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β 1 integrins isolated from embryonic chicken fibroblasts bind to monomers and polymers of type I collagen
Author(s) -
Potts A. Jeannette,
Little Charles D.
Publication year - 1992
Publication title -
journal of cellular physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.529
H-Index - 174
eISSN - 1097-4652
pISSN - 0021-9541
DOI - 10.1002/jcp.1041520316
Subject(s) - integrin , collagen receptor , alpha (finance) , cytoplasm , beta (programming language) , chemistry , type i collagen , protein subunit , biology , microbiology and biotechnology , biochemistry , receptor , construct validity , nursing , computer science , patient satisfaction , programming language , gene , endocrinology , medicine
Abstract The avian integrin β 1 subfamily consists of multiple α‐β subunit heterodimers. We employed two different physical states of type I collagen, monomers and fibrils, in the isolation and characterization of avian collagen integrins. Affinity chromatography showed that three integrins, tentatively designated α 155 β 1 (band 1), α 5a β 1 , and α 3 β 1 (band 2), bind fibrillar and monomeric collagen under physiological ionic conditions and require divalent cations for binding activity. Sodium chloride gradients (0–0.5 M) were used to assess the functional ability of the integrins to remain bound to the two forms of type I collagen. The results show that integrins elute from the two forms of collagen with distinct fractionation profiles. One integrin, α 155 β 1 , binds fibrillar collagen with relatively higher affinity than the other β 1 receptors. This same avian integrin, α 155 β 1 , is immunoreactive with an antiserum (Hynes et al., 1989) raised against a peptide that corresponds to the entire α 5 cytoplasmic domain, and coincidently, part of the α 6 cytoplasmic domain (de Curtis et al., 1991). Cell biological studies employing double immunofluorescence show that integrins recognized by this antiserum co‐localize with extracellular deposits of type I collagen. © 1992 Wiley‐Liss, Inc.