The occurrence of three different proteoglycan species in chick embryo cartilage. Isolation and characterization of a second proteoglycan (PG-Lb) and its precursor form.

Abstract

Three different molecular species of proteoglycan (designated PG-H, PG-Lb, and PG-Lt) have been isolated from chick embryo epiphyseal cartilage. PG-H is a major proteoglycan of the tissue and identical, or nearly identical, with so-called cartilage-characteristic proteoglycan previously described in mammalian and avian cartilages. The third proteoglycan, PG-Lt, differs from the other two in containing disulfide-bonded collagenous polypeptides (Noro, A., Kimata, K., Oike, Y., Shinomura, T., Maeda, N., Yano, S., Takahashi, N., and Suzuki, S. (1983) J. Biol. Chem. 258, 9323-9331). The second proteoglycan, PG-Lb, consists of a core protein with Mr congruent to 52,000 dermatan sulfate copolymer chains with glucuronic acid/iduronic acid residues. Upon chondroitinase ABC digestion, the proteoglycan yields a protein-enriched core fraction of Mr congruent to 43,000. Its amino acid composition, tryptic peptide profile, and immunochemical properties indicate that PG-Lb is distinctly different from PG-H and PG-Lt in core protein structure. PG-Lb shows no specific binding with hyaluronic acid. Pulse-chase experiments with [3H]serine indicate that PG-Lb is first synthesized as a precursor form (pro-PG-Lb) that can be distinguished from PG-Lb by the production of a core molecule of Mr congruent to 52,000 after chondroitinase ABC digestion. This core molecule is labeled when [2-3H]mannose is used as a precursor, suggesting that it contains a glycoprotein type oligosaccharide. Since the core molecule from pro-PG-Lb is significantly larger in molecular weight than that from PG-Lb, the conversion of pro-PG-Lb to PG-Lb should involve scission of the polypeptide or possibly removal of mannose-containing oligosaccharide chain.