Sphingosine-1-phosphate inhibits extracellular matrix protein-induced haptotactic motility but not adhesion of B16 mouse melanoma cells.
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 integrin in ECM-stimulated motility of melanoma cells.
Sadahira
Y
Y
Biomembrane Institute, Seattle, WA 98119.
Zheng
M
M
Ruan
F
F
Hakomori
S
S
Igarashi
Y
Y
D000818:Animals; D002448:Cell Adhesion / Q000187:drug effects*; D002633:Chemotaxis / Q000187:drug effects*; D016326:Extracellular Matrix Proteins / Q000037:antagonists & inhibitors* / Q000494:pharmacology; D008246:Lysophospholipids; D008546:Melanoma, Experimental; D051379:Mice; D013110:Sphingosine / Q000031:analogs & derivatives* / Q000494:pharmacology; D014407:Tumor Cells, Cultured
D016326:Extracellular Matrix Proteins; D008246:Lysophospholipids; C060506:sphingosine 1-phosphate; D013110:Sphingosine