Download PDF
Thromb Haemost 1995; 74(03): 813-821
DOI: 10.1055/s-0038-1649829
Review Article
Schattauer GmbH Stuttgart

The α2β1 Integrin: A Collagen Receptor on Platelets and other Cells

Samuel A Santoro
The Department of Pathology, Washington University School of Medicine, St. Louis, MO, USA
,
Mary M Zutter
The Department of Pathology, Washington University School of Medicine, St. Louis, MO, USA
› Author Affiliations
Further Information

Publication History

Received 17 June 1994

Accepted after resubmission 09 May 1995

Publication Date:
09 July 2018 (online)

Also available at
  PDF Download  Permissions and Reprints
 

  • References

  • 1 Baumgartner HR. Platelet interaction with collagen fibrils in flowing blood. I. Reaction of human platelets with α-chymotrypsin-digested subendothelium Thromb Haemost 1977; 37: 1-16
    Article in Thieme ConnectPubMedGoogle Scholar
  • 2 Santoro SA. In: Platelet Membrane Receptors: Molecular Biology, Immunology, Biochemistry and Pathology. Jamieson GA. ed Alan R. Liss, Inc; New York: 1988. pp 291-314
    Google Scholar
  • 3 Weiss HJ, Turitto VT, Baumgartner HR. Effect of shear rate oil platelet interaction with subendothelium in citrated and native blood. I. Shear rate-dependent decrease of adhesion in von Willebrand’s disease and the Bernard-Soulier syndrome J Lab Clin Med 1978; 92: 750-764
    PubMedGoogle Scholar
  • 4 Houdijk WP M, Sakariassen KS, Nievelstein PF E M, Sixma J. Role of factor VIII von Willebrand factor and fibronectin in the interaction of platelets in flowing blood with monomeric and fibrillar collagen types I and II. J Clin Invest 1985; 75: 531-540
    CrossrefPubMedGoogle Scholar
  • 5 Baumgartner HR, Tschopp TB, Meyer D. Shear rate dependent inhibition of platelet adhesion and aggregation on collagenous surfaces by antibodies to human factor. Br.J Haematol 1980; 44: 127-139
    CrossrefPubMedGoogle Scholar
  • 6 Spaet TH, Lejnieks I. A technique for estimation of platelet collagen adhesion. Proc Soe Exp Biol 1969; 132: 1038-1041
    PubMedGoogle Scholar
  • 7 Albelda SM, Buch CA. Integrins and other cell adhesion molecules. FASEB J 1990; 4: 2868-2880
    CrossrefPubMedGoogle Scholar
  • 8 Hemler ME. VLA proteins in the integrin family: Structures, functions, and their role on leukocytes. Ann Rev Immunol 1990; 80: 365-400
    PubMedGoogle Scholar
  • 9 Ruoslahti E. Integrins. J Clin Invest 1991; 87: 1-5
    CrossrefPubMedGoogle Scholar
  • 10 Hynes RO. Integrins: Versatility, modulation, and signalling in cell adhesion. Cell 1992; 69: 11-25
    CrossrefPubMedGoogle Scholar
  • 11 Argraves WS, Suzuki S, Arai H, Thompson K, Pierschbacher MD, Ruoslahti E. Amino acid sequence of the human fibronectin receptor. J Cell Biol 1987; 105: 1183-1190
    CrossrefPubMedGoogle Scholar
  • 12 Altruda F, Cervella P, Tarone G, Balzac F, Stefanuto G, Silengo L. A human β1 integrin subunit with a unique cytoplasmic domain generated by alternative RNA processing. Gene 1990; 95: 261-266
    CrossrefPubMedGoogle Scholar
  • 13 Languino LR, Ruoslahti E. An alternative form of the integrin β1 subunit with a variant cytoplasmic domain. J Biol Chem 1992; 267: 7116-7120
    PubMedGoogle Scholar
  • 14 Takada Y, Ylanne J, Mandelman D, Puzon W, Ginsberg MH. A point mutation of integrin β1 subunit blocks binding of α5β1 to fibronectin and invasin but not recruitment to adhesion plaques. J Cell Biol 1992; 119: 913-921
