Cloning and characterization of rat sphingosine kinase 1 with an N-terminal extension

Sphingosine kinase (SK) is an enzyme that converts sphingosine to sphingosine 1-phosphate, a lysophospholipid with various cellular functions. Here, we report cloning and characterization of a novel isoform of rat SK1 (rSK1) with an N-terminal extension (long-rSK1). Long-rSK1 is 458 amino acid-long...

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Bibliographic Details
Published in:Biochemical and biophysical research communications 2007-12, Vol.364 (3), p.702-707
Main Authors: Park, Chang Gyo, Lee, Hyun Sil, Lee, Hoi Young, Park, Chang Shin, Choi, Oksoon Hong
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Animals
Cations, Divalent - metabolism
Cloning
Cloning, Molecular
Gene Expression Profiling
Gene Expression Regulation, Enzymologic
Isoenzymes - chemistry
Isoenzymes - genetics
Isoenzymes - metabolism
Kinetics
Molecular Sequence Data
Phosphotransferases (Alcohol Group Acceptor) - chemistry
Phosphotransferases (Alcohol Group Acceptor) - genetics
Phosphotransferases (Alcohol Group Acceptor) - metabolism
Rat long-sphingosine kinase 1
Rats
Rats, Wistar
Sphingosine 1-phosphate
Substrate Specificity
Tissue distribution
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Summary:Sphingosine kinase (SK) is an enzyme that converts sphingosine to sphingosine 1-phosphate, a lysophospholipid with various cellular functions. Here, we report cloning and characterization of a novel isoform of rat SK1 (rSK1) with an N-terminal extension (long-rSK1). Long-rSK1 is 458 amino acid-long and has a calculated molecular weight of 49.8kDa. Deduced amino acid sequences of rat and human long-SK1 have high homology (71.3% identity and 78.9% similarity). Long-rSK1 mRNA is widely expressed throughout the tissues including brain, heart, lung, liver, kidney, and spleen, whereas mRNA encoding rSK1 has been shown not to be expressed in heart or liver. When the long-rSK1 was transfected in COS-7 cells, SK activity was 53-fold increased. Substrate specificity and dependency on divalent cations of long-rSK1 were similar to those of rSK1. Taken together, the fact that long-rSK1 with similar enzymatic characteristics to rSK1 displays differential tissue distribution may suggest an additional role of long-rSK1.
ISSN:0006-291X
1090-2104
DOI:10.1016/j.bbrc.2007.10.075