On the identity of vitronectin and S-protein: immunological crossreactivity and functional studies.

作者: BR Tomasini , DF Mosher

DOI: 10.1182/BLOOD.V68.3.737.737

关键词:

摘要: Vitronectin (serum spreading factor), a major serum cell adhesion molecule, was compared with S-protein, the inhibitor of C5-9 membrane attack complex. Data from literature indicate that S-protein and vitronectin are alpha globulins same aminoterminal residues, amino acid compositions, concentrations in normal plasma (150 to 250 micrograms/mL). Both proteins have been reported interact thrombin-antithrombin The cDNA sequences were recently determined found be almost identical. In present studies, rabbit-anti-S-protein monoclonal antibody both recognized 65,000- 75,000-molecular weight (mol wt) polypeptides when or separated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis transferred nitrocellulose paper. 65,000 75,000-mol wt bound more avidly than anti-vitronectin heparin coupled agarose. presence absence constituted difference between heparin-binding plasma. When complement-activated unactivated filtration, coeluted C9 high-mol-wt fractions activated but not serum. Purified promoted human skin fibroblasts. degraded thrombin. On basis immunological functional, as well biochemical, properties, therefore, same.

参考文章(20)
D W Barnes, J Silnutzer, Isolation of human serum spreading factor. Journal of Biological Chemistry. ,vol. 258, pp. 12548- 12552 ,(1983) , 10.1016/S0021-9258(17)44211-6
S. Suzuki, A. Oldberg, E.G. Hayman, M.D. Pierschbacher, E. Ruoslahti, Complete amino acid sequence of human vitronectin deduced from cDNA. Similarity of cell attachment sites in vitronectin and fibronectin. The EMBO Journal. ,vol. 4, pp. 2519- 2524 ,(1985) , 10.1002/J.1460-2075.1985.TB03965.X
C R Ill, E Ruoslahti, Association of thrombin-antithrombin III complex with vitronectin in serum. Journal of Biological Chemistry. ,vol. 260, pp. 15610- 15615 ,(1985) , 10.1016/S0021-9258(17)36302-0
S Suzuki, M D Pierschbacher, E G Hayman, K Nguyen, Y Ohgren, E Ruoslahti, Domain structure of vitronectin. Alignment of active sites. Journal of Biological Chemistry. ,vol. 259, pp. 15307- 15314 ,(1984) , 10.1016/S0021-9258(17)42550-6
D W Barnes, J E Reing, B Amos, Heparin-binding Properties of Human Serum Spreading Factor* Journal of Biological Chemistry. ,vol. 260, pp. 9117- 9122 ,(1985) , 10.1016/S0021-9258(17)39338-9
Eckhard R. Podack, William P. Kolb, Hans J. Müller-Eberhard, The SC5b-7 complex: Formation, isolation, properties, and subunit composition Journal of Immunology. ,vol. 119, pp. 2024- 2029 ,(1977)
E. G. Hayman, M. D. Pierschbacher, Y. Ohgren, E. Ruoslahti, Serum spreading factor (vitronectin) is present at the cell surface and in tissues Proceedings of the National Academy of Sciences of the United States of America. ,vol. 80, pp. 4003- 4007 ,(1983) , 10.1073/PNAS.80.13.4003
Michael D. Pierschbacher, Shintaro Suzuki, Erkki Ruoslahti, Edward G. Hayman, Vitronectin—A major cell attachment-promoting protein in fetal bovine serum Experimental Cell Research. ,vol. 160, pp. 245- 258 ,(1985) , 10.1016/0014-4827(85)90173-9