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Distribution of fetal bovine serum fibronectin and endogenous rat cell fibronectin in extracellular matrix

Normal rat kidney cells were cultured in medium supplemented with normal fetal bovine serum (FBS) or FBS depleted of fibronectin. The cell surface fibronectin of these cultures was visualized by indirect immunofluorescence using species-specific antisera for either rat fibronectin or bovine fibronec...

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Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 1979
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2110434/
https://www.ncbi.nlm.nih.gov/pubmed/389940
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collection PubMed
description Normal rat kidney cells were cultured in medium supplemented with normal fetal bovine serum (FBS) or FBS depleted of fibronectin. The cell surface fibronectin of these cultures was visualized by indirect immunofluorescence using species-specific antisera for either rat fibronectin or bovine fibronectin. Anti-rat-fibronectin revealed fibrillar structures on the cells grown in either normal medium or fibronectin-depleted medium. Anti-bovine fibronectin revealed similar fibrillar networks, but only on the cells grown in medium containing bovine fibronectin. Staining in each case was abolished by absorption with the homologous antigen. It appears that exogenous fibronectin was incorporated into the same structures as endogenous fibronectin. This finding suggests that circulating fibronectin may serve as a building block for the assembly of extracellular matrix, possibly by cells which are incapable of synthesizing it.
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spelling pubmed-21104342008-05-01 Distribution of fetal bovine serum fibronectin and endogenous rat cell fibronectin in extracellular matrix J Cell Biol Articles Normal rat kidney cells were cultured in medium supplemented with normal fetal bovine serum (FBS) or FBS depleted of fibronectin. The cell surface fibronectin of these cultures was visualized by indirect immunofluorescence using species-specific antisera for either rat fibronectin or bovine fibronectin. Anti-rat-fibronectin revealed fibrillar structures on the cells grown in either normal medium or fibronectin-depleted medium. Anti-bovine fibronectin revealed similar fibrillar networks, but only on the cells grown in medium containing bovine fibronectin. Staining in each case was abolished by absorption with the homologous antigen. It appears that exogenous fibronectin was incorporated into the same structures as endogenous fibronectin. This finding suggests that circulating fibronectin may serve as a building block for the assembly of extracellular matrix, possibly by cells which are incapable of synthesizing it. The Rockefeller University Press 1979-10-01 /pmc/articles/PMC2110434/ /pubmed/389940 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
Distribution of fetal bovine serum fibronectin and endogenous rat cell fibronectin in extracellular matrix
title Distribution of fetal bovine serum fibronectin and endogenous rat cell fibronectin in extracellular matrix
title_full Distribution of fetal bovine serum fibronectin and endogenous rat cell fibronectin in extracellular matrix
title_fullStr Distribution of fetal bovine serum fibronectin and endogenous rat cell fibronectin in extracellular matrix
title_full_unstemmed Distribution of fetal bovine serum fibronectin and endogenous rat cell fibronectin in extracellular matrix
title_short Distribution of fetal bovine serum fibronectin and endogenous rat cell fibronectin in extracellular matrix
title_sort distribution of fetal bovine serum fibronectin and endogenous rat cell fibronectin in extracellular matrix
topic Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2110434/
https://www.ncbi.nlm.nih.gov/pubmed/389940