Selective integrin subunit reduction disrupts fibronectin extracellular matrix deposition and fibrillin 1 gene expression.

Publisher: Springer Country of Publication: Netherlands NLM ID: 0364456 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1573-4919 (Electronic) Linking ISSN: 03008177 NLM ISO Abbreviation: Mol Cell Biochem Subsets: MEDLINE

Publication: New York : Springer
Original Publication: The Hague, Dr. W. Junk B. V. Publishers.

Integrin alpha5*/genetics ; Integrin alpha5*/metabolism ; Integrin alphaV*/genetics ; Integrin alphaV*/metabolism; Extracellular Matrix/*metabolism ; Microfilament Proteins/*metabolism; Cell Adhesion ; Cell Line, Tumor ; Fibrillin-1 ; Fibrillins ; Fibronectins/metabolism ; Gene Expression Regulation ; Humans ; Integrin alpha2/genetics ; Integrin alpha2/metabolism ; Integrin beta3/genetics ; Integrin beta3/metabolism ; Integrins ; Microfilament Proteins/genetics ; Osteosarcoma/metabolism ; RNA, Small Interfering ; Retinal Pigment Epithelium/cytology ; Retinal Pigment Epithelium/metabolism

Integrins are transmembrane receptors that can specifically bind extracellular matrix (ECM) proteins. Assembly of the ECM protein fibronectin into fibrils has been shown to be a cell-mediated process that requires integrins. Like fibronectin, fibrillin 1 is an ECM glycoprotein that can assemble into fibrils, but the role of integrins in fibril formation is not understood. To investigate the role of integrins in fibrillin 1 ECM deposition, cells that normally produce and assemble fibrillin 1 fibers in vitro were stably transfected with plasmid constructs encoding short interfering RNAs that target specific integrin subunits. Cells that were deficient in α2- and β3-integrin subunits produced and deposited fibronectin normally, but cells that were deficient for α5 and αV were unable to elaborate a fibronectin matrix, although they continued to produce and secrete the protein. Surprisingly, the cells that were unable to elaborate a fibronectin matrix also lost fibrillin 1 gene expression.

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R03 AR 049887-02 United States AR NIAMS NIH HHS

0 (FBN1 protein, human)
0 (Fibrillin-1)
0 (Fibrillins)
0 (Fibronectins)
0 (Integrin alpha2)
0 (Integrin alpha5)
0 (Integrin alphaV)
0 (Integrin beta3)
0 (Integrins)
0 (Microfilament Proteins)
0 (RNA, Small Interfering)

Date Created: 20120712 Date Completed: 20130410 Latest Revision: 20211021

20250114

10.1007/s11010-012-1383-y

22782528