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An Mr = 524,000 oligomeric protein was isolated from bovine cartilage and designated COMP (Cartilage Oligomeric Matrix Protein). The protein is composed of disulfide-bonded subunits with an apparent Mr of 100,000 each. It is markedly anionic, probably due to its high contents of aspartic acid and glutamic acid, as well as to its substitution with negatively(More)
A non-collagenous quantitatively prominent protein was purified from guanidine hydrochloride extracts of bovine tracheal cartilage. Purification was achieved by cesium chloride density gradient centrifugation and chromatography on DEAE-cellulose at pH 7.0 followed by CM-cellulose at pH 5.0. The protein has a marked tendency to form aggregates in denaturing(More)
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(More)
We have determined the primary structure of a 59 kd collagen binding protein which is present in many types of connective tissues, e.g. cartilage, tendon, skin, sclera and cornea. The amino acid sequence, deducted from a 2662 bp cDNA clone, predicts a 42 kd protein with a high content of leucine residues. Most of the protein consists of homologous 23 amino(More)
Fibroblasts synthesize a variety of proteoglycans among which is a family of structurally related small proteoglycans, i.e. PG-S1 (biglycan) and PG-S2 (decorin). Fibromodulin, which is present in some tissues as a keratan sulfate proteoglycan, also belongs to this family. We have used primary fibroblasts from fetal skin and bovine sclera in culture to study(More)
We have determined the structure and partially sequenced the human fibromodulin gene. The translated region of the gene is composed of two exons. An exon in the 5'-non translated region is separated from the next exon by a 1 kb intron. This exon, which encodes the major part of the translated region, is 983 bp and is followed by an approx. 5 kbp intron. The(More)
Recombinant fragments alpha, beta, and gamma were prepared comprising about 100 C-terminal residues of the corresponding polypeptide chains in the three-stranded alpha-helical coiled-coil domain of laminin. Circular dichroism spectra, thermal transition profiles, non-denaturing gels, analytical ultracentrifugation, and calorimetry indicated alpha-helicity(More)
Ledbetter, S. R., Tyree, B.. Hashell. J. R. & Horrigan. E. A. ( 1985) J . Biol. C'hrm. 260,8106-8 I 13 Hassell, J. R., Noonan, D. M., Ledbetter, S. R. & Laurie. G. W. (1986) C'ihri Found. Symp. 124,204-222 Noonan. D. M.. Horrigan. E. A.. Ledbetter. S. R.. Vogeli. G., Sasaki. M.. Yamada. Y. & Hassell. J . R. ( 1988) J . Riol. ('hem. 263, 16379-16387(More)