    CrossrefPubMedGoogle Scholar
  • 15 Lee JO, Rieu P, Arnaout MA, Liddington R. Crystal structure of the A domain from the α subunit of integrin CR3 (CD11b/CDl8). Cell 1995; 80: 631-638
    CrossrefPubMedGoogle Scholar
  • 16 Takada Y, Puzon W. Identification of a regulatory region of integrin β1 subunit using activating and inhibiting antibodies. J Biol Chem 1993; 268: 17597-17601
    PubMedGoogle Scholar
  • 17 Otey CA, Pavalko FM, Burridge K. An interaction between α-actinin and the β1 integrin subunit in vitro. J Cell Biol 1990; 111: 721-729
    CrossrefPubMedGoogle Scholar
  • 18 Kieffer N, Guichard J, Breton-Gorius J. Dynamic redistribution of major platelet surface receptors after contact-induced platelet activation and spreading - An immunoelection microscopy study. Am J Pathol 1992; 140: 57-73
    PubMedGoogle Scholar
  • 19 Fox JE B. Linkage of a membrane skeleton to integral membrane glycoproteins in human platelets. Identification of one of the glycoproteins asglycoprotein Ib J Clin Invest 1985; 76: 1673-1683
    CrossrefPubMedGoogle Scholar
  • 20 Bienz D, Clemetson KJ. Human platelet glycoprotein la-One component is only expressed on the surface of activated platelets and may be a granule constituent. J Biol Chem 1989; 264: 507-514
    PubMedGoogle Scholar
  • 21 Takada Y, Hemler ME. The primary structure of the VLA-2/collagen receptor a2 subunit (platelet GPIa): Homology to other integrins and the presence of a possible collagen-binding domain. J Cell Biol 1989; 109: 397-407
    CrossrefPubMedGoogle Scholar
  • 22 Ignatius MJ, Large TH, Houde M, Tawil JW, Barton A, Esch F, Carbonetto S, Reichardt LF. Molecular cloning of the rat integrin α1-subunit: A receptor for laminin and collagen. J Cell Biol 1990; 111: 709-720
    CrossrefPubMedGoogle Scholar
  • 23 D’Souza SE, Ginsberg MH, Burke TA, Plow EF. The ligand binding site of the platelet integrin receptor GP IIb-IIIa is proximal to the second calcium binding domain of its α subunit. J Biol Chem 1990; 265: 3440-3446
    PubMedGoogle Scholar
  • 24 Smith JW, Cheresh DA. Integrin (αvβ3)-ligand interaction. J Biol Chem 1990; 265: 2168-2172
    PubMedGoogle Scholar
  • 25 Kamata T, Puzon W, Takada Y. Identification of putative ligand binding sites within I domain of integrin α2β1(VLA-2, CD49b/CD29) . J Biol Chem 1994; 269: 9659-9663
    PubMedGoogle Scholar
  • 26 Ueda T, Rieu P, Brayer J, Amaout MA. Identification of the complement iC3b binding site in the β2 integrin CR3 (CD1lb/CD18). Proc Natl Acad Sci USA 1994; 91: 10680-10684
    CrossrefPubMedGoogle Scholar
  • 27 Bahou WF, Potter CL, Mirza H. The VLA-2 (a2β1) I domain functions as a ligand-specific recognition sequence for endothelial cell attachment and spreading: Molecular and fuctional characterization. Blood 1994; 84: 3734-3741
    PubMedGoogle Scholar
  • 28 Kamata T, Takada Y. Direct binding of collagen to the I domain of integrin α2β1j(VLA-2, CD49b/CD29) in a divalent cation-independent manner. J Biol Chem 1994; 269: 26006-26010
    PubMedGoogle Scholar
  • 29 Michishita M, Videm V, Arnaout MA. A novel divalent cation-binding site in the A domain of the β2 integrin CR3 (CD1lb/CD18) is essential for ligand binding. Cell 1993; 72: 857-867
    CrossrefPubMedGoogle Scholar
  • 30 Chan BM C, Kassner PD, Schiro JA, Byers HR, Kupper TS, Hemler ME. Distinct cellular functions mediated by different VLA integrin α subunit cytoplasmic domains. Cell 1992; 68: 1051-1060
