GENERATION OF A MONOCLONAL-ANTIBODY AGAINST AVIAN SMALL DERMATAN SULFATE PROTEOGLYCAN - IMMUNOLOCALIZATION AND TISSUE DISTRIBUTION OF PG-II (DECORIN) IN EMBRYONIC-TISSUES

Chick embryonic skeletal muscle synthesizes three major types of proteoglycans: large chondroitin sulfate proteoglycans, small dermatan sulfate proteoglycans and small heparan sulfate proteoglycans. A monoclonal antibody has been raised which recognizes the small dermatan sulfate proteoglycan. Immunoblot analysis of a partially purified preparation of skeletal muscle proteoglycans indicates that the antibody reacts with a molecule which migrates with an estimated M(r) of 100000. Prior treatment of the proteoglycans with chondroitinase results in immunostaining of a species of estimated M(r) 45 000. These values for the intact proteoglycan and its core protein suggest that the antibody is directed against a proteoglycan of the PG-II or decorin class. Immunohistochemistry indicates a widespread distribution of the proteoglycan, which is localized in connective tissue septa of skeletal and cardiac muscle, dermis, tendon, bone, perichondrium and cornea. Immunoblot analysis of the proteoglycan core proteins from these tissues demonstrates that the antibody recognizes the same 45 000-dalton band in each tissue. The widespread tissue distribution is also consistent with the antibody being directed against an epitope of PG-II. Neither the glycosaminoglycan chains nor N-linked oligosaccharides are required for reactivity and the antibody cross-reacts with other avian material, but not mammalian. This antibody, which has been designated CB-I, reveals developmental stage-specific changes in the deposition of PG-II in embryonic limb bud and skeletal muscle.