Please use this identifier to cite or link to this item:
Scopus Web of Science® Altmetric
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
Statement of
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):
Appears in Collections:Molecular and Biomedical Science publications

Files in This Item:
There are no files associated with this item.

Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.