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PMID: 2164774 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Widespread histologic distribution of the alpha 2 beta 1 integrin cell-surface collagen receptor.

The American journal of pathology ·Vol. 137 ·No. 1 ·1990-07-00 ·Pages 113-20

Zutter MM, Santoro SA

Abstract

The alpha 2 beta 1 integrin (platelet membrane glycoprotein Ia-IIa, VLA-2, ECMR-II) functions as a cell surface receptor for collagen. The authors have determined the histologic distribution of the alpha 2 beta 1 receptor in normal tissues by immunohistochemical technique. The studies revealed that the alpha 2 beta 1 receptor was expressed on fibroblasts, endothelial cells, and epithelial cells from multiple sites including skin, tonsil, breast, sweat gland, gastrointestinal tract, lung, bladder, cervix, and prostate. Follicular dendritic cells of the lymph node, tonsil, and spleen and dendritic cells of the thymus also expressed the alpha 2 beta 1 receptor. The receptor also was present on Schwann cells of ganglia and on neuroglia. Greatly enhanced expression of the receptor in regions of proliferating epithelium suggests that enhanced expression of alpha 2 beta 1 is associated with orderly, regulated cell proliferation. The circumferential staining pattern of the alpha 2 beta 1 integrin within many epithelia is virtually identical to that observed for other adhesive receptors, such as the cadherins, which have been implicated in cell-cell adhesion.

MeSH Terms
Cell Adhesion Humans Immunohistochemistry Integrins/analysis Receptors, Cell Surface/analysis Receptors, Collagen
Chemicals
Integrins Receptors, Cell Surface Receptors, Collagen
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Zutter M M
Department of Pathology, Washington University, School of Medicine, St. Louis, Missouri 63110.
Santoro S A
References (25)
25 references, click to expand
  1. Progression of type II cell hypertrophy and hyperplasia during silica-induced pulmonary inflammation.
    Lab Invest. 1987 Nov;57(5):546-54 PMID: 2824924
  2. Identification of multiple cell adhesion receptors for collagen and fibronectin in human fibrosarcoma cells possessing unique alpha and common beta subunits.
    J Cell Biol. 1987 Oct;105(4):1873-84 PMID: 2822727
  3. Platelet glycoproteins Ia, 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 Feb;81(2):505-13 PMID: 3276732
  4. 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 Apr 5;263(10):4516-9 PMID: 2832397
  5. Isolation and characterization of a platelet surface collagen binding complex related to VLA-2.
    Biochem Biophys Res Commun. 1988 May 31;153(1):217-23 PMID: 2837201
  6. 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 Aug;37(4):385-93 PMID: 2458366
  7. The function of multiple extracellular matrix receptors in mediating cell adhesion to extracellular matrix: preparation of monoclonal antibodies to the fibronectin receptor that specifically inhibit cell adhesion to fibronectin and react with platelet glycoproteins Ic-IIa.
    J Cell Biol. 1988 Nov;107(5):1881-91 PMID: 2846588
  8. Human vascular endothelial cells express a membrane protein complex immunochemically indistinguishable from the platelet VLA-2 (glycoprotein Ia-IIa) complex.
    Blood. 1989 Apr;73(5):1235-41 PMID: 2930838
  9. Cadherin cell-adhesion molecules in human epithelial tissues and carcinomas.
    Cancer Res. 1989 Apr 15;49(8):2128-33 PMID: 2702654
  10. The membrane glycoprotein Ia-IIa (VLA-2) complex mediates the Mg++-dependent adhesion of platelets to collagen.
    J Cell Biol. 1989 May;108(5):1917-24 PMID: 2715183
  11. A novel integrin (alpha E beta 4) from human epithelial cells suggests a fourth family of integrin adhesion receptors.
    EMBO J. 1989 Mar;8(3):673-80 PMID: 2542022
  12. Identification and characterization of cell-substratum adhesion receptors on cultured human endothelial cells.
    J Clin Invest. 1989 Jun;83(6):1992-2002 PMID: 2786007
  13. Isolated human follicular dendritic cells display a unique antigenic phenotype.
    J Exp Med. 1989 Jun 1;169(6):2043-58 PMID: 2471772
  14. The primary structure of the VLA-2/collagen receptor alpha 2 subunit (platelet GPIa): homology to other integrins and the presence of a possible collagen-binding domain.
    J Cell Biol. 1989 Jul;109(1):397-407 PMID: 2545729
  15. Collagen-platelet interactions: evidence for a direct interaction of collagen with platelet GPIa/IIa and an indirect interaction with platelet GPIIb/IIIa mediated by adhesive proteins.
    Blood. 1989 Jul;74(1):182-92 PMID: 2546619
  16. Use of avidin-biotin-peroxidase complex (ABC) in immunoperoxidase techniques: a comparison between ABC and unlabeled antibody (PAP) procedures.
    J Histochem Cytochem. 1981 Apr;29(4):577-80 PMID: 6166661
  17. Very late activation antigens on rheumatoid synovial fluid T lymphocytes. Association with stages of T cell activation.
    J Clin Invest. 1986 Sep;78(3):696-702 PMID: 3018043
  18. Identification of a 160,000 dalton platelet membrane protein that mediates the initial divalent cation-dependent adhesion of platelets to collagen.
    Cell. 1986 Sep 12;46(6):913-20 PMID: 3757029
  19. Use of the monoclonal antibody 12F1 to characterize the differentiation antigen VLA-2.
    J Immunol. 1987 Jan 1;138(1):226-33 PMID: 3023488
  20. Integrins: a family of cell surface receptors.
    Cell. 1987 Feb 27;48(4):549-54 PMID: 3028640
  21. Cell matrix adhesion-related proteins VLA-1 and VLA-2: regulation of expression on T cells.
    J Immunol. 1987 May 1;138(9):2941-8 PMID: 3106495
  22. The lymphocyte function-associated LFA-1, CD2, and LFA-3 molecules: cell adhesion receptors of the immune system.
    Annu Rev Immunol. 1987;5:223-52 PMID: 3109455
  23. Immunocytochemistry of cell surface heparan sulfate proteoglycan in mouse tissues. A light and electron microscopic study.
    J Histochem Cytochem. 1987 Oct;35(10):1079-88 PMID: 2957423
  24. New perspectives in cell adhesion: RGD and integrins.
    Science. 1987 Oct 23;238(4826):491-7 PMID: 2821619
  25. Cell surface receptors for extracellular matrix molecules.
    Annu Rev Cell Biol. 1987;3:179-205 PMID: 2825736
Article Info
Journal
The American journal of pathology
Abbr.
Am J Pathol
ISSN
0002-9440
Published
1990-07-00
Pages
113-20
Language
English
Region
United States
NLM ID
0370502
PMCID
PMC1877693
Subset
IM
Grants
NHLBI NIH HHS · HL-40506 · United States
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