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Sphingosine 1-phosphate induces platelet/endothelial cell adhesion molecule-1 phosphorylation in human endothelial cells through cSrc and Fyn.
Cell Signal. 2008 Aug; 20(8):1521-7.CS

Abstract

Sphingosine 1-phosphate (S1P) is a multifunctional phospholipid which acts through a specific family of G protein-coupled receptors. Platelet/endothelial cell adhesion molecule-1 (PECAM-1) form trans-homophilic binding at lateral cell border. Upon stimulation, its cytoplasmic tyrosine residues could be phosphorylated and interact with various downstream signaling molecules. In this study, we demonstrated that S1P induced PECAM-1 tyrosine phosphorylation in human umbilical cord vein cells (HUVECs). By pharmacological inhibitors, it was suggested that G(i) and Src family kinases were involved in PECAM-1 phosphorylation. Moreover, cSrc and Fyn siRNA significantly suppressed S1P-induced PECAM-1 phosphorylation. These results suggested that S1P-induced PECAM-1 phosphorylation through G(i) and subsequent cSrc and Fyn. Our findings provide further understanding of S1P and PECAM-1 signaling as well as their functions in endothelial cells.

Authors+Show Affiliations

Institute of Zoology, National Taiwan University, No 1, Sec. 4, Roosevelt Rd., Taipei 10617, Taiwan, ROC.No affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

18502612

Citation

Huang, Yu-Ting, et al. "Sphingosine 1-phosphate Induces Platelet/endothelial Cell Adhesion Molecule-1 Phosphorylation in Human Endothelial Cells Through cSrc and Fyn." Cellular Signalling, vol. 20, no. 8, 2008, pp. 1521-7.
Huang YT, Chen SU, Chou CH, et al. Sphingosine 1-phosphate induces platelet/endothelial cell adhesion molecule-1 phosphorylation in human endothelial cells through cSrc and Fyn. Cell Signal. 2008;20(8):1521-7.
Huang, Y. T., Chen, S. U., Chou, C. H., & Lee, H. (2008). Sphingosine 1-phosphate induces platelet/endothelial cell adhesion molecule-1 phosphorylation in human endothelial cells through cSrc and Fyn. Cellular Signalling, 20(8), 1521-7. https://doi.org/10.1016/j.cellsig.2008.04.008
Huang YT, et al. Sphingosine 1-phosphate Induces Platelet/endothelial Cell Adhesion Molecule-1 Phosphorylation in Human Endothelial Cells Through cSrc and Fyn. Cell Signal. 2008;20(8):1521-7. PubMed PMID: 18502612.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Sphingosine 1-phosphate induces platelet/endothelial cell adhesion molecule-1 phosphorylation in human endothelial cells through cSrc and Fyn. AU - Huang,Yu-Ting, AU - Chen,Shee-Uan, AU - Chou,Chia-Hong, AU - Lee,Hsinyu, Y1 - 2008/04/18/ PY - 2008/01/23/received PY - 2008/03/21/revised PY - 2008/04/07/accepted PY - 2008/5/27/pubmed PY - 2008/9/23/medline PY - 2008/5/27/entrez SP - 1521 EP - 7 JF - Cellular signalling JO - Cell Signal VL - 20 IS - 8 N2 - Sphingosine 1-phosphate (S1P) is a multifunctional phospholipid which acts through a specific family of G protein-coupled receptors. Platelet/endothelial cell adhesion molecule-1 (PECAM-1) form trans-homophilic binding at lateral cell border. Upon stimulation, its cytoplasmic tyrosine residues could be phosphorylated and interact with various downstream signaling molecules. In this study, we demonstrated that S1P induced PECAM-1 tyrosine phosphorylation in human umbilical cord vein cells (HUVECs). By pharmacological inhibitors, it was suggested that G(i) and Src family kinases were involved in PECAM-1 phosphorylation. Moreover, cSrc and Fyn siRNA significantly suppressed S1P-induced PECAM-1 phosphorylation. These results suggested that S1P-induced PECAM-1 phosphorylation through G(i) and subsequent cSrc and Fyn. Our findings provide further understanding of S1P and PECAM-1 signaling as well as their functions in endothelial cells. SN - 0898-6568 UR - https://www.unboundmedicine.com/medline/citation/18502612/Sphingosine_1_phosphate_induces_platelet/endothelial_cell_adhesion_molecule_1_phosphorylation_in_human_endothelial_cells_through_cSrc_and_Fyn_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0898-6568(08)00120-4 DB - PRIME DP - Unbound Medicine ER -