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Sphingosine‐1‐phosphate Inhibits Haptotactic Motility by Overproduction of Focal Adhesion Sites in B16 Melanoma Cells through EDG‐Induced Activation of Rho
Author(s) -
YAMAMURA S.,
HAKOMORI S.,
WADA A.,
IGARASHI Y.
Publication year - 2000
Publication title -
annals of the new york academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.712
H-Index - 248
eISSN - 1749-6632
pISSN - 0077-8923
DOI - 10.1111/j.1749-6632.2000.tb06566.x
Subject(s) - paxillin , focal adhesion , motility , microbiology and biotechnology , integrin , chemistry , sphingosine 1 phosphate , phosphorylation , ptk2 , cell adhesion , sphingosine , biology , cell , biochemistry , mitogen activated protein kinase kinase , receptor , protein kinase a
A bstract : We investigated the molecular mechanism by which Sph‐1‐P affects the FN‐dependent haptotactic motility of serum‐starved mouse melanoma B16/F10 cells. We found that EDG‐5‐induced Rho activation followed by enhanced tyrosine phosphorylation of FAK and paxillin, and β1‐integrin activation leading to overexpression of focal adhesion sites, as well as increment of stress fiber formation, must be the molecular basis of inhibition of haptotactic cell motility by Sph‐1‐P.