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A tissue-specific protein fraction has been detected in rat osteogenic tissue. Dissociative extraction of adult rat bone matrix with 4 M guanidinium chloride solution was followed sequentially by gel chromatography and polyacrylamide gel electrophoresis. By the latter procedure a prominent protein component of molecular weight 19,000 was isolated from the low molecular weight fraction, and antibodies directed against this protein were raised in rabbits. The antibodies were mainly against antigenic sites on this protein, as shown by protein blotting techniques. By embedding rat tissues in hydrophilic plastic and by using immunohistochemical procedures the presence of this protein was demonstrated specifically in bone matrix in vivo, in osteogenic tissue developing in diffusion chamber culture, and in a malignant osteoblast cell line (UMR 106). Soft tissues (liver, kidney, spleen, gut, skin, thymus, eye) showed no reactivity with the antiserum and in vitro a further malignant osteoblast cell line (ROS 17/2.8) did not synthesize the 19,000 molecular weight protein. This protein appears to be expressed solely by osteogenic tissue and may be used as a biochemical criterion of osteogenic differentiation.

Original publication

DOI

10.1002/jbmr.5650020305

Type

Journal article

Journal

Journal of bone and mineral research : the official journal of the American Society for Bone and Mineral Research

Publication Date

06/1987

Volume

2

Pages

191 - 199

Addresses

Nuffield Department of Orthopaedic Surgery, University of Oxford, Nuffield Orthopaedic Centre, UK.

Keywords

Animals, Rats, Proteins, Immunoenzyme Techniques, Electrophoresis, Polyacrylamide Gel, Osteogenesis, Molecular Weight