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Sphingolipid-to-glycerophospholipid conversion in SPL-null cells implies the existence of an alternative isozyme.
Biochem Biophys Res Commun 2005; 329(2):474-9BB

Abstract

Sphingosine-1-phosphate (S1P) lyase catalyzes the cleavage of the bioactive lipid molecule S1P to phosphoethanolamine and hexadecenal, both of which are utilized as glycerophospholipid precursors. Until now, only one gene, SPL, has been identified as encoding a S1P lyase. In the present study, SPL-null F9 cells were able to convert radiolabeled dihydrosphingosine to glycerophospholipids, albeit at much lower efficiency than parent cells. Lysates prepared from the SPL-null cells exhibited weak but significant dihydrosphingosine-1-phosphate lyase activity in vitro. These results provide evidence of the existence of an alternative S1P lyase.

Authors+Show Affiliations

Department of Biomembrane and Biofunctional Chemistry, Graduate School of Pharmaceutical Sciences, Hokkaido University, Kita 12-jo, Nishi 6-choume, Kita-ku, Sapporo 060-0812, Japan.No affiliation info availableNo 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

15737611

Citation

Ikeda, Mika, et al. "Sphingolipid-to-glycerophospholipid Conversion in SPL-null Cells Implies the Existence of an Alternative Isozyme." Biochemical and Biophysical Research Communications, vol. 329, no. 2, 2005, pp. 474-9.
Ikeda M, Kihara A, Kariya Y, et al. Sphingolipid-to-glycerophospholipid conversion in SPL-null cells implies the existence of an alternative isozyme. Biochem Biophys Res Commun. 2005;329(2):474-9.
Ikeda, M., Kihara, A., Kariya, Y., Lee, Y. M., & Igarashi, Y. (2005). Sphingolipid-to-glycerophospholipid conversion in SPL-null cells implies the existence of an alternative isozyme. Biochemical and Biophysical Research Communications, 329(2), pp. 474-9.
Ikeda M, et al. Sphingolipid-to-glycerophospholipid Conversion in SPL-null Cells Implies the Existence of an Alternative Isozyme. Biochem Biophys Res Commun. 2005 Apr 8;329(2):474-9. PubMed PMID: 15737611.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Sphingolipid-to-glycerophospholipid conversion in SPL-null cells implies the existence of an alternative isozyme. AU - Ikeda,Mika, AU - Kihara,Akio, AU - Kariya,Yuki, AU - Lee,Yong-Moon, AU - Igarashi,Yasuyuki, PY - 2005/01/31/received PY - 2005/3/2/pubmed PY - 2005/5/6/medline PY - 2005/3/2/entrez SP - 474 EP - 9 JF - Biochemical and biophysical research communications JO - Biochem. Biophys. Res. Commun. VL - 329 IS - 2 N2 - Sphingosine-1-phosphate (S1P) lyase catalyzes the cleavage of the bioactive lipid molecule S1P to phosphoethanolamine and hexadecenal, both of which are utilized as glycerophospholipid precursors. Until now, only one gene, SPL, has been identified as encoding a S1P lyase. In the present study, SPL-null F9 cells were able to convert radiolabeled dihydrosphingosine to glycerophospholipids, albeit at much lower efficiency than parent cells. Lysates prepared from the SPL-null cells exhibited weak but significant dihydrosphingosine-1-phosphate lyase activity in vitro. These results provide evidence of the existence of an alternative S1P lyase. SN - 0006-291X UR - https://www.unboundmedicine.com/medline/citation/15737611/Sphingolipid_to_glycerophospholipid_conversion_in_SPL_null_cells_implies_the_existence_of_an_alternative_isozyme_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0006-291X(05)00259-7 DB - PRIME DP - Unbound Medicine ER -