C-terminal splicing of NTPDase2 provides distinctive catalytic properties, cellular distribution and enzyme regulation

The Biochemical Journal
Carol J H WangP R Thorne

Abstract

The present study provides functional characterization of alternative splicing of the NTPDase2 (ecto-nucleoside triphosphate diphosphohydrolase-2) involved in the regulation of extracellular nucleotide concentrations in a range of organ systems. A novel NTPDase2beta isoform produced by alternative splicing of the rat NTPDase2 gene provides an extended intracellular C-terminus and distinguishes itself from NTPDase2alpha isoform in gaining several intracellular protein kinase CK2 (casein kinase 2) phosphorylation sites and losing the intracellular protein kinase C motif. The plasmids containing NTPDase2alpha or NTPDase2beta cDNA were used to stably transfect Chinese-hamster ovary-S cells. Imaging studies showed that NTPDase2alpha was predominantly membrane-bound, whereas NTPDase2beta had combined cell surface and intracellular localization. alpha and beta isoforms showed variations in divalent cation dependence and substrate specificity for nucleoside-5'-triphosphates and nucleoside-5'-diphosphates. NTPDase2beta exhibited reduced ATPase activity and no apparent ADPase activity. NTPDase2 isoforms demonstrated similar sensitivity to inhibitors such as suramin and pyridoxal phosphate-6-azophenyl-2',4'-disulphonic acid, and different...Continue Reading

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Citations

Apr 13, 2011·Purinergic Signalling·Aileen F Knowles
May 5, 2012·Purinergic Signalling·Herbert ZimmermannNorbert Sträter
Jan 21, 2011·Nucleic Acids Research·Eyal MorNoam Shomron
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Aug 23, 2012·Gene·Olga KelemenStefan Stamm
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Dec 20, 2014·Purinergic Signalling·Débora A GonzálezMariano A Ostuni
May 11, 2010·The Journal of Biological Chemistry·Barbara C BöckWilfried Roth
Mar 11, 2010·Clinical Cancer Research : an Official Journal of the American Association for Cancer Research·Chandra BartholomeuszNaoto T Ueno

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