ras upon antibody-mediated α2β1 integrin activation in T-lymphoblastic cells, J. Biol. Chem. 268:20701–20704.

    PubMed  CAS  Google Scholar 

  • Kassner, P. D., and Hemler, M. E., 1993, Interchangeable a chain cytoplasmic domains play a positive role in control of cell adhesion mediated by VLA-4, a β1 integrin, J. Exp. Med. 178:649–660.

    PubMed  CAS  Google Scholar 

  • Kassner, P. D., Kawaguchi, S., and Hemler, M. E., 1994, Minimum a chain cytoplasmic tail sequence needed to support integrin-mediated adhesion, J. Biol. Chem. 269:19859–19867.

    PubMed  CAS  Google Scholar 

  • Kaufmann, R., Frosch, D., Westphal, C., Weber, L., and Klein, C. E., 1989, Integrin VLA-3: Ultrastructural localization at cell-cell contact sites of human cell cultures, J. Cell Biol. 109:1807–1815.

    PubMed  CAS  Google Scholar 

  • Kern, A., Briesewitz, R., Bank, I., and Marcantonio, E. E., 1994, The role of the I domain in ligand binding of the human integrin α1β1, J. Biol. Chem. 269:22811–22816.

    PubMed  CAS  Google Scholar 

  • Kim, J. P., Chen, J. D., and Woodley, D. T., 1992a, Mechanism of human keratinocyte migration on fibronectin: Unique roles of RGD site and integrins, J. Cell. Physiol. 151:443–450.

    PubMed  CAS  Google Scholar 

  • Kim, J. P., Zhang, K., Kramer, R. H., Schall, T. J., and Woodley, D. T., 1992b, Integrin receptors and RGD sequences in human keratinocyte migration: Unique antimigratory function of α3β1, J. Invest. Dermatol. 98:764–770.

    PubMed  CAS  Google Scholar 

  • Kim, J. P., Zhang, K., Chen, J. D. Kramer, R. H., and Woodley, D. T., 1994, Vitronectin-driven human keratinocyte locomotion is mediated by the αvβ5 integrin receptor, J. Biol. Chem. 269:26926–26932.

    PubMed  CAS  Google Scholar 

  • Kim, L. T., Ishihara, S., Lee, C. C., Akiyama, S. K., Yamada, K. M., and Grinnell, F., 1992, Altered glycosylation and cell surface expression of β1 integrin receptors during keratinocyte activation, J. Cell Sci. 103:743–753.

    PubMed  CAS  Google Scholar 

  • Klebe, R. J., 1974, Isolation of a collagen-dependent cell attachment factor, Nature 250:248–251.

    PubMed  CAS  Google Scholar 

  • Koivisto, L., Heino, J., Hakkinen, L., and Larjava, H., 1994, The size of the intracellular β1-integrin precursor pool regulates maturation of β1-integrin subunit and associated α-subunits, Biochem. J. 300:771–779.

    PubMed  CAS  Google Scholar 

  • Kornberg, L. J., Earp, H. S., Turner, C. E., Prockop, C., and Juliano, R. L., 1991, Signal transduction by integrins: Increased protein tyrosine phosphorylation caused by clustering of βl integrins, Proc. Natl. Acad. Sci. USA 88:8392–8396.

    PubMed  CAS  Google Scholar 

  • Kornberg, L., Earp, H. S., Parsons, J. T., Schaller, M., and Juliano, R. L., 1992, Cell adhesion or integrin clustering increases phosphorylation of a focal adhesion-associated tyrosine kinase, J. Biol. Chem. 267:23439–23442.

    PubMed  CAS  Google Scholar 

  • Kurpakus, M. A., Quaranta, V., and Jones, J. C., 1991, Surface relocation of α6β4 integrins and assembly of hemidesmosomes in an in vitro model of wound healing, J. Cell Biol. 115:1737–1750.

