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THE COUPLING OF VINCULIN TO THE CYTOSKELETON IS NOT ESSENTIAL FOR MECHANO‐CHEMICAL SIGNALING IN F9 CELLS
Author(s) -
Goldmann Wolfgang H.
Publication year - 2002
Publication title -
cell biology international
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.932
H-Index - 77
eISSN - 1095-8355
pISSN - 1065-6995
DOI - 10.1006/cbir.2001.0854
Subject(s) - vinculin , microbiology and biotechnology , cytoskeleton , integrin , intracellular , fibronectin , signal transduction , calcium in biology , chemistry , cell culture , myosin light chain kinase , biology , cell , myosin , focal adhesion , biochemistry , extracellular matrix , genetics
It is well established that mechanical forces can regulate cell growth and guide tissue remodeling, yet little is known about how mechanical signals act at the cell surface membrane to produce biochemical changes in the cell. To explore this question, I used a mouse embryonic F9 vinculin‐deficient cell line (γ229), which, unlike wild‐type cells, shows no fibronectin‐dependent cell spreading. The wild‐type cell line exhibited a twofold increase in area over four hours. I observed (i) an earlier rise in intracellular free calcium from ∼0.2 to ∼3μ m in wild‐type compared with γ229 cells, thus similar calcium levels after 4h; (ii) an initial higher ratio of p‐MAP/MAP‐Kinase for γ229, but similar FA‐Kinase activation; and (iii) a marginal change in intracellular pH [pH] i in both F9 cell lines. When I applied controlled local stresses directly to integrin receptors using RGD‐coated magnetic beads, they displaced to a lesser extent in wild‐type than in γ229 cells. Both F9 cell lines showed a small stress‐dependent rise in [Ca 2+ ] i levels and similar PKA‐c activity. In summary, the mechanical linkage of integrin‐vinculin‐cytoskeleton seemed not to be essential for chemical signal transduction.