The human integrin VLA-2 is a collagen receptor on some cells and a collagen/laminin receptor on others

Journal Article · Fri Dec 01 00:00:00 EST 1989 · Proceedings of the National Academy of Sciences of the United States of America; (USA)

DOI:https://doi.org/10.1073/pnas.86.24.9906· OSTI ID:7138062

Elices, M J; Hemler, M E ^[1]

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1. Harvard Medical School, Boston, MA (USA)

The integrin heterodimer VLA-2, previously known as a collagen receptor, is now shown also to be a laminin receptor. Adhesion of the human melanoma cell line LOX to laminin was inhibited by anti-VLA {alpha}{sup 2} antibodies. Because VLA-2-mediated LOX cell attachment to laminin was not inhibited by digestion with collagenase, collagen contamination of laminin was not a factor. In addition, VLA-2 from LOX cells bound to immobilized laminin, and binding was disrupted by EDTA but not by Arg-Gly-Asp (RGD) peptides. VLA-3 also bound to laminin-Sepharose, although less avidly than VLA-2. Thus, at least four separate members of the integrin {beta}{sub 1} subfamily serve as laminin receptors - i.e., VLA-2 and VLA-3 (this study) together with VLA-1 and VLA-6 (other reports). Whereas LOX and other cell lines used VLA-2 as both a laminin and collagen receptor, fibroblast VLA-2 mediated collagen but not laminin binding. Likewise, VLA-2 from platelets did not interact with laminin. Despite this functional discordancy, VLA-2 from laminin-binding and nonbinding sources was indistinguishable by all immunochemical and biochemical criteria examined. Thus, functional differences in VLA-2 may be due to cell type-specific modulation.

• OSTI ID: 7138062
• Journal Information: Proceedings of the National Academy of Sciences of the United States of America; (USA), Vol. 86:24; ISSN 0027-8424
• Country of Publication: United States
• Language: English

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59 BASIC BIOLOGICAL SCIENCES
CHROMIUM 51
TRACER TECHNIQUES
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MEMBRANE PROTEINS
MOLECULAR STRUCTURE
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GLYCOPROTEINS
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ISOTOPE APPLICATIONS
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NUCLEI
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550201* - Biochemistry- Tracer Techniques