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A basement membrane‐associated glycoprotein from skeletal muscle
Author(s) -
Marton Linda S. G.,
Arnason Barry G. W.
Publication year - 1982
Publication title -
journal of cellular biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.028
H-Index - 165
eISSN - 1097-4644
pISSN - 0730-2312
DOI - 10.1002/jcb.240190406
Subject(s) - hydroxylysine , glycoprotein , basement membrane , laminin , biochemistry , glomerular basement membrane , chemistry , fibronectin , skeletal muscle , collagenase , membrane glycoproteins , type iv collagen , extracellular matrix , microbiology and biotechnology , biology , amino acid , kidney , enzyme , endocrinology , lysine , glomerulonephritis
Abstract We have isolated a major glycoprotein that appears to be associated with rat skeletal muscle basement membrane. We determined that the glycoprotein was part of the muscle cell surface complex when we found it to be enriched in preparations of muscle ghosts. We isolate the glycoprotein from homogenized muscle preextracted with 4 M and 8 M urea. It elutes as a major component in the presence of 8 M urea/50 mM 2‐mercaptoethanol. Its apparent molecular weight on sodium dodecyl sulfate gels is 130,000. Amino acid analysis indicates that it is not a collagen but that it does contain small amounts of hydroxyproline and hydroxylysine. There may be collagenous domains in the glycoprotein molecule, for it is cleaved into three fragments by purified bacterial collagenase. Immunoperoxidase staining confirms that the 130,000‐dalton protein is localized at the surface of adult skeletal muscle cells. It is probably a general basement membrane‐associated glycoprotein because we found material immunologically cross‐reactive with the muscle glycoprotein in basement membrane regions of kidney, liver, brain, and small intestine. We have shown the glycoprotein to be distinct from fibronectin, laminin, and types I, III, IV, and V collagens in enzyme‐linked immunosorbent assays.