A type VI collagen-related glycopolypeptide is the major concanavalin A-binding component in pig skin.
The major concanavalin A-binding component in urea/deoxycholate/mercaptoethanol extracts of pig skin was a collagenous disulphide-cross-linked glycopolypeptide with an apparent molecular mass of 150 kDa and a pI of 5.5. Antiserum against the electrophoretically purified glycopolypeptide gave strong dermal staining similar to that seen with fluorescent concanavalin A. Immunocytochemical labelling showed prominent labelling of 3-4 nm dermal microfilaments, particularly those associated with dermal blood vessels and mast cells. Immunoblotting with authentic antiserum indicated that the major skin glycopolypeptide was probably identical with collagen-like glycoprotein, the tissue form of the alpha 1/alpha 2 subunits of type VI collagen. This was confirmed by immunoblotting of authentic type VI collagen from pepsin-treated pig skin. Immunoblotting, metabolic labelling with [3H]glucosamine and immune precipitation showed that an immunoreactive collagenous glycopolypeptide was synthesized and secreted by cultured pig skin fibroblasts. The results suggest that type VI collagen is the major concanavalin A-binding component in pig skin.
King
I A
IA
Dermatology Research Group, M.R.C. Clinical Research Centre, Harrow, Middx., U.K.
Tabiowo
A
A
Fryer
P R
PR
Pope
F M
FM
D000818:Animals; D002478:Cells, Cultured; D003094:Collagen / Q000378:metabolism*; D003208:Concanavalin A / Q000378:metabolism*; D005347:Fibroblasts / Q000378:metabolism; D006020:Glycopeptides / Q000378:metabolism*; D012867:Skin / Q000378:metabolism*; D013552:Swine
D006020:Glycopeptides; D003208:Concanavalin A; D003094:Collagen