    PubMed  CAS  Google Scholar 

  • LaFlamme, S. E., Akiyama, S. K., and Yamada, K. M., 1992, Regulation of fibronectin receptor distribution, J. Cell Biol. 117:437–447.

    PubMed  CAS  Google Scholar 

  • LaFlamme, S. E., Thomas, L. A., Yamada, S. S., and Yamada, K. M., 1994, Single-subunit chimeric integrins as mimics and inhibitors of endogenous integrin functions. J. Cell Biol. 126:1287–1298.

    PubMed  CAS  Google Scholar 

  • Larjava, H., 1991, Expression of β1 integrins in normal human keratinocytes. Am. J. Med. Sci. 301:63–68.

    PubMed  CAS  Google Scholar 

  • Larjava, H., Peltonen, J., Akiyama, S. K., Yamada, S. S., Gralnick, H. R., Uitto, J., and Yamada, K. M., 1990, Novel function for β1 integrins in keratinocyte cell-cell interactions, J. Cell Biol. 110:803–815.

    PubMed  CAS  Google Scholar 

  • Larjava, H., Salo, T., Haapasalmi, K., Kramer, R. H., and Heino, J., 1993, Expression of integrins and basement membrane components by wound keratinocytes, J. Clin. Invest. 92:1425–1435.

    PubMed  CAS  Google Scholar 

  • Lee, E. C., Lotz, M. M., Stelle, G. D., and Mercurio, A. M., 1992, The integrin α6β4 is a laminin receptor, J. Cell Biol. 117:671–678.

    PubMed  CAS  Google Scholar 

  • Lenter, M., and Vestweber, D., 1994, The integrin chains β1 and α6 associate with the chaperone calnexin prior to integrin assembly, J. Biol. Chem. 269:12263–12268.

    PubMed  CAS  Google Scholar 

  • Leung-Hagesteijn, C. Y., Milankov, K., Michalak, M., Wilkins, J., and Dedhar, S., 1994, Cell attachment to extracellular matrix substrates is inhibited upon down-regulation of expression of calreticulin, an intracellular integrin α-subunit-binding protein, J. Cell Sci. 107:589–600.

    PubMed  CAS  Google Scholar 

  • Lewis, J. M., and Schwartz, M. A., 1995, Mapping in vivo associations of cytoplasmic proteins with integrin βl cytoplasmic domain mutants, Mol. Biol. Cell 6:151–160.

    PubMed  CAS  Google Scholar 

  • Lin, C. Q., and Bissell, M. J., 1993, Multi-faceted regulation of cell differentiation by extracellular matrix, FASEB J. 7:737–743.

    PubMed  CAS  Google Scholar 

  • Lindberg, F. P., Gresham, H. D., Schwarz, E., and Brown, E. J., 1993, Molecular cloning of integrin-associated protein: an immunoglobulin family member with multiple membrane-spanning domains implicated in αvβ3-dependent ligand binding, J. Cell Biol. 123:485–496.

    PubMed  CAS  Google Scholar 

  • Loftus, J. C., O’Toole, T. E., Plow, E. F., Glass, A., Frelinger, A. L., and Ginsberg, M. H., 1990, A β3 integrin mutation abolishes ligand binding and alters divalent cation-dependent conformation, Science 249:915–918.

    PubMed  CAS  Google Scholar 

  • Lukashev, M. E., Sheppard, D., and Pytela, R., 1994, Disruption of integrin function and induction of tyrosine phosphorylation by the autonomously expressed βl integrin cytoplasmic domain, J. Biol. Chem. 269:18311–18314.

    PubMed  CAS  Google Scholar 

  • Mackie, E. J., Halfter, W., and Liverani, D., 1988, Induction of tenascin in healing wounds, J. Cell Biol. 107:2757–2767.

    PubMed  CAS  Google Scholar 

  • Marchisio, P. C., Bondanza, S., Cremona, O., Cancedda, R., and De Luca, M., 1991, Polarized expression of integrin receptors (α6β4, α2βl, α3β1, and αvβ5) and their relationship with the cytoskeleton and basement membrane matrix in cultured human keratinocytes, J. Cell Biol. 112:761–773.