    CrossrefPubMedGoogle Scholar
  • 31 Kawaguchi S, Hemler ME. Role of the α subunit cytoplasmic domain in the regulation of adhesive activity mediated by the integrin VLA-2. J Biol Chem 1993; 268: 16279-16285
    PubMedGoogle Scholar
  • 32 Kassner PD, Kawaguchi S, Hemler ME. Minimum a chain cytoplasmic tail sequence needed to support integrin mediated adhesion. J Biol Chem 1994; 269: 19859-19867
    PubMedGoogle Scholar
  • 33 Dedhar S. Novel functions for calreticulin: interaction with integrins and modulation of gene expression. Trends Biochem Sci 1994; 19: 269-271
    CrossrefPubMedGoogle Scholar
  • 34 Leung-Hagesteijn CY, Milankov K, Michalak M, Williams J, Dedhar S. Cell attachment to extracellular matrix substrates is inhibited upon down regulation of calreticulin, an intracellular integrin α-subunit-binding protein. J Cell Sci 1994; 107: 589-600
    PubMedGoogle Scholar
  • 35 Wu JE, Santoro SA. Complex patterns of expression suggest extensive roles for the α2β1 integrin in murine development. Dev Dynamics 1994; 199: 292-314
    CrossrefPubMedGoogle Scholar
  • 36 Kaplan C, Morell-Kopp MC, Kroll H, Kiefel V, Schlegel N, Chesnel N, Mueller-Eckhardt C. HPA-5b (Bra) neonatal alloimmune thrombocytopenia: Clinical and immunological analysis of 39 cases. Br J Haematol 1991; 78: 425-429
    CrossrefPubMedGoogle Scholar
  • 37 Kiefel V, Schechter Y, Atias D, Santoso S, Mueller-Eckardt C. Neonatal alloimmune thrombocytopenia due to anti-Brb(HPA-5a). Vox Sang 1991; 60: 244-245
    PubMedGoogle Scholar
  • 38 Bettaieb A, Fromont P, Rodet M, Godeau B, Duedari N, Bierling P. Brb,a platelet alloantigen involvedin neonatal alloimmune thrombocytopenia. Vox Sang 1991; 60: 230-234
    PubMedGoogle Scholar
  • 39 Bierling P, Fromont P, Bettaieb A, Duedari N. Anti-Bra antibodies in the French population. Br J Haematol 1989; 73: 428-429
    CrossrefPubMedGoogle Scholar
  • 40 Christie DJ, Pulkrabek S, Putnam JL, Slatoff ML, Pischel KD. Posttransfusion purpura due to alloantibody reactive with glycoprotein Ia/IIa (Anti- HPA-5b). Blood 1991; 77: 2785-2789
    PubMedGoogle Scholar
  • 41 Warkentin TE, Smith JW, Hayward CP M, Ali AM, Kelton JG. Thrombocytopenia caused by passive transfusion of antiglycoprotein Ia/IIa alloantibody (Anti-HPA-5b). Blood 1992; 79: 2480-2484
    PubMedGoogle Scholar
  • 42 Kiefel V, Santoso S, Weisheit M, Mueller-Eckhardt C. The Bra/Brb alloantigen system on human platelets. Blood 1989; 733: 2219-2223
    PubMedGoogle Scholar
  • 43 Santoso S, Kalb R, Walka M, Kiefel V, Mueller-Eckhardt C, Newman PJ. The human platelet alloantigens Bra and Brb are associated with a single amino acid polymorphism on glycoprotein Ia (integrin subunit α2). J Clin Invest 1993; 92: 2427-2432
    CrossrefPubMedGoogle Scholar
  • 44 Chan BM C, Hemler ME. Multiple functional forms of the integrin VLA-2 can be derived from a single α2cDNA clone: Interconversion of forms induced by an anti-β1antibody. J Cell Biol 1993; 120: 537-543
    CrossrefPubMedGoogle Scholar
  • 45 Pullman WE, Bodmer WF. Cloning and characterization of a gene that regulates cell adhesion. Nature 1992; 356: 529-532
    CrossrefPubMedGoogle Scholar
  • 46 Kainoh M, Ikeda Y, Nishio S, Nakadate T. Glycoprotein Ia/IIa-mediated activation-dependent platelet adhesion to collagen. Thromb Res 1992; 65: 165-176
