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Fibronectin receptors of phagocytes. Characterization of the Arg-Gly- Asp binding proteins of human monocytes and polymorphonuclear leukocytes

We have defined the cell surface molecules of human monocytes and PMN that bind to the chymotryptic cell binding domain of Fn and to a synthetic peptide, KYAVTGRGDS, based on the sequence of Fn, by affinity chromatography. Monocytes express two receptors that differ in their affinity for CBD-Sepharo...

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Detalles Bibliográficos
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 1988
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2188897/
https://www.ncbi.nlm.nih.gov/pubmed/2965209
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description We have defined the cell surface molecules of human monocytes and PMN that bind to the chymotryptic cell binding domain of Fn and to a synthetic peptide, KYAVTGRGDS, based on the sequence of Fn, by affinity chromatography. Monocytes express two receptors that differ in their affinity for CBD-Sepharose and peptide-Sepharose, but that both recognize the RGD sequence. Only a single receptor is purified from PMN, which resembles the monocyte surface molecule that binds to peptide-Sepharose. These receptors are not part of the Mac-1, LFA-1, p(150,95) family, but do have homology to the platelet Fn receptor, gpIIb/IIIa. Interestingly, the antigenic crossreactivity between gpIIb/IIIa and the phagocyte receptors purified on peptide-Sepharose is largely in the beta chain of the receptors. The alpha chains appear to be distinct, based on molecular weight, antigenic analysis, and ligand specificity. This receptor also seems to be the surface molecule on monocytes that is critical for phagocytosis enhancement by Fn. Thus, we have defined the phagocyte Fn receptor that transduces the signal for increased phagocytosis by monocytes; it may be a third member of a family of adhesion molecules that includes the gpIIb/IIIa of platelets and the vitronectin receptor of fibroblasts.
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spelling pubmed-21888972008-04-17 Fibronectin receptors of phagocytes. Characterization of the Arg-Gly- Asp binding proteins of human monocytes and polymorphonuclear leukocytes J Exp Med Articles We have defined the cell surface molecules of human monocytes and PMN that bind to the chymotryptic cell binding domain of Fn and to a synthetic peptide, KYAVTGRGDS, based on the sequence of Fn, by affinity chromatography. Monocytes express two receptors that differ in their affinity for CBD-Sepharose and peptide-Sepharose, but that both recognize the RGD sequence. Only a single receptor is purified from PMN, which resembles the monocyte surface molecule that binds to peptide-Sepharose. These receptors are not part of the Mac-1, LFA-1, p(150,95) family, but do have homology to the platelet Fn receptor, gpIIb/IIIa. Interestingly, the antigenic crossreactivity between gpIIb/IIIa and the phagocyte receptors purified on peptide-Sepharose is largely in the beta chain of the receptors. The alpha chains appear to be distinct, based on molecular weight, antigenic analysis, and ligand specificity. This receptor also seems to be the surface molecule on monocytes that is critical for phagocytosis enhancement by Fn. Thus, we have defined the phagocyte Fn receptor that transduces the signal for increased phagocytosis by monocytes; it may be a third member of a family of adhesion molecules that includes the gpIIb/IIIa of platelets and the vitronectin receptor of fibroblasts. The Rockefeller University Press 1988-03-01 /pmc/articles/PMC2188897/ /pubmed/2965209 Text en This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/).
spellingShingle Articles
Fibronectin receptors of phagocytes. Characterization of the Arg-Gly- Asp binding proteins of human monocytes and polymorphonuclear leukocytes
title Fibronectin receptors of phagocytes. Characterization of the Arg-Gly- Asp binding proteins of human monocytes and polymorphonuclear leukocytes
title_full Fibronectin receptors of phagocytes. Characterization of the Arg-Gly- Asp binding proteins of human monocytes and polymorphonuclear leukocytes
title_fullStr Fibronectin receptors of phagocytes. Characterization of the Arg-Gly- Asp binding proteins of human monocytes and polymorphonuclear leukocytes
title_full_unstemmed Fibronectin receptors of phagocytes. Characterization of the Arg-Gly- Asp binding proteins of human monocytes and polymorphonuclear leukocytes
title_short Fibronectin receptors of phagocytes. Characterization of the Arg-Gly- Asp binding proteins of human monocytes and polymorphonuclear leukocytes
title_sort fibronectin receptors of phagocytes. characterization of the arg-gly- asp binding proteins of human monocytes and polymorphonuclear leukocytes
topic Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2188897/
https://www.ncbi.nlm.nih.gov/pubmed/2965209