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Stimulation of the chemotactic migration of human fibroblasts by transforming growth factor beta

Transforming growth factor beta (TGF-beta) is a potent chemoattractant in vitro for human dermal fibroblasts. Intact disulfide and perhaps the dimeric structure of TGF-beta is essential for its ability to stimulate chemotactic migration of fibroblasts, since reduction with 2-ME results in a marked l...

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Detalles Bibliográficos
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 1987
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2188256/
https://www.ncbi.nlm.nih.gov/pubmed/3491869
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description Transforming growth factor beta (TGF-beta) is a potent chemoattractant in vitro for human dermal fibroblasts. Intact disulfide and perhaps the dimeric structure of TGF-beta is essential for its ability to stimulate chemotactic migration of fibroblasts, since reduction with 2-ME results in a marked loss of its potency as a chemoattractant. Although epidermal growth factor (EGF) appears to be capable of modulating some effects of TGF-beta, it does not alter the chemotactic response of fibroblasts to TGF-beta. Specific polyvalent rabbit antibodies to homogeneously pure TGF-beta block its chemotactic activity but has no effect on the other chemoattractants tested (platelet-derived growth factor, fibronectin, and denatured type I collagen). Since TGF-beta is secreted by a variety of neoplastic and normal cells including platelets, monocytes/macrophages, and lymphocytes, it may play a critical role in vivo in embryogenesis, host response to tumors, and the repair response that follows damage to tissues by immune and nonimmune reactions.
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spelling pubmed-21882562008-04-17 Stimulation of the chemotactic migration of human fibroblasts by transforming growth factor beta J Exp Med Articles Transforming growth factor beta (TGF-beta) is a potent chemoattractant in vitro for human dermal fibroblasts. Intact disulfide and perhaps the dimeric structure of TGF-beta is essential for its ability to stimulate chemotactic migration of fibroblasts, since reduction with 2-ME results in a marked loss of its potency as a chemoattractant. Although epidermal growth factor (EGF) appears to be capable of modulating some effects of TGF-beta, it does not alter the chemotactic response of fibroblasts to TGF-beta. Specific polyvalent rabbit antibodies to homogeneously pure TGF-beta block its chemotactic activity but has no effect on the other chemoattractants tested (platelet-derived growth factor, fibronectin, and denatured type I collagen). Since TGF-beta is secreted by a variety of neoplastic and normal cells including platelets, monocytes/macrophages, and lymphocytes, it may play a critical role in vivo in embryogenesis, host response to tumors, and the repair response that follows damage to tissues by immune and nonimmune reactions. The Rockefeller University Press 1987-01-01 /pmc/articles/PMC2188256/ /pubmed/3491869 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
Stimulation of the chemotactic migration of human fibroblasts by transforming growth factor beta
title Stimulation of the chemotactic migration of human fibroblasts by transforming growth factor beta
title_full Stimulation of the chemotactic migration of human fibroblasts by transforming growth factor beta
title_fullStr Stimulation of the chemotactic migration of human fibroblasts by transforming growth factor beta
title_full_unstemmed Stimulation of the chemotactic migration of human fibroblasts by transforming growth factor beta
title_short Stimulation of the chemotactic migration of human fibroblasts by transforming growth factor beta
title_sort stimulation of the chemotactic migration of human fibroblasts by transforming growth factor beta
topic Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2188256/
https://www.ncbi.nlm.nih.gov/pubmed/3491869