    CrossrefPubMedGoogle Scholar
  • 47 Coller BS, Beer JH, Scudder LE, Steinberg MH. Collagen-platelet interaction: Evidence for a direct interaction of collagen with platelet GPI/IIa and an indirect interaction with platelet GPIIb/IIIa mediated by adhesive proteins. Blood 1989; 74: 182-192
    PubMedGoogle Scholar
  • 48 Shadle PJ, Barondes SH. Adhesion of human platelets to immobilized trimeric collagen. J Cell Biol 1982; 95: 361-365
    CrossrefPubMedGoogle Scholar
  • 49 Santoro SA. Identification of a 160,000 dalton platelet membrane protein that mediates the initial divalent cation-dependent adhesion of platelets to collagen. Cell 1986; 46: 913-920
    CrossrefPubMedGoogle Scholar
  • 50 Staatz WD, Rajpara SM, Wayner EA, Carter WG, Santoro SA. The membrane glycoprotein Ia-IIa (VLA-2) complex mediates the Mg++- dependent adhesion of platelets to collagen. J Cell Biol 1989; 108: 1917-1924
    CrossrefPubMedGoogle Scholar
  • 51 Saelman EU M, Nieuwenhuis HK, Hese KM, de Groot Ph G, Heijnen HF G, Sage EH, Williams S, McKeown L, Gralnick HR, Sixma JJ. Platelet adhesion to collagen types I through VIII under conditions of stasis and flow is mediated by GPIa/IIa (α2β1-integrin). Blood 1994; 83: 1244-1250
    PubMedGoogle Scholar
  • 52 Santoro SA, Rajpara SM, Staatz WD, Woods VLJr. Isolation and characterization of a platelet surface collagen binding complex related to VLA-2. Biochem Biophys Res Commun 1988; 153: 217-233
    CrossrefPubMedGoogle Scholar
  • 53 Kunicki TJ, Nurden AT, Pidard D, Russell NR, Caen JP. Characterization of human platelet glycoprotein antigens giving rise to individual immunoprecipitates in crossed-immunoelectrophoresis. Blood 1981; 58: 1190-1197
    PubMedGoogle Scholar
  • 54 Pischel KD, Bluestein HG, Woods VLJr. Platelets glycoproteins la, Ic, and IIa are physicochemically indistinguishable from the very late activation antigens adhesion-related proteins of lymphocytes and other cell types. J Clin Invest 1988; 81: 505-513
    CrossrefPubMedGoogle Scholar
  • 55 Kunicki TJ, Nugent DJ, Staats SJ, Orchekowski RP, Wayner EA, Carter WG. The human fibroblast class II extracellular matrix receptor mediates platelet adhesion to collagen and is identical to the platelet glycoprotein Ia-IIa complex. J Biol Chem 1988; 263: 4516-4519
    PubMedGoogle Scholar
  • 56 Takada Y, Wayner EA, Carter WG, Hemler ME. Extracellular matrix receptors, ECMRII and ECMRI, for collagen and fibronectin correspond to VLA-2 and VLA-3 in the VLA family of heterodimers. J Cell Biochem 1988; 37: 385-393
    CrossrefPubMedGoogle Scholar
  • 57 Staatz WD, Peters KJ, Santoro SA. Divalent cation-dependent structure in the platelet membrane glycoprotein Ia-IIa (VLA-2) complex. Biochem Biophys Res Commun 1990; 168: 107-113
    CrossrefPubMedGoogle Scholar
  • 58 Gralnick HR, McKeown LP, Williams SS, Lawrence JC, Shafer BC, Kramer WS, Hanemann KE, Vail ML, Magruder LE. A murine monoclonal antibody that identifies a157/130 kDa platelet collagen receptor. Circulation 1988; 78 Suppl (Suppl. 02) 308
    PubMedGoogle Scholar
  • 59 Polanowska-Grabowska R, Gear AR L. High-speed platelet adhesion under conditions of rapid flow. Proc Natl Acad Sci USA 1992; 89: 5754-5758
    CrossrefPubMedGoogle Scholar
  • 60 Parmentier S, Catimel B, McGregor L, Leung LL K, McGregor JL. Role of glycoprotein IIa (β1subunit of very late activation antigens) in platelet functions. Blood 1991; 78: 2021-2026
