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Modulation of Microvascular Smooth Muscle Adhesion and Mechanotransduction by Integrin‐linked Kinase
Author(s) -
Sun Zhe,
Huang Shaoxing,
Li Zhaohui,
MartinezLemus Luis A.,
Meininger Gerald A.
Publication year - 2010
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.24.1_supplement.779.2
Subject(s) - integrin linked kinase , microbiology and biotechnology , focal adhesion , integrin , chemistry , fibronectin , mechanotransduction , cell adhesion , vascular smooth muscle , paxillin , vinculin , signal transduction , cell , kinase , extracellular matrix , protein kinase a , biology , endocrinology , biochemistry , cyclin dependent kinase 2 , smooth muscle
Integrin‐linked kinase (ILK) is a multi‐functional protein that acts both as a kinase and as a scaffolding protein in focal adhesions (FA). In this study we investigated the involvement of ILK in the adhesion of arteriolar vascular smooth muscle cells (VSMC) to fibronectin (FN) and in the mechano‐responsiveness of VSMC FA. ILK was knocked down in VSMC using ILK‐shRNA constructs. Atomic force microscopy (AFM) was used to characterize VSMC interactions with FN, to measure VSMC stiffness and to apply and measure forces at a VSMC single FA site. ILK was localized to FA and silencing ILK promoted cell spreading, enhanced cell adhesion, reduced cell proliferation, increased number of FAs and altered the expression of vinculin, paxillin and hic‐5. Silencing of ILK also enhanced α5β1 integrin adhesion to FN, decreased cell stiffness and increased contractile responses to application of a pulling force at a single FN‐FA site. The function of ILK in arteriolar VSMC appears linked to signaling pathways leading to inhibition of cell spreading, cell adhesion, FA formation, and mechano‐responsiveness. (Supported by NIH HL58690 to G.A. Meininger)