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Sphingosine‐1‐phosphate inhibits extracellular matrix protein‐induced haptotactic motility but not adhesion of B16 mouse melanoma cells
Author(s) -
Sadahira Yoshito,
Zheng Mingzhe,
Ruan Fuqiang,
Hakomori Sen-itiroh,
Igarashi Yasuyuki
Publication year - 1994
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(94)80180-0
Subject(s) - motility , sphingosine 1 phosphate , extracellular matrix , sphingosine , microbiology and biotechnology , chemistry , adhesion , extracellular , focal adhesion , sphingolipid , melanoma , biophysics , biochemistry , biology , phosphorylation , receptor , cancer research , organic chemistry
Sphingosine‐1‐phosphate (Sph‐1‐P), the initial product of Sph catabolism, inhibited chemotactic motility of a few lines of tumor cells [(1992) Proc. Natl. Acad. Sci. USA 89, 9686]. We now report that Sph‐1‐P even at very low concentration (10–100 nM) inhibits integrin‐dependent motility of melanoma cells induced by extracellular matrix (ECM), although it did not affect integrin‐dependent adhesion to ECM. Other Sph‐related compounds tested (including sphinganine‐1‐P) were much less effective than Sph‐1‐P at inhibiting motility, and also had no effect on integrin‐dependent adhesion of tumor cells to ECM. Our findings suggest that Sph‐1‐P inhibits actin filament reorganization by affecting cytoplasmic connection to integrin in ECM‐stimulated motility of melanoma cells.