Fibrillin-1 microfibril deposition is dependent on fibronectin assembly

被引：115

作者：

Kinsey, Rachel ^{[1
]}

Williamson, Matthew R. ^{[1
]}

Chaudhry, Shazia ^{[1
]}

Mellody, Kieran T. ^{[1
]}

McGovern, Amanda ^{[1
]}

Takahashi, Seiichiro ^{[2
]}

Shuttleworth, C. Adrian ^{[1
]}

Kielty, Cay M. ^{[1
]}

机构：

[1] Univ Manchester, Fac Life Sci, Wellcome Trust Ctr Cell Matrix Res, Manchester M13 9PT, Lancs, England

[2] Max Planck Inst Biochem, Dept Mol Med, D-82152 Martinsried, Germany

来源：

JOURNAL OF CELL SCIENCE | 2008年 / 121卷 / 16期

基金：

英国医学研究理事会; 英国惠康基金;

关键词：

fibrillin-1; microfibrils; fibronectin; integrin; Rho kinase;

D O I：

10.1242/jcs.029819

中图分类号：

Q2 [细胞生物学];

学科分类号：

071009 ; 090102 ;

摘要：

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 beta 1-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 beta 1 integrins in fibronectin-depleted cultures is insufficient to rescue microfibril assembly. In fibronectin(RGE/RGE) mutant mouse fibroblast cultures, which do not engage alpha 5 beta 1 integrin, extracellular assembly of both fibronectin and microfibrils is markedly reduced. Thus, pericellular microfibril assembly is regulated by fibronectin fibrillogenesis.

引用

页码：2696 / 2704

页数：9

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