Abstract
Type IX collagen is a recently characterized product of chondrocytes. The molecules of this collagen are heterotrimers of three genetically distinct polypeptide chains. One of the three chains contains chondroitin and/or dermatan sulfate glycosaminoglycan chains, giving the molecule a proteoglycan character. In fact, Type IX collagen has been identified with the proteoglycan Lt (PG-Lt), first isolated by Noro, A., Kimata, K., Oike, Y., Shinomura, T., Maeda, N., Yano, S., Takahashi, N., and Suzuki, S. (1983) J. Biol. Chem. 258, 9323-9331 from chick embryonic tibia and femur. Based on amino acid sequences predicted from the nucleotide sequences of cDNA and genomic clones specific for two of the chains of Type IX collagen, we have synthesized oligopeptides representing portions of the two chains. In addition, an oligopeptide has been made based on a partial amino acid sequence of the third chain. Antibodies against the synthetic peptides have been generated in rabbits, and the polyclonal sera have allowed identification of the three genetically distinct polypeptide subunits of Type IX collagen. In addition, labeling with [35S]sulfate and treatment with chondroitinase ABC demonstrates that glycosaminoglycan chains are present on the subunit that has been given the designation alpha 2(IX).
Highlights
Type IX collagen is a recently characterized product distribution leads one to suspect that their primary role may ofchondrocytes.Themoleculesof this collagen are not be mechanical
Antibodies against the synthetic peptides have contains covalently attached chondroitin and/or dermatan been generated in rabbits, and the polyclonhalavseerasulfate glycosaminoglycan chains (12), giving Type IX collaallowed identification of the thregeenetically distinct gen a proteoglycan character
Polyclonal antibodies against one of the triple-helical domains labeling with [SsS]sulfateandtreatment with chon- of Type IX collagen, Vaughan et al (13) have identified Type droitinase ABC demonstrates that glycosaminoglycan IX collagen with the proteoglycan Lt (PG-Lt), first isolated chains are presenton the subunit that has been given by Noro et al (14) from chick embryonic tibia and femur
Summary
Type IX collagen is a recently characterized product distribution leads one to suspect that their primary role may ofchondrocytes.Themoleculesof this collagen are not be mechanical. Varying amounts of free peptide dissolved in 10pl of phosphate-buffered saline were preincubated with an amount of preformed immune complex shown to be sufficient to precipitate 80% of the labeled test antigen in direct precipitation assays.
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