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| COMP (CARTILAGE OLIGOMERIC MATRIX PROTEIN) IS STRUCTURALLY RELATED TO THE THROMBOSPONDINS |
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| Author(s): OLDBERG A, ANTONSSON P, LINDBLOM K, HEINEGARD D |
| Source: JOURNAL OF BIOLOGICAL CHEMISTRY Volume: 267 Issue: 31 Pages: 22346-22350 Published: NOV 5 1992 |
| Times Cited: 209 References: 31 |
| Abstract: Cloning and sequence analysis of cartilage oligomeric matrix protein (COMP) cDNA, representing a cartilage pentameric protein, revealed a protein of 755 amino acid residues with a calculated molecular mass of 82,700 Da. Expression of the cDNA in COS cells showed that COMP is a homopolymer composed of five identical disulfide-linked subunits. COMP is homologous to the carboxyl-terminal half of thrombospondin, and the homologies include 89% and 54% of the residues in COMP and thrombospondin, respectively. The similarities are most pronounced in the carboxyl-terminal domains and in the calcium binding type 3 repeat domains in which about 60% of the amino acid residues are identical. In the type 2/epidermal growth factor repeat domains the two proteins contain 41 % identical residues. The sequence of the amino-terminal 84-amino acid residues is unique for COMP. Comparison of the amino acid sequences in the type 2 and type 3 repeat domains of COMP and the thrombospondins shows that COMP is the product of a unique gene and not the result of an alternatively spliced thrombospondin gene. |
| Document Type: Article |
| Language: English |
| Reprint Address: OLDBERG, A (reprint author), UNIV LUND, DEPT MED & PHYSIOL CHEM, POB 94, S-22100 LUND, SWEDEN |
| Publisher: AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC, 9650 ROCKVILLE PIKE, BETHESDA, MD 20814 |
| Subject Category: Biochemistry & Molecular Biology |
| IDS Number: JW719 |
| ISSN: 0021-9258 |
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| | | | | | | | | Record from Web of Science® | | | | | | | | | |