    PubMed  CAS  Google Scholar 

  • Marinkovich, M. P., Keene, D. R., Rimberg, C. S., and Burgeson, R. E., 1993, Cellular origin of the dermal-epidermal basement membrane, Dev. Dynam. 197:255–267.

    CAS  Google Scholar 

  • McNamee, H. P., Ingber, D. E., and Schwartz, M. A., 1993, Adhesion to fibronectin stimulates inositol lipid synthesis and enhances PDGF-induced inositol lipid breakdown, J. Cell Biol. 121:673–678.

    PubMed  CAS  Google Scholar 

  • Metzger, H., 1992, Transmembrane signaling: The joy of aggregation, J. Immunol. 149:1477–1487.

    PubMed  CAS  Google Scholar 

  • Miyamoto, S., Akiyama, S. K., and Yamada, K. M., 1995a, Synergistic roles for receptor occupancy and aggregation in integrin transmembrane function, Science 267:883–885.

    PubMed  CAS  Google Scholar 

  • Miyamoto, S., Teramoto, H., Coso, O. A., Gutkind, J. S., Burbelo, P. D., Akiyama, S. K., and Yamada, K. M., 1995b, Integrin function: Molecular hierarchies of cytoskeletal and signaling molecules, J. Cell Biol., 131:791–805.

    PubMed  CAS  Google Scholar 

  • Morino, N., Mimura, T., Hamasaki, K., Tobe, K., Ueki, K., Kikuchi, K., Takehara, K., Kadowaki, T., Yazaki, Y., and Nojima, Y., 1995, Matrix/integrin interaction activates the mitogen-activated protein kinase, p44erk-l and p42erk-2, J. Biol. Chem. 270:269–273.

    PubMed  CAS  Google Scholar 

  • Mueller, S. C., Kelly, T., Dai, M. Z., Dai, H. N., and Chen, W. T., 1989, Dynamic cytoskeleton-integrin associations induced by cell binding to immobilized fibronectin, J. Cell Biol. 109:3455–3464.

    PubMed  CAS  Google Scholar 

  • Murakami, J., Nishida, T., and Otori, T., 1992, Coordinated appearance of β1 integrins and fibronectin during corneal wound healing, J. Lab. Clin. Med. 120:86–93.

    PubMed  CAS  Google Scholar 

  • Nermut, M. V., Green, N. M., Eason, P., Yamada, S. S., and Yamada, K. M., 1988, Electron microscopy and structural model of human fibronectin receptor, EMBO J. 7:4093–4099.

    PubMed  CAS  Google Scholar 

  • Ödland, G., and Ross, R., 1968, Human wound repair. I. Epidermal regeneration, J. Cell Biol. 39:135–157.

    PubMed  Google Scholar 

  • O’Keefe, E. J., Payne, Jr., R. E., Russell, N., and Woodley, D. T., 1985, Spreading and enhance motility of human keratinocytes on fibronectin, J. Invest. Dermatol. 85:125–130.

    PubMed  Google Scholar 

  • Otey, C. A., Pavalko, F. M., and Burridge, K., 1990, An interaction between α-actinin and the β1 integrin subunit in vitro, J. Cell Biol 111:721–729.

    PubMed  CAS  Google Scholar 

  • Otey, C. A., Vasquez, G. B., Burridge, K., and Erickson, B. W., 1993, Mapping of the α-actinin binding site within the β1 integrin cytoplasmic domain, J. Biol. Chem. 268:21193–21197.

    PubMed  CAS  Google Scholar 

  • O’Toole, T. E., Katagiri, Y., Faull, R. J., Peter, K., Tamura, R., Quaranta, V., Loftus, J. C., Shattil, S. J., and Ginsberg, M. H., 1994, Integrin cytoplasmic domains mediate inside-out signal transduction, J. Cell Biol. 124(6): 1047–1059.

