Partial cDNA sequence encoding a globular domain at the C terminus of the rat cartilage proteoglycan.
We have isolated and sequenced a cDNA clone of 872 base pairs from the 3' end of the mRNA for the large cartilage specific proteoglycan from rat. Identification was confirmed by a comparison with published protein sequence. Hybridization analysis shows the presence of an 8-9-kilobase mRNA for this proteoglycan in rat and chick sternal chondrocytes and rat chondrosarcoma cells, but not in RNA from rat fibroblasts, vitamin A-treated chick chondrocytes, chick crop, or bone. The carboxyl portion of the proteoglycan is deduced to terminate in a globular domain, which includes a region homologous to a chick hepatic lectin, and is possibly involved in binding to N-acetylglucosamine. The clone extends into a region where serines are clustered, probably the start of the chondroitin sulfate-rich region.
D000595:Amino Acid Sequence; D000818:Animals; D037263:Asialoglycoprotein Receptor; D001483:Base Sequence; D002356:Cartilage / Q000032:analysis*; D002645:Chickens; D002813:Chondrosarcoma / Q000032:analysis; D004247:DNA / Q000032:analysis*; D009693:Nucleic Acid Hybridization; D011061:Poly A / Q000032:analysis; D011509:Proteoglycans / Q000235:genetics*; D012313:RNA / Q000032:analysis; D012333:RNA, Messenger; D051381:Rats; D011971:Receptors, Immunologic / Q000032:analysis
D037263:Asialoglycoprotein Receptor; D011509:Proteoglycans; D012333:RNA, Messenger; D011971:Receptors, Immunologic; D011061:Poly A; D012313:RNA; D004247:DNA