    PubMedGoogle Scholar
  • 61 Haimovich B, Lipfert L, Brugge JS, Shattil SJ. Tyrosine phosphorylation and cytoskeletal reorganization in platelets are triggered by interaction of integrin receptors with their immobilized ligands. J Biol Chem 1993; 268: 15868-15877
    PubMedGoogle Scholar
  • 62 Nieuwenhuis HK, Akkerman JW N, Houdijk WP M, Sixma JJ. Human blood platelets showing no response to collagen fail to express surface glycoprotein Ia. Nature 1985; 318: 470-472
    CrossrefPubMedGoogle Scholar
  • 63 Nieuwenhuis HK, Sakariassen KS, Houdijk WP M, Nievelstein PF M, Sixma JJ. Deficiency of platelet membrane glycoprotein la associated with a decreased platelet adhesion tosubendothelium: A defect in platelet spreading. Blood 1986; 68: 692-695
    PubMedGoogle Scholar
  • 64 Kehrel B, Balleisen L, Kokott R, Mesters R, Stenzinger W, Clemetson KJ, Van deLoo J. Deficiency of intact thrombospondin and membrane glycoprotein la in platelets with defective collagen-induced aggregation and spontaneous loss of disorder. Blood 1988; 71: 1074-1078
    PubMedGoogle Scholar
  • 65 Handa M, Watanabe K, Kawai Y, Kamata T, Koyama T, Nagai H, Ikeda Y. Platelet unresponsiveness to collagen: Involvement of glycoprotein Ia-IIa (α2β1-integrin) deficiency associated with a myeloproliferative disorder. Thromb Haemost 1995; 73: 521-528
    Article in Thieme ConnectPubMedGoogle Scholar
  • 66 Deckmyn H, Chew SL, Vermylen J. Lack of platelet response to collagen associated with an autoantibody against glycoprotein la: Anovel cause of acquired qualitative platelet dysfunction. Thromb Haemost 1990; 64: 74-79
    Article in Thieme ConnectPubMedGoogle Scholar
  • 67 Karniguian A, Legrand YJ, Lefraneier P, Caen JP. Effect of collagen- derived octapcptide on different steps of the platelet/collagcn interaction. Thromb Res 1983; 32: 592-604
    PubMedGoogle Scholar
  • 68 Morton LF, Peachey AR, Barnes MJ. Platelet reactive sites in collagens type I and type III. Evidence for separate adhesion and aggregatory sites Biochem J 1989; 258: 157-163
    CrossrefPubMedGoogle Scholar
  • 69 Santoro SA, Walsh JJ, Staatz WD, Baranski KJ. Distinct determinants on collagen support α2β1 integrin-mediated platelets adhesion and platelet activation. Cell Regulation 1991; 2: 905-913
    CrossrefPubMedGoogle Scholar
  • 70 Cardarelli PM, Yamagata S, Taguchi I, Gorcsan F, Chiang SL, Lobl T. The collagen receptor α2β1,from MG-63 and HTI080 cells, interacts with a cyclic RGD peptide. J Biol Chem 1992; 267: 23159-23164
    PubMedGoogle Scholar
  • 71 Staat WD, Walsh JJ, Pexton T, Santoro SA. The 2β1 integrin cell surface collagen receptor binds to the α1(l)-CB3 peptide of collagen. J Biol Chem 1990; 265: 4778-4781
    PubMedGoogle Scholar
  • 72 Schiro JA, Chan BM C, Roswit WT, Kassner PD, Pentland AP, Hemler ME, Eisen AZ, Kupper TS. Integrin α2β1(VLA-2) mediates reorganization and contractionof collagen matrices by human cells. Cell 1991; 67: 403-410
    CrossrefPubMedGoogle Scholar
  • 73 Gullberg D, Tuner DC, Borg TK, Terracio L, Rubin K. Different β1integrin collagen receptors on rat hepatoeytes and cardiac fibroblasts. Exp Cell Res 1990; 190: 254-264
    CrossrefPubMedGoogle Scholar
  • 74 Gullberg D, Gehlsen KR, Turner DC, Ahlen K, Zijenah LS, Barnes MJ, Rubin K. Analysis of α1β1,α2β1 and α3β1 integrins in cell-collagen interactions: Identification of conformation dependent α1β1 binding sites in collagen type I. EMBO J 1992; 11: 3865-3873
