Cartilage matrix proteins. A basic 36-kDa protein with a restricted distribution to cartilage and bone

• Published in: The Journal of biological chemistry 1991-10, Vol.266 (30), p.20428-20433
• Main Authors: LARSSON, T, SOMMARIN, Y, PAULSSON, M, ANTONSSON, P, HEDBOM, E, WENDEL, M, HEINEGARD, D
• Format: Article
• Language: English
• Subjects: Animals; Biological and medical sciences; Biotin - metabolism; Blotting, Western; Bone Matrix - cytology; Bone Matrix - metabolism; Cartilage - cytology; Cartilage - metabolism; Cattle; Cell structures and functions; Chromatography, Liquid; Electrophoresis, Polyacrylamide Gel; Enzyme-Linked Immunosorbent Assay; Extracellular Matrix Proteins - metabolism; Fundamental and applied biological sciences. Psychology; matrix; Molecular and cellular biology; proteins; Tissue Distribution; trachea
• ISSN: 0021-9258; 1083-351X
• DOI: 10.1016/S0021-9258(18)54941-3

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 solutions of high ionic strength, e.g. 6 M guanidine hydrochloride. The purified protein contains a single, Mr 36,000 polypeptide chain, with a particularly high content of leucine. It contains about 1% carbohydrate with a remarkable absence of hexosamines and sialic acid, whereas xylose, galactose, mannose, and fucose were identified in the preparation. The protein was identified in extracts of cartilage and bone and could be shown to be primarily extracellular. Tendon may contain trace amounts of the protein, whereas extracts of several other tissues showed no immunoreactivity in enzyme-linked immunosorbent assay.