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Substrate adhesion of rat hepatocytes: a comparison of laminin and fibronectin as attachment proteins

In previous studies rat hepatocytes have been shown to adhere to substrates composed of collagen or fibronectin. In the present communication, the basement membrane protein laminin is reported to mediated the attachment and spreading of hepatocytes. The cell attachment-mediating activity of laminin...

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Detalles Bibliográficos
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 1981
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2111839/
https://www.ncbi.nlm.nih.gov/pubmed/6265475
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description In previous studies rat hepatocytes have been shown to adhere to substrates composed of collagen or fibronectin. In the present communication, the basement membrane protein laminin is reported to mediated the attachment and spreading of hepatocytes. The cell attachment-mediating activity of laminin was compared with that of fibronectin. The activity of fibronectin was heat sensitive, whereas laminin retained its activity after boiling. On the other hand, reduction and alkylation or periodate oxidation of the proteins affected only the cell attachment activity of laminin. Preincubation of cells with soluble fibronectin inhibited initial cell attachment to fibronectin but not to laminin substrates, and, reversely, soluble laminin selectively inhibited cell attachment to laminin. These results suggest that attachment of cells to substrates of the two proteins involves different cellular receptors recognizing distinct and nonidentical structures in the proteins.
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spelling pubmed-21118392008-05-01 Substrate adhesion of rat hepatocytes: a comparison of laminin and fibronectin as attachment proteins J Cell Biol Articles In previous studies rat hepatocytes have been shown to adhere to substrates composed of collagen or fibronectin. In the present communication, the basement membrane protein laminin is reported to mediated the attachment and spreading of hepatocytes. The cell attachment-mediating activity of laminin was compared with that of fibronectin. The activity of fibronectin was heat sensitive, whereas laminin retained its activity after boiling. On the other hand, reduction and alkylation or periodate oxidation of the proteins affected only the cell attachment activity of laminin. Preincubation of cells with soluble fibronectin inhibited initial cell attachment to fibronectin but not to laminin substrates, and, reversely, soluble laminin selectively inhibited cell attachment to laminin. These results suggest that attachment of cells to substrates of the two proteins involves different cellular receptors recognizing distinct and nonidentical structures in the proteins. The Rockefeller University Press 1981-07-01 /pmc/articles/PMC2111839/ /pubmed/6265475 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
Substrate adhesion of rat hepatocytes: a comparison of laminin and fibronectin as attachment proteins
title Substrate adhesion of rat hepatocytes: a comparison of laminin and fibronectin as attachment proteins
title_full Substrate adhesion of rat hepatocytes: a comparison of laminin and fibronectin as attachment proteins
title_fullStr Substrate adhesion of rat hepatocytes: a comparison of laminin and fibronectin as attachment proteins
title_full_unstemmed Substrate adhesion of rat hepatocytes: a comparison of laminin and fibronectin as attachment proteins
title_short Substrate adhesion of rat hepatocytes: a comparison of laminin and fibronectin as attachment proteins
title_sort substrate adhesion of rat hepatocytes: a comparison of laminin and fibronectin as attachment proteins
topic Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2111839/
https://www.ncbi.nlm.nih.gov/pubmed/6265475