Sphingosine prevents diacylglycerol signaling to mitogen-activated protein kinase in airway smooth muscle
作者： D. Tolan , A. M. Conway , N. J. Pyne , S. Pyne
DOI: 10.1152/AJPCELL.1997.273.3.C928
关键词:
摘要: Because many agonists utilize diacylglycerol (DAG) to initiate nuclear transcriptional activity via protein kinase C (PKC), we have investigated whether sphingosine might counter DAG. Sphingosine inhibited PKC in an isolated airway smooth muscle cell lysate and prevented the activation of mitogen-activated (MAPK) by platelet-derived growth factor, bradykinin, phorbol 12-myristate 13-acetate intact cells. MAPK response all involves PKC. The stimulation [3H]palmitate-labeled cells with sphingosine, presence butan-1-ol (0.3%, vol/vol), induced increase [3H]phosphatidate (PtdOH) but was without effect on [3H]DAG. [3H]PtdOH synthesis inhibited, whereas [3H]DAG levels were increased DAG inhibitor R-59949, indicating that stimulates phospholipase C/DAG kinase. Recycling from PtdOH a sphingosine-dependent inhibition phosphohydrolase-2 activity. In conclusion, sphingosine-induced conversion may serve optimize MAPK. This account for antiproliferative action sphingosine.
strath.ac.uk
sci-hub.se 参考文章(26)
Susan PYNE, Nigel J. PYNE, The differential regulation of cyclic AMP by sphingomyelin-derived lipids and the modulation of sphingolipid-stimulated extracellular signal regulated kinase-2 in airway smooth muscle. Biochemical Journal. ,vol. 315, pp. 917- 923 ,(1996) , 10.1042/BJ3150917
M Liyanage, D Frith, S Stabel, K Vollmer, G Kour, O Sözeri, G E Mark rd, Activation of the c-Raf protein kinase by protein kinase C phosphorylation. Oncogene. ,vol. 7, pp. 2259- 2262 ,(1992)
B Lassègue, R W Alexander, M Clark, M Akers, K K Griendling, Phosphatidylcholine is a major source of phosphatidic acid and diacylglycerol in angiotensin II-stimulated vascular smooth-muscle cells. Biochemical Journal. ,vol. 292, pp. 509- 517 ,(1993) , 10.1042/BJ2920509
S C Jamdar, W F Cao, Properties of phosphatidate phosphohydrolase in rat adipose tissue. Biochemical Journal. ,vol. 301, pp. 793- 799 ,(1994) , 10.1042/BJ3010793
I N Fleming, S J Yeaman, Purification and characterization of N-ethylmaleimide-insensitive phosphatidic acid phosphohydrolase (PAP2) from rat liver Biochemical Journal. ,vol. 308, pp. 983- 989 ,(1995) , 10.1042/BJ3080983
Yaakov Lavie, Orly Piterman, Mordechai Liscovitch, Inhibition of phosphatidic acid phosphohydrolase activity by sphingosine FEBS Letters. ,vol. 277, pp. 7- 10 ,(1990) , 10.1016/0014-5793(90)80796-L
Sujoy Ghosh, Jay C. Strum, Vicki A. Sciorra, Larry Daniel, Robert M. Bell, Raf-1 kinase possesses distinct binding domains for phosphatidylserine and phosphatidic acid. Phosphatidic acid regulates the translocation of Raf-1 in 12-O-tetradecanoylphorbol-13-acetate-stimulated Madin-Darby canine kidney cells. Journal of Biological Chemistry. ,vol. 271, pp. 8472- 8480 ,(1996) , 10.1074/JBC.271.14.8472
A. Gomez-Muñoz, A. Martin, L. O'Brien, D.N. Brindley, Cell-permeable ceramides inhibit the stimulation of DNA synthesis and phospholipase D activity by phosphatidate and lysophosphatidate in rat fibroblasts. Journal of Biological Chemistry. ,vol. 269, pp. 8937- 8943 ,(1994) , 10.1016/S0021-9258(17)37058-8
Piero Crespo, Ningzhi Xu, William F. Simonds, J. Silvio Gutkind, Ras-dependent activation of MAP kinase pathway mediated by G-protein βγ subunits Nature. ,vol. 369, pp. 418- 420 ,(1994) , 10.1038/369418A0
R Seger, D Seger, A A Reszka, E S Munar, H Eldar-Finkelman, G Dobrowolska, A M Jensen, J S Campbell, E H Fischer, E G Krebs, Overexpression of mitogen-activated protein kinase kinase (MAPKK) and its mutants in NIH 3T3 cells. Evidence that MAPKK involvement in cellular proliferation is regulated by phosphorylation of serine residues in its kinase subdomains VII and VIII. Journal of Biological Chemistry. ,vol. 269, pp. 25699- 25709 ,(1994) , 10.1016/S0021-9258(18)47305-X