期刊论文详细信息
FEBS Letters
N,N‐Dimethylsphingosine 1‐phosphate activates human platelets
Yamamura, Soichiro2  Ruan, Fuqiang2  Yatomi, Yutaka1  Igarashi, Yasuyuki2  Kume, Shoji1  Ozaki, Yukio1 
[1]Department of Laboratory Medicine, Yamanashi Medical University, Tamaho-cho, Nakakoma-gun, Yamanashi 409-38, Japan
[2]The Biomembrane Institute, Seattle, WA 98195, USA
关键词: N;    N-Dimethylsphingosine 1-phosphate;    N;    N-Dimethylsphingosine;    Sphingosine 1-phosphate;    Sphingolipid;    Platelet activation;    DMS-1-P;    N;    N-dimethylsphingosine 1-phosphate;    DMS;    N;    N-dimethylsphingosine;    Sph-1-P;    sphingosine 1-phosphate;    Sph;    sphingosine;    Cer;    ceramide;    Cer-1-P;    ceramide 1-phosphate;    SPC;    sphingosylphosphorylcholine;   
DOI  :  10.1016/S0014-5793(97)01321-5
学科分类:生物化学/生物物理
来源: John Wiley & Sons Ltd.
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【 摘 要 】

We recently reported that N,N-dimethylsphingosine 1-phosphate (DMS-1-P) can be formed from N,N-dimethylsphingosine (DMS) in activated platelets [Y. Yatomi et al., Biochem. Biophys. Res. Commun. 231 (1997) 848–851]. In this study, we synthesized, for the first time, DMS-1-P and examined the functional effects of DMS-1-P and its related sphingolipids on platelets. Although exogenous DMS was inactive, its phosphorylated derivative, DMS-1-P, induced platelet intracellular Ca2+ mobilization and shape change, but not aggregation or release reactions. Since sphingosine 1-phosphate (Sph-1-P) is structurally related to DMS-1-P and activates platelets more strongly than DMS-1-P, a competitive binding experiment for [3H]Sph-1-P was performed using DMS-1-P. DMS-1-P reduced the binding of [3H]Sph-1-P to platelets almost as much as unlabeled Sph-1-P did. These results suggest that DMS-1-P activates platelets via an interaction with a platelet surface receptor for Sph-1-P.

【 授权许可】

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