    PubMed  Google Scholar 

  • O’Toole, T. E., Mandelman, D., Forsyth, J., Shattil, S. J., Plow, E. F., and Ginsberg, M. H., 1991, Modulation of the affinity of integrin αIIbβ3 (GPIIb-IIIa) by the cytoplasmic domain of αIIb, Science 254:845–847.

    PubMed  Google Scholar 

  • Paallysaho, T., Tervo, T., Virtanen, I., and Tervo, K., 1992, Integrins in the normal and healing corneal epithelium, Acta Ophthalmol. Suppl. 202:22–25.

    PubMed  Google Scholar 

  • Pardi, R., Inverardi, L., Rugarli, C., and Bender, J. R., 1992, Antigen-receptor complex stimulation triggers protein kinase C-dependent CD11a/CD18-cytoskeleton association in T lymphocytes, J. Cell Biol. 116:1211–1220.

    PubMed  CAS  Google Scholar 

  • Pasqualini, R., and Hemler, M. E., 1994, Contrasting roles for integrin β1 and β5 cytoplasmic domains in subcellular localization, cell proliferation, and cell migration, J. Cell Biol. 125:447–460.

    PubMed  CAS  Google Scholar 

  • Pavalko, F. M., and LaRoche, S. M., 1993, Activation of human neutrophils induces an interaction between the integrin β2-subunit (CD18) and the actin binding protein alpha-actinin, J. Immunol. 151:3795–3807.

    PubMed  CAS  Google Scholar 

  • Pavalko, F. M., and Otey, C. A., 1994, Role of adhesion molecule cytoplasmic domains in mediating interactions with the cytoskeleton, Proc. Soc. Exp. Biol. Med. 205:282–293.

    PubMed  CAS  Google Scholar 

  • Pfaff, M., Aumailley, M., Specks, U., Knolle, J., Zerwes, H. G., and Timpl, R., 1993, Integrin and Arg-Gly-Asp dependence of cell adhesion to the native and unfolded triple helix of collagen type VI, Exp. Cell Res. 206(1):167–176.

    PubMed  CAS  Google Scholar 

  • Plopper, G., and Ingber, D. E., 1993, Rapid induction and isolation of focal adhesion complexes, Biochem. Biophys. Res. Commun. 193:571–578.

    PubMed  CAS  Google Scholar 

  • Plow, E. F., D’Souza, S. E., and Ginsberg, M. H., 1992, Ligand binding to GPIIb-IIIa: A status report, Semin. Thromb. Hemost. 18:324–332.

    PubMed  CAS  Google Scholar 

  • Ramaswamy, H., and Hemler, M. E., 1990, Cloning, primary structure and properties of a novel human integrin β subunit, EMBO J. 9:1561–1568.

    PubMed  CAS  Google Scholar 

  • Randi, A. M., and Hogg, N., 1994, I domain of β2 integrin lymphocyte function-associated antigen-1 contains a binding site for ligand intercellular adhesion molecule-1, J. Biol. Chem. 269:12395–12398.

    PubMed  CAS  Google Scholar 

  • Rojiani, M. V., Finlay, B. B., Gray, V., and Dedhar, S., 1991, In vitro interaction of a polypeptide homologous to human Ro/SS-A antigen (calreticulin) with a highly conserved amino acid sequence in the cytoplasmic domain of integrin α subunits, Biochemistry 30:9859–9866.

    PubMed  CAS  Google Scholar 

  • Rousselle, P., Lunstrum, G. P., Keene, D. R., and Burgeson, R. E., 1991, Kalinin: An epithelium-specific basement membrane adhesion molecule that is a component of anchoring filaments, J. Cell Biol. 114:567–576.

    PubMed  CAS  Google Scholar 

  • Ruoslahti, E., 1991, Integrins, J. Clin. Invest. 87:1–5.

    PubMed  CAS  Google Scholar 

  • Sastry, S. K., and Horwitz, A. F., 1993, Integrin cytoplasmic domains: Mediators of cytoskeletal linkages and extra-and intracellular initiated transmembrane signaling, Curr. Opin. Cell Biol. 5:819–831.

    PubMed  CAS  Google Scholar 

  • Schaller, M. D., Otey, C. A., Hildebrand, J. D., and Parsons, J. T., 1995, Focal adhesion kinase and paxillin bind to peptides mimicking beta integrin cytoplasmic domains, J. Cell Biol. 130:1181–1187.

    PubMed  CAS  Google Scholar 

  • Schiro, J. A., Chan, B. M., Roswit, W. T., Kassner, P. D., Pentland, A. P., Hemler, M. E., Eisen, A. Z., and Kupper, T. S., 1991, Integrin α2β1 (VLA-2) mediates reorganization and contraction of collagen matrices by human cells, Cell 67:403–410.

    PubMed  CAS  Google Scholar 

  • Schlessinger, J., 1988, Signal transduction by allosteric receptor oligomerization, Trends Biochem. Sci. 13:443–447.

    PubMed  CAS  Google Scholar 

  • Schmidt, C. E., Horwitz, A. F., Lauffenburger, D. A., and Sheetz, M. P., 1993, Integrin-cytoskeletal interactions in migrating fibroblasts are dynamic, asymmetric, and regulated, J. Cell Biol. 123:977–991.

    PubMed  CAS  Google Scholar 

  • Schwartz, M. A., 1993, Spreading of human endothelial cells on fibronectin or vitronectin triggers elevation of intracellular free calcium, J. Cell Biol. 120:1003–1010.

    PubMed  CAS  Google Scholar 

  • Schwartz, M. A., and Denninghoff, K., 1994, αv Integrins mediate the rise in intracellular calcium in endothelial cells on fibronectin even though they play a minor role in adhesion, J. Biol. Chem. 269:11133–11137.

    PubMed  CAS  Google Scholar 

  • Schwartz, M. A., and Lechene, C., 1992, Adhesion is required for protein kinase C-dependent activation of the Na+/H+ antiporter by platelet-derived growth factor, Proc. Natl. Acad. Sci. USA 89:6138–6141.

    PubMed  CAS  Google Scholar 

  • Schwartz, M. A., Ingber, D. E., Lawrence, M., Springer, T., and Lechene, C., 1991a, Multiple integrins share the ability to induce elevation of intracellular pH, Exp. Cell Res. 195:533–535.

    PubMed  CAS  Google Scholar 

  • Schwartz, M. A., Lechene, C., and Ingber, D. E., 1991b, Insoluble fibronectin activates the Na/H antiporter by clustering and immobilizing integrin α1β5, independent of cell shape, Proc. Natl. Acad. Sci. USA 88:7849–7853.

    PubMed  CAS  Google Scholar 

  • Shattil, S. J., and Brugge, J. S., 1991, Protein tyrosine phosphorylation and the adhesive functions of platelets, Curr. Opin. Cell Biol. 3:869–879.

    PubMed  CAS  Google Scholar 

  • Shimizu, Y., Van Seventer, G. A., Horgan, K. J., and Shaw, S., 1990, Regulated expression and binding of three VLA (β1) integrin receptors on T cells, Nature 345:250–253.

    PubMed  CAS  Google Scholar 

  • Singer, I.I., 1979, The fibronexus: A transmembrane association of fibronectin-containing fibers and bundles of 5 nm microfilaments in hamster and human fibroblasts, Cell 16:675–685.

    PubMed  CAS  Google Scholar 

  • Singer, I.I., Kawka, D. W., Kazazis, D. M., and Clark, R. A. F., 1984, In vivo codistribution of fibronectin and actin fibers in granulation tissue: Immunofluorescence and electron microscope studies of the fibronexus at the myofibroblast surface, J. Cell Biol. 98:2091–2106.

    PubMed  CAS  Google Scholar 

  • Smith, J. W., and Cheresh, D. A., 1990, Integrin (αvβ3)-ligand interaction. Identification of a heterodimeric RGD binding site on the vitronectin receptor, J. Biol. Chem. 265:2168–2172.

    PubMed  CAS  Google Scholar 

  • Song, W. K., Wang, W., Sato, H., Bielser, D. A., and Kaufman, S. J., 1993, Expression of α7 integrin cytoplasmic domains during skeletal muscle development: Alternate forms, conformational change, and homologies with serine/threonine kinases and tyrosine phosphatases, J. Cell Sci. 106:1139–1152.

    PubMed  CAS  Google Scholar 

  • Sonnenberg, A., 1993, Integrins and their ligands, Curr. Top. Microbiol. Immunol. 184:7–35.

    PubMed  CAS  Google Scholar 

  • Sonnenberg, A., Linders, C. J. T., Modderman, P. W., Damsky, C. H., Aumailley, M., and Timpl, R., 1990, Integrin recognition of different cell-binding fragments of laminin (P1, E3, E8) and evidence that α6β1 but not α6β4 functions as a major receptor for fragment E8, J. Cell Biol. 110:2145–2155.

    PubMed  CAS  Google Scholar 

  • Springer, T. A., 1994, Traffic signals for lymphocyte recirculation and leukocyte emigration: The multistep paradigm, Cell 76:301–314.

    PubMed  CAS  Google Scholar 

  • Staatz, W. D., Fok, K. F., Zutter, M. M., Adams, S. P., Rodriguez, B. A., and Santoro, S. A., 1991, Identification of a tetrapeptide recognition sequence for the α2β1 integrin in collagen, J. Biol. Chem. 266:7363–7367.

    PubMed  CAS  Google Scholar 

  • Stanley, J. R., Alvarez, O. M., Bere, E. W., Eaglstein, W. H., and Katz, S. I., 1981, Detection of membrane zone antigens during epidermal wound healing in pigs, J. Invest. Dermatol. 7:240–243.

    Google Scholar 

  • Stanley, P., Bates, P. A., Harvey, J., Bennett, R. I., and Hogg, N., 1994, Integrin LFA-1 alpha subunit contains an ICAM-1 binding site in domains V and VI, EMBO J. 13:1790–1798.

    PubMed  CAS  Google Scholar 

  • Staquet, M. J., Levarlet, B., Dezutter-Dambuyant, C., Schmitt, D., and Thivolet, J., 1990, Identification of specific human epithelial cell integrin receptors as VLA proteins, Exp. Cell Res. 187:277–283.

    PubMed  CAS  Google Scholar 

  • Stenn, K. S., 1981, Epibolin: A protein of human plasma that supports epithelial cell movement, Proc. Natl. Acad. Sci. USA 78:6907–6911.

    PubMed  CAS  Google Scholar 

  • Stenn, K. S., 1987, Coepibolin, the activity of human serum that enhances the cell-spreading properties of epibolin, associates with albumin, J. Invest. Dermatol. 89:59–63.

    PubMed  CAS  Google Scholar 

  • Stepp, M. A., Spurr-Michaud, S., Tisdale, A., Elwell, J., and Gipson, I. K., 1990, α6β4 Integrin heterodimer is a component of hemidesmosomes, Proc. Natl. Acad. Sci. USA 87:8970–8974.

    PubMed  CAS  Google Scholar 

  • Stepp, M. A., Spurr-Michaud, S., and Gipson, I. K., 1993, Integrins in the wounded and unwounded stratified squamous epithelium of the cornea, Invest. Ophthalmol. Vis. Sci. 34:1829–1844.

    PubMed  CAS  Google Scholar 

  • Streuli, C. H., Bailey, N., and Bissell, M. J., 1991, Control of mammary epithelial differentiation: Basement membrane induces tissue-specific gene expression in the absence of cell-cell interaction and morphological polarity, J. Cell Biol. 115:1383–1395.

    PubMed  CAS  Google Scholar 

  • Suzuki, S., Huang, Z.-S., and Tanihara, H., 1990, Cloning of an integrin β subunit exhibiting high homology with integrin β3 subunit, Proc. Natl. Acad. Sci. USA 87:5354–5358.

    PubMed  CAS  Google Scholar 

  • Symington, B. E., 1990, Fibronectin receptor overexpression and loss of transformed phenotype in a stable variant of the K562 cell line, Cell. Regul. 1:637–648.

    PubMed  CAS  Google Scholar 

  • Symington, B. E., 1992, Fibronectin receptor modulates cyclin-dependent kinase activity, J. Biol. Chem. 267:25744–25747.

    PubMed  CAS  Google Scholar 

  • Symington, B. E., Takada, Y., and Carter, W. G., 1993, Interaction of integrins α3βl and α2β1: Potential role in keratinocyte intercellular adhesion, J. Cell Biol. 120:523–535.

    PubMed  CAS  Google Scholar 

  • Takada, Y., Ylanne, J., Mandelman, D., Puzon, W., and Ginsberg, M. H., 1992, A point mutation of integrin β1 subunit blocks binding of α5β1 to fibronectin and invasin but not recruitment to adhesion plaques, J. Cell Biol. 119:913–921.

    PubMed  CAS  Google Scholar 

  • Tamura, R. N., Rozzo, C., Starr, L., Chambers, J., Reichardt, L. F., Cooper, H. M., and Quaranta, V., 1990, Epithelial integrin α6β4: Complete primary structure of α6 and variant forms of β4, J. Cell Biol. 111:1593–1604.

    PubMed  CAS  Google Scholar 

  • Tapley, P., Horwitz, A., Buck, C., Duggan, K., and Rohrschneider, L., 1989, Integrins isolated from Rous sarcoma virus-transformed chicken embryo fibroblasts, Oncogene 4:325–333.

    PubMed  CAS  Google Scholar 

  • Tenchini, M. L., Adams, J. C., Gilbert, C., Steel, J., Hudson, D. L., Malcovati, M., and Watt, R M., 1993, Evidence against a major role for integrins in calcium-dependent intercellular adhision of epidermal keratinocytes, Cell Adhesion Commun. 1:55–66.

    CAS  Google Scholar 

  • Tervo, T., van Setten, G. B., Paallysaho, T., Tarkkanen, A., and Tervo, K., 1992, Wound healing of the ocular surface, Ann. Med. 24:19–27.

    PubMed  CAS  Google Scholar 

  • Toda, K.-I., Tuan, T.-L., Brown, P. J., and Grinnell, F., 1987, Fibronectin receptors of human keratinocytes and their expression during cell culture, J. Cell Biol. 105:3097–3104.

    PubMed  CAS  Google Scholar 

  • Tuckwell, D. S., Brass, A., and Humphries, M. J., 1992, Homology modelling of integrin EF-hands. Evidence for widespread use of a conserved cation-binding site, Biochem. J. 285:325–331.

    PubMed  CAS  Google Scholar 

  • Tuckwell, D. S., Weston, S. A., and Humphries, M. J., 1993, Integrins: A review of their structure and mechanisms of ligand binding, Symp. Soc. Exp. Biol. 47:107–136.

    PubMed  CAS  Google Scholar 

  • Tuckwell, D. S., Ayad, S., Grant, M. E., Takigawa, M., and Humphries, M. J., 1994, Conformation dependence of integrin-type II collagen binding. Inability of collagen peptides to support α2β1 binding, and mediation of adhesion to denatured collagen by a novel α5β1-fibronectin bridge, J. Cell Sci. 107(Pt 4):993–1005.

    PubMed  CAS  Google Scholar 

  • Turner, C. E., and Burridge, K., 1991, Transmembrane molecular assemblies in cell-extracellular matrix interactions, Curr. Opin. Cell. Biol. 3:849–853.