    PubMedGoogle Scholar
  • 75 Saelman EU M, Horton LF, Barnes MJ, Gralnick HR, Hese KM, Nieuwenhuis HK, de Groot Ph G, Sixma JJ. Platelet adhesion to cyanogen- bromide fragments of collagen α1(1) under flow conditions. Blood 1993; 82: 3029-3033
    PubMedGoogle Scholar
  • 76 Staatz WD, Fok KF, Zutter MM, Adams SP, Rodriquez BA, Santoro SA. Identification of a tetrapeptide recognition sequence for the α2β1 integrin incollagen. J Biol Chem 1991; 266: 7363-7367
    PubMedGoogle Scholar
  • 77 Morton LF, Peachey AR, Zijenah LS, Goodall AH, Humphries MJ, Barnes MJ. Conformation-dependent platelet adhesion to collagen involving integrin α2β1-mediated and other mechanisms: multiple α2β1, recognition sites in collagen type I. Biochem J 1994; 299: 791-797
    CrossrefPubMedGoogle Scholar
  • 78 Tuckwell DS, Ayad S, Grant ME, Takigawa M, Humphries MJ. 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 α5β1fibronectin bridge. J Cell Science 1994; 107: 993-1005
    PubMedGoogle Scholar
  • 79 Vandenberg P, Kern A, Ries A, Luckenbill-Edds L, Mann K, Kühn K. Characterization of a type IV collagen major cell binding site with affinity to the α1β1 and the α2β2 integrins. J Cell Biol 1991; 113: 1475-1483
    CrossrefPubMedGoogle Scholar
  • 80 Weston SA, Hulmes DJ S, Mould AP, Watson RB, Humphries MJ. Identification of integrin α2β1 as cell surface receptor for the carboxyl-terminal propeptide of type I procollagen. J Biol Chem 1994; 269: 20982-20986
    PubMedGoogle Scholar
  • 81 Zutter MM, Santoro SA. Widespread histologic distribution of the α2β1 integrin cell-surface collagen receptor. Am J Pathol 1990; 137: 113-120
    PubMedGoogle Scholar
  • 82 Chan BM C, Matsuura N, Takada Y, Zetter BR, Hemler ME. In vitro and vivo consequences of VLA-2 expression on rhabdomyosarcoma cells. Science 1991; 251: 1600-1602
    CrossrefPubMedGoogle Scholar
  • 83 Keely PJ, Fong AM, Zutter MM, Santoro SA. Alteration of collagen- dependent adhesion, motility, and morphogenesis by the expression of antisense α2 integrin mRNA in mammary cells. J Cell Sci 1995; 108: 595-607
    PubMedGoogle Scholar
  • 84 Zutter MM, Santoro SA, Staatz WD, Tsung YL. Re-expression of α2β1 integrin abrogates the malignant phenotype of breast carcinoma cells. Proc Natl Acad Sci USA. 1995 in press
    PubMedGoogle Scholar
  • 85 Elices MJ, Hemler ME. The human integrin VLA-2 is a collagen receptor on some cells and a collagen/laminin receptor onothers. Proc Natl Acad Sci USA 1989; 86: 9906-9910
    CrossrefPubMedGoogle Scholar
  • 86 Languino LR, Gehlsen KR, Wayner E, Carter WG, Engvall E, Ruoslahti E. Endothelial cells use α2β1 integrin as a laminin receptor. J Cell Biol 1989; 109: 2455-2462
    CrossrefPubMedGoogle Scholar
  • 87 Kirchhofer D, Languino LR, Ruoslahti E, Pierschbacher MD. α2β1integrins from different cell types show different binding specifications. J Biol Chem 1990; 265: 615-618
    PubMedGoogle Scholar
  • 88 Bergelson JM, Shepley MP, Chan BM C, Hemler ME, Finberg RW. Identification of the integrin VLA-2 as a receptor for echovirus. J Science 1992; 255: 1718-1720
    CrossrefPubMedGoogle Scholar
  • 89 Bergelson JM, Chan BM C, Finberg RW, Hemler ME. The integrin VLA-2 binds echovirus I and extracellular matrix ligands by different mechanisms. J Clin Invest 1993; 92: 232-239
