Sphingosine‐1‐phosphate inhibits extracellular matrix protein‐induced haptotactic motility but not adhesion of B16 mouse melanoma cells

FEBS Letters

Zheng, Mingzhe¹  Ruan, Fuqiang¹  Hakomori, Sen-itiroh¹  Sadahira, Yoshito¹  Igarashi, Yasuyuki¹ 

[1] The Biomembrane Institute, 201 Elliott Ave W, Seattle, WA 98119, USA

关键词: Sphingosine-1-phosphate;    Cell motility;    Cell adhesion;    Matrix protein;    Actin filament;    Haptotaxis;    Cer;    ceramide;    DMS;    dimethyl-sphingosine;    ECM;    extracellular matrix;    FN;    fibronectin;    FNR;    fibronectin receptor(s);    LM;    laminin;    Sph;    Sphingosine;    Sph-1-P;    Sphingosine-1-phosphate;    TMS;    trimethyl-sphingosine;   

DOI  :  10.1016/0014-5793(94)80180-0

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown