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.

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