Please use this identifier to cite or link to this item: http://hdl.handle.net/2440/44832
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Type: Journal article
Title: Sphingosine kinase 1 is a critical component of the copper-dependent FGF1 export pathway
Author: Soldi, R.
Mandinova, A.
Venkataraman, K.
Hla, T.
Vadas, M.
Pitson, S.
Duarte, M.
Graziani, I.
Kolev, V.
Kacer, D.
Kirov, A.
Maciag, T.
Prudovsky, I.
Citation: Experimental Cell Research, 2007; 313(15):3308-3318
Publisher: Academic Press Inc Elsevier Science
Issue Date: 2007
ISSN: 0014-4827
1090-2422
Statement of
Responsibility: 
Raffaella Soldi, Anna Mandinova, Krishnan Venkataraman, Timoty Hla, Mathew Vadas, Stuart Pitson, Maria Duarte, Irene Graziani, Vihren Kolev, Doreen Kacer, Aleksandr Kirov, Thomas Maciag and Igor Prudovsky
Abstract: Sphingosine kinase 1 catalyzes the formation of sphingosine-1-phosphate, a lipid mediator involved in the regulation of angiogenesis. Sphingosine kinase 1 is constitutively released from cells, even though it lacks a classical signal peptide sequence. Because copper-dependent non-classical stress-induced release of FGF1 also regulates angiogenesis, we questioned whether sphingosine kinase 1 is involved in the FGF1 release pathway. We report that (i) the coexpression of sphingosine kinase 1 with FGF1 inhibited the release of sphingosine kinase 1 at 37 degrees C; (ii) sphingosine kinase 1 was released at 42 degrees C in complex with FGF1; (iii) sphingosine kinase 1 null cells failed to release FGF1 at stress; (iv) sphingosine kinase 1 is a high affinity copper-binding protein which formed a complex with FGF1 in a cell-free system, and (v) sphingosine kinase 1 over expression rescued the release of FGF1 from inhibition by the copper chelator, tetrathiomolybdate. We propose that sphingosine kinase 1 is a component of the copper-dependent FGF1 release pathway.
Keywords: Cells, Cultured; NIH 3T3 Cells; Fibroblasts; Animals; Mice, Knockout; Mice; Copper; Molybdenum; Phosphotransferases (Alcohol Group Acceptor); Fibroblast Growth Factor 1; Chelating Agents; Cloning, Molecular; Temperature; Protein Transport
Description: Copyright © 2007 Elsevier Inc. All rights reserved.
RMID: 0020072442
DOI: 10.1016/j.yexcr.2007.05.031
Description (link): http://www.elsevier.com/wps/find/journaldescription.cws_home/622826/description#description
Appears in Collections:Molecular and Biomedical Science publications

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