    CrossrefPubMedGoogle Scholar
  • 90 Symington BE, Takada Y, Carter WG. Interaction of integrins α3β1 and α2β1 Potential role in keratinocyte intercellular adhesion. J Cell Biol 1993; 120: 523-535
    CrossrefPubMedGoogle Scholar
  • 91 Sriramarao P, Mendler M, Bourdon MA. Endothelial cell attachment and spreading on human tenascin is mediated by α2β1 and αvβ3 integrins. J Cell Sci 1993; 105: 1001-1012
    PubMedGoogle Scholar
  • 92 Kunicki TJ, Orchekowski R, Annis D, Honda Y. Variability of integrin α2β1 activity on human platelets. Blood 1993; 82: 2693-2703
    PubMedGoogle Scholar
  • 93 Burger SR, Zutter MM, Sturgill-Koszycki S, Santoro SA. Increased cell surface expression of functional α2β1 integrin accompanies the mega- karyocytic differentiation of K562 leukemia cells. Exp Cell Res 1992; 28-35
    PubMedGoogle Scholar
  • 94 Lozzio CB, Lozzio BB. Human chronic myelogenous leukemia cell-line with positive Philadelphia chromosome. Blood 1975; 45: 321-324
    CrossrefPubMedGoogle Scholar
  • 95 Leary JF, Ohlsson-Wilhelm BM, Giuliano R, LaBella S, Darley B, Rowley PT. Multipotent human hematopoietic cell line K562:Lineage- specific constitutive and inducible antigens. Leuk Res 1987; 11: 807-815
    CrossrefPubMedGoogle Scholar
  • 96 Zutter MM, Fong AM, Krigman HR, Santoro SA. Differential regulation of the α2β1 and αllbβ3integrin genes during megakaryocytic differentiation of pluripotent K562 leukemia cells . J Biol Chem 1992; 267: 20233-20238
    PubMedGoogle Scholar
  • 97 Zutter MM, Santoro SA, Painter AS, Tsung YL, Gafford A. The human α2integrin gene promoter:Identification of positive and negative regulatory elements important for cell-type and developmentally-restricted gene expression . J Biol Chem 1994; 269: 463-469
    PubMedGoogle Scholar
  • 98 Birkenmeier TM, McQuillan JJ, Boedeker ED, Argaves WS, Ruoslahti E, Dean DC. The α5β1fibronectin receptor: Characterization of the α5 gene promoter. J Biol Chem 1991; 266: 20544-20549
    PubMedGoogle Scholar
  • 99 Prandini MH, Uzan G, Martin F, Thevenon D, Marguerie G. Characterization of a specific erythromegakaryocytic enhancer with the glycoprotein llb promoter. J Biol Chem 1992; 267: 10370-10374
    PubMedGoogle Scholar
  • 100 Hickstein DD, Baker DM, Gallahon KA, Back AL. Identification of the promoter of the myelomonocytic leukemia integrin CDIIb. Proc Natl Acad Sci USA 1992; 89: 2105-2109
    CrossrefPubMedGoogle Scholar
  • 101 Lopez-Cabrera M, Nueda A, Vera A, Garcia-Aguilar J, Tugores A, Corbi AL. Characterization of the p150, 95 leukocyte integrin α subunit (CD11c) gene promoter. J Biol Chem 1993; 268: 1187-1193
    PubMedGoogle Scholar
  • 102 Smale ST, Baltimore D. The ”Initiator” as a transcription control element. Cell 1989; 57: 103-113
    CrossrefPubMedGoogle Scholar
  • 103 Dynan WS, Tijan R. The promoter-specific transcription factor Splbinds to upstream sequences in the SV40 early promoter. Cell 1983; 35: 79-87
    CrossrefPubMedGoogle Scholar
  • 104 Spanopoulou E, Giguere V, Grosveld F. The functional domains of the murine ”Thy-1” gene promoter . Mol Cell Biol 1991; 11: 2216-2228
    CrossrefPubMedGoogle Scholar
  • 105 Zutter MM, Painter AD, Staatz WD, Tsung YL. Regulation of α2 integrin gene expression in cells with megakaryocytic features: A common theme of three necessary elements. Blood. 1995 in press
    PubMedGoogle Scholar