Abstract
Thrombospondin, a high molecular weight glycoprotein secreted by platelets in response to activation by thrombin, has been identified by immunofluorescence in bovine aortic endothelial cells, human foreskin fibroblasts, and human aortic smooth muscle cells. Immunofluorescence patterns were found to be similar using antisera raised to thrombospondins purified either from bovine aortic endothelial cells or from human platelets. Radioimmune precipitation of pulse-labeled cellular proteins confirmed the presence of thrombospondin in positively stained cells. A sensitive quantitative enzyme-linked immunosorbent assay (ELISA) was developed and used to determine that the accumulation of secreted thrombospondin was similar for endothelial cells and fibroblasts but was higher for smooth muscle cells. The presence of thrombospondin in a variety of cells suggests that its function may not be limited to an involvement in platelet interactions.
Full Text
The Full Text of this article is available as a PDF (1.0 MB).
Selected References
These references are in PubMed. This may not be the complete list of references from this article.
- Baenziger N. L., Brodie G. N., Majerus P. W. A thrombin-sensitive protein of human platelet membranes. Proc Natl Acad Sci U S A. 1971 Jan;68(1):240–243. doi: 10.1073/pnas.68.1.240. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Gartner T. K., Gerrard J. M., White J. G., Williams D. C. Fibrinogen is the receptor for the endogenous lectin of human platelets. Nature. 1981 Feb 19;289(5799):688–690. doi: 10.1038/289688a0. [DOI] [PubMed] [Google Scholar]
- Jaffe E. A., Leung L. L., Nachman R. L., Levin R. I., Mosher D. F. Thrombospondin is the endogenous lectin of human platelets. Nature. 1982 Jan 21;295(5846):246–248. doi: 10.1038/295246a0. [DOI] [PubMed] [Google Scholar]
- Lawler J. W., Slayter H. S., Coligan J. E. Isolation and characterization of a high molecular weight glycoprotein from human blood platelets. J Biol Chem. 1978 Dec 10;253(23):8609–8616. [PubMed] [Google Scholar]
- Lawler J. W., Slayter H. S. The release of heparin binding peptides from platelet thrombospondin by proteolytic action of thrombin, plasmin and trypsin. Thromb Res. 1981 May 1;22(3):267–279. doi: 10.1016/0049-3848(81)90119-5. [DOI] [PubMed] [Google Scholar]
- McPherson J., Sage H., Bornstein P. Isolation and characterization of a glycoprotein secreted by aortic endothelial cells in culture. Apparent identity with platelet thrombospondin. J Biol Chem. 1981 Nov 10;256(21):11330–11336. [PubMed] [Google Scholar]
- Mosher D. F., Doyle M. J., Jaffe E. A. Synthesis and secretion of thrombospondin by cultured human endothelial cells. J Cell Biol. 1982 May;93(2):343–348. doi: 10.1083/jcb.93.2.343. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Phillips D. R., Jennings L. K., Prasanna H. R. Ca2+-mediated association of glycoprotein G (thrombinsensitive protein, thrombospondin) with human platelets. J Biol Chem. 1980 Dec 25;255(24):11629–11632. [PubMed] [Google Scholar]
- Sage H., Bornstein P. Preparation and characterization of procollagens and procollagen-collagen intermediates. Methods Enzymol. 1982;82(Pt A):96–127. doi: 10.1016/0076-6879(82)82061-2. [DOI] [PubMed] [Google Scholar]
- Sage H., Crouch E., Bornstein P. Collagen synthesis by bovine aortic endothelial cells in culture. Biochemistry. 1979 Nov 27;18(24):5433–5442. doi: 10.1021/bi00591a028. [DOI] [PubMed] [Google Scholar]
- Sage H., Pritzl P., Bornstein P. Secretory phenotypes of endothelial cells in culture: comparison of aortic, venous, capillary, and corneal endothelium. Arteriosclerosis. 1981 Nov-Dec;1(6):427–442. doi: 10.1161/01.atv.1.6.427. [DOI] [PubMed] [Google Scholar]
- Saglio S. D., Slayter H. S. Use of a radioimmunoassay to quantify thrombospondin. Blood. 1982 Jan;59(1):162–166. [PubMed] [Google Scholar]