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Abstract 


Platelet-associated fibronectin antigen has been identified by radioimmunoassay and immunofluorescent techniques. In radioimmunoassay, platelet fibronectin was immunochemically indistinguishable from plasma fibronectin. Platelet and plasma fibronectin were bound and eluted from gelatin-sepharose under similar conditions. The level of platelet fibronectin in detergent extracts of washed platelets from 12 healthy adults was 2.85 +/- 1.24 microgram/10(9) platelets. Immunofluorescence with F(ab')2 fragments of immunochemically purified antifibronectin showed that all platelets stained with a discrete punctate pattern. The identification of platelet fibronectin antigen raises the possibility that this protein may participate in platelet-platelet or platelet-surface interactions.

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Logo of jcinvestThe Journal of Clinical Investigation
J Clin Invest. 1979 Mar; 63(3): 540–543.
PMCID: PMC371985
PMID: 372243

Identification and quantitation of platelet-associated fibronectin antigen.

Abstract

Platelet-associated fibronectin antigen has been identified by radioimmunoassay and immunofluorescent techniques. In radioimmunoassay, platelet fibronectin was immunochemically indistinguishable from plasma fibronectin. Platelet and plasma fibronectin were bound and eluted from gelatin-sepharose under similar conditions. The level of platelet fibronectin in detergent extracts of washed platelets from 12 healthy adults was 2.85 +/- 1.24 microgram/10(9) platelets. Immunofluorescence with F(ab')2 fragments of immunochemically purified antifibronectin showed that all platelets stained with a discrete punctate pattern. The identification of platelet fibronectin antigen raises the possibility that this protein may participate in platelet-platelet or platelet-surface interactions.

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Selected References

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  • Hynes RO, Bye JM. Density and cell cycle dependence of cell surface proteins in hamster fibroblasts. Cell. 1974 Oct;3(2):113–120. [Abstract] [Google Scholar]
  • Yamada KM, Olden K. Fibronectins--adhesive glycoproteins of cell surface and blood. Nature. 1978 Sep 21;275(5677):179–184. [Abstract] [Google Scholar]
  • Vaheri A, Mosher DF. High molecular weight, cell surface-associated glycoprotein (fibronectin) lost in malignant transformation. Biochim Biophys Acta. 1978 Sep 18;516(1):1–25. [Abstract] [Google Scholar]
  • Plow EF, Hougie C, Edgington TS. Neoantigenic expressions engendered by plasmin cleavage of fibrinogen. J Immunol. 1971 Nov;107(5):1496–1500. [Abstract] [Google Scholar]
  • Ginsberg MH, Kozin F, O'Malley M, McCarty DJ. Release of platelet constituents by monosodium urate crystals. J Clin Invest. 1977 Nov;60(5):999–1007. [Europe PMC free article] [Abstract] [Google Scholar]
  • Tangen O, Berman HJ, Marfey P. Gel filtration. A new technique for separation of blood platelets from plasma. Thromb Diath Haemorrh. 1971 Jun 30;25(2):268–278. [Abstract] [Google Scholar]
  • Weber K, Osborn M. The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis. J Biol Chem. 1969 Aug 25;244(16):4406–4412. [Abstract] [Google Scholar]
  • Mosesson MW, Chen AB, Huseby RM. The cold-insoluble globulin of human plasma: studies of its essential structural features. Biochim Biophys Acta. 1975 Apr 29;386(2):509–524. [Abstract] [Google Scholar]
  • Mosher DF. Cross-linking of cold-insoluble globulin by fibrin-stabilizing factor. J Biol Chem. 1975 Aug 25;250(16):6614–6621. [Abstract] [Google Scholar]
  • Niewiarowski S. Proteins secreted by the platelet. Thromb Haemost. 1977 Dec 15;38(4):924–938. [Abstract] [Google Scholar]
  • Tollefsen DM, Feagler JR, Majerus PW. The binding of thrombin to the surface of human platelets. J Biol Chem. 1974 Apr 25;249(8):2646–2651. [Abstract] [Google Scholar]
  • Miletich JP, Jackson CM, Majerus PW. Interaction of coagulation factor Xa with human platelets. Proc Natl Acad Sci U S A. 1977 Sep;74(9):4033–4036. [Europe PMC free article] [Abstract] [Google Scholar]

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