Fibrillin-1 microfibril deposition is dependent on fibronectin assembly-Reference-Cited by-同舟云学术

Fibrillin-1 microfibril deposition is dependent on fibronectin assembly

Published:2008-08-15 Issue:16 Volume:121 Page:2696-2704
ISSN:1477-9137
Container-title:Journal of Cell Science
language:en
Short-container-title:

Author:

Kinsey Rachel¹,Williamson Matthew R.¹,Chaudhry Shazia¹,Mellody Kieran T.¹,McGovern Amanda¹,Takahashi Seiichiro²,Shuttleworth C. Adrian¹,Kielty Cay M.¹

Affiliation:

1. Wellcome Trust Centre for Cell-Matrix Research, Faculty of Life Science, Michael Smith Building, Oxford Road, University of Manchester, Manchester M13 9PT, UK

2. Max Planck Institute of Biochemistry, Department of Molecular Medicine, Am Klopferspitz 18, 82152 Martinsried, Germany

Abstract

Newly deposited microfibrils strongly colocalise with fibronectin in primary fibroblasts. Microfibril formation is grossly inhibited by fibronectin depletion, but rescued by supplementation with exogenous cellular fibronectin. As integrin receptors are key determinants of fibronectin assembly, we investigated whether they also influenced microfibril deposition. Analysis of β1-integrin-receptor-null fibroblasts, blockage of cell surface integrin receptors that regulate fibronectin assembly and disruption of Rho kinase all result in suppressed deposition of both fibronectin and microfibrils. Antibody activation of β1 integrins in fibronectin-depleted cultures is insufficient to rescue microfibril assembly. In fibronectinRGE/RGE mutant mouse fibroblast cultures, which do not engage α5β1 integrin, extracellular assembly of both fibronectin and microfibrils is markedly reduced. Thus, pericellular microfibril assembly is regulated by fibronectin fibrillogenesis.

Publisher

The Company of Biologists

Subject

Cell Biology

Link

http://journals.biologists.com/jcs/article-pdf/121/16/2696/1505375/2696.pdf

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