A heparin-binding protein involved in inhibition of smooth-muscle cell proliferation

Author:

Lankes W1,Griesmacher A1,Grünwald J2,Schwartz-Albiez R3,Keller R1

Affiliation:

1. Institut für Klinische Chemie und Pathobiochemie der RWTH Aachen, Pauwelsstraβe, 5100 Aachen

2. Institut für Arterioskleroseforschung an der Universität Münster, Domagkstraβe 3, 4400 Münster

3. Institut für Immunologie und Genetik, Deutsches Krebsforschungszentrum, Im Neuenheimer Feld 280, 6900 Heidelberg, W. Germany

Abstract

A heparin-binding protein was isolated from bovine uteri and purified to homogeneity. This protein appears as a double band of approx. 78 kDa in SDS/polyacrylamide-gel electrophoresis and has an isoelectric point of 5.2. The binding of heparin to this protein is saturable. No other glycosaminoglycan from mammalian tissue, such as hyaluronic acid, chondroitin sulphate, dermatan sulphate or keratan sulphate, binds to the 78 kDa protein. Dextran sulphate binds in a non-saturable fashion. Certain heparan sulphate polysaccharide structures are required for binding to the 78 kDa protein. Some proteoheparan sulphates, such as endothelial cell-surface proteoheparan sulphate, show only weak interaction with the 78 kDa protein in contrast with a basement-membrane proteoheparan sulphate from HR-9 cells. Antibodies against the 78 kDa protein inhibit binding of proteoheparan [35S]sulphate from basement membranes to smooth-muscle cells. Conventional antibodies, Fab fragments and some monoclonal antibodies, inhibit smooth-muscle cell proliferation in a similar range as that observed for heparin. The protein was detected in a variety of tissues and cells but not in blood cells. A possible role of this protein as a receptor for heparin or heparan sulphate and its function in the control of the arterial wall structure are discussed.

Publisher

Portland Press Ltd.

Subject

Cell Biology,Molecular Biology,Biochemistry

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