    PubMed  CAS  Google Scholar 

  • Wayner, E. A., Orlando, R. A., and Cheresh, D. A., 1991, Integrins αvβ3 and αvβ5 contribute to cell attachment to vitronectin but differentially distribute on the cell surface, J. Cell Biol. 113:919–929.

    PubMed  CAS  Google Scholar 

  • Welch, M. P., Odland, G. F., and Clark, R. A. F., 1990, Temporal relationships of F-actin bundle formation, collagen and fibronectin matrix assembly, and fibronectin receptor expression to wound contraction, J. Cell Biol. 110:133–145.

    PubMed  CAS  Google Scholar 

  • Wenczak, B. A., Lynch, J. B., and Nanney, L. B., 1992, Epidermal growth factor receptor distribution in bum wounds. Implications for growth factor-mediated repair, J. Clin. Invest. 90:2392–2401.

    PubMed  CAS  Google Scholar 

  • Werb, Z., Tremble, P. M., Behrendtsen, O., Crowley, E., and Damsky, C. H., 1989, Signal transduction through the fibronectin receptor induces collagenase and stromelysin gene expression, J. Cell Biol. 109:877–889.

    PubMed  CAS  Google Scholar 

  • Wilke, M. S., and Skubitz, A. P. N., 1991, Human keratinocytes adhere to multiple distinct peptide sequences of laminin, J. Invest. Dermatol. 97:141–146.

    PubMed  CAS  Google Scholar 

  • Yamada, K. M., 1991, Adhesive recognition sequences, J. Biol. Chem. 266:12809–12812.

    PubMed  CAS  Google Scholar 

  • Yamada, K. M., Aota, S., Akiyama, S. K., and LaFlamme, S. E., 1992, Mechanisms of fibronectin and integrin function during cell adhesion and migration, Cold Spring Harb. Symp. Quant. Biol. 57:203–212.

    PubMed  CAS  Google Scholar 

  • Ylanne, J., Chen, Y., O’Toole, T. E., Loftus, J. C., Takada, Y., and Ginsberg, M. H., 1993, Distinct functions of integrin a and β subunit cytoplasmic domains in cell spreading and formation of focal adhesions, J. Cell Biol. 122(1):223–233.

    PubMed  CAS  Google Scholar 

  • Zambruno, G., Marchisio, P. C., Marconi, A., Vaschieri, C., Melchiori, A., Giannetti, A., and De Luca M., 1995, Transforming growth factor-β1 modulates β1 and β5 integrin receptors and induces the de novo expression of the αvβ6 heterodimer in normal human keratinocytes: Implications for wound healing, J. Cell Biol. 129:853–865.

    PubMed  CAS  Google Scholar 

  • Zetter, B. R., 1993, Adhesion molecules in tumor metastasis, Semin. Cancer Biol. 4:219–229.

    PubMed  CAS  Google Scholar 

  • Zheng, M., Fang, H., and Hakomori, S., 1994, Functional role of N-glycosylation in α5β1 integrin receptor. De-N-glycosylation induces dissociation or altered association of α5β1 subunits and concomitant loss of fibronectin binding activity, J. Biol. Chem. 269:12325–12331.

    PubMed  CAS  Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Editor information

Editors and Affiliations

Rights and permissions

Reprints and permissions

Copyright information

© 1988 Springer Science+Business Media New York

About this chapter

Cite this chapter

Yamada, K.M., Gailit, J., Clark, R.A.F. (1988). Integrins in Wound Repair. In: Clark, R.A.F. (eds) The Molecular and Cellular Biology of Wound Repair. Springer, Boston, MA. https://doi.org/10.1007/978-1-4899-0185-9_9

Download citation

  • DOI: https://doi.org/10.1007/978-1-4899-0185-9_9

  • Publisher Name: Springer, Boston, MA

  • Print ISBN: 978-1-4899-0187-3

  • Online ISBN: 978-1-4899-0185-9

  • eBook Packages: Springer Book Archive

Publish with us

Policies and ethics