Sphingosine-1-phosphate lyase SPL is an endoplasmic reticulum-resident, integral membrane protein with the pyridoxal 5′-phosphate binding domain exposed to the cytosol
作者： Mika Ikeda , Akio Kihara , Yasuyuki Igarashi
DOI: 10.1016/J.BBRC.2004.10.036
关键词: Endoplasmic reticulum 、 Integral membrane protein 、 STIM1 、 Sphingosine-1-phosphate 、 Binding domain 、 Biology 、 Biochemistry 、 Lyase 、 Lyase activity 、 Cytosol
摘要: Sphingosine-1-phosphate (S1P) is a sphingolipid metabolite that functions as bioactive lipid molecule. S1P degraded either by lyase or phosphohydrolase. The gene encoding mammalian lyase, SPL, has been identified. Here, we characterize the SPL protein in its expression, localization, and topology. expression levels of correlated well with dihydrosphingosine-1-phosphate (DHS1P) activity most tissues. However, liver heart exhibited high DHS1P activities compared to their levels. mRNA was temporally regulated during mouse embryonal development. Immunofluorescence microscopy demonstrated localized at endoplasmic reticulum. Proteinase K digestion studies revealed large hydrophilic domain, containing active site, faces cytosol. This site orientation opposite phosphohydrolase, indicating degradation two S1P-degrading enzymes occurs spatially separated sides
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sci-hub.se 参考文章(34)
P.P. Van Veldhoven, G.P. Mannaerts, Subcellular localization and membrane topology of sphingosine-1-phosphate lyase in rat liver. Journal of Biological Chemistry. ,vol. 266, pp. 12502- 12507 ,(1991) , 10.1016/S0021-9258(18)98927-1
Gia K Voeltz, Melissa M Rolls, Tom A Rapoport, Structural organization of the endoplasmic reticulum EMBO Reports. ,vol. 3, pp. 944- 950 ,(2002) , 10.1093/EMBO-REPORTS/KVF202
R. W. Keenan, Kazuhiko. Okabe, The degradation of tritiated dihydrosphingosine in the intact rat. Biochemistry. ,vol. 7, pp. 2696- 2701 ,(1968) , 10.1021/BI00847A037
Shimon Gatt, Yechezkel Barenholz, Degradation of sphingosine bases by cell-free preparations. α-hydroxy palmitic acid, an intermediate of phytosphingosine degradation Biochemical and Biophysical Research Communications. ,vol. 32, pp. 588- 594 ,(1968) , 10.1016/0006-291X(68)90277-5
Susan PYNE, Nigel J. PYNE, Sphingosine 1-phosphate signalling in mammalian cells Biochemical Journal. ,vol. 349, pp. 385- 402 ,(2000) , 10.1042/0264-6021:3490385
Karl-Anders Karlsson, On the chemistry and occurrence of sphingolipid long-chain bases. Chemistry and Physics of Lipids. ,vol. 5, pp. 6- 43 ,(1970) , 10.1016/0009-3084(70)90008-3
Y. Igarashi, Functional Roles of Sphingosine, Sphingosine 1-Phosphate, and Methylsphingosines: In Regard to Membrane Sphingolipid Signaling Pathways Journal of Biochemistry. ,vol. 122, pp. 1080- 1087 ,(1997) , 10.1093/OXFORDJOURNALS.JBCHEM.A021865
Åke Nilsson, Kjell Ragnar Reistad, Bengt Lindberg, P. Karrer, Akira Shimizu, Conversion of dihydrosphingosin to palmitaldehyde and palmitic acid with cell-free preparations of guinea pig intestinal mucosa Acta Chemica Scandinavica. ,vol. 24, pp. 598- 604 ,(1970) , 10.3891/ACTA.CHEM.SCAND.24-0598
Julie D. Saba, Futoshi Nara, Alicia Bielawska, Steven Garrett, Yusuf A. Hannun, The BST1 Gene of Saccharomyces cerevisiaeIs the Sphingosine-1-phosphate Lyase * Journal of Biological Chemistry. ,vol. 272, pp. 26087- 26090 ,(1997) , 10.1074/JBC.272.42.26087
Akio Kihara, Mika Ikeda, Yuki Kariya, Eun-Young Lee, Yong-Moon Lee, Yasuyuki Igarashi, Sphingosine-1-phosphate lyase is involved in the differentiation of F9 embryonal carcinoma cells to primitive endoderm. Journal of Biological Chemistry. ,vol. 278, pp. 14578- 14585 ,(2003) , 10.1074/JBC.M211416200