ZFIN ID: ZDB-PUB-091120-67
NTPDase family in zebrafish: Nucleotide hydrolysis, molecular identification and gene expression profiles in brain, liver and heart
Rosemberg, D.B., Rico, E.P., Langoni, A.S., Spinelli, J.T., Pereira, T.C., Dias, R.D., Souza, D.O., Bonan, C.D., and Bogo, M.R.
Date: 2010
Source: Comparative biochemistry and physiology. Part B, Biochemistry & molecular biology   155(3): 230-240 (Journal)
Registered Authors: Bonan, Carla Denise
Keywords: NTPDase, Zebrafish, Nucleotide hydrolysis, Phylogenetic analysis, Gene expression profiles
MeSH Terms:
  • Adenosine Diphosphate/metabolism*
  • Adenosine Triphosphate/metabolism*
  • Amino Acid Sequence
  • Animals
  • Brain/drug effects
  • Brain/metabolism
  • Computational Biology
  • Enzyme Inhibitors/pharmacology
  • Female
  • Gene Expression Profiling*
  • Heart/drug effects
  • Humans
  • Hydrolysis/drug effects
  • Liver/drug effects
  • Liver/metabolism
  • Male
  • Mice
  • Molecular Sequence Data
  • Myocardium/metabolism
  • Nucleoside-Triphosphatase/chemistry
  • Nucleoside-Triphosphatase/genetics*
  • Nucleoside-Triphosphatase/metabolism*
  • Phylogeny
  • Sequence Homology, Amino Acid
  • Zebrafish/genetics*
  • Zebrafish/metabolism*
PubMed: 19922813 Full text @ Comp. Biochem. Physiol. B Biochem. Mol. Biol.
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ABSTRACT
The nucleoside triphosphate diphosphohydrolase (NTPDase) family cleaves tri- and diphosphonucleosides to monophosphonucleosides and is responsible for terminating purinergic transmission. Since the NTPDase family in zebrafish is poorly understood, here we evaluated the nucleotide hydrolysis in three tissues of adult zebrafish (brain, liver, and heart), confirmed the presence of distinct NTPDase members by a phylogenetic analysis and verified their relative gene expression profiles in the respective tissues. A different profile of ATP and ADP hydrolysis in brain, liver, and heart as a function of time and protein concentration was observed. Sodium azide (20mM), ARL 67156 (300muM) and Suramin (300muM) differently altered the nucleotide hydrolysis in zebrafish tissues, suggesting the contribution of distinct NTPDase activities. Homology-based searches identified the presence of NTPDase1-6 and NTPDase8 orthologs and the phylogeny also grouped three NTPDase2 and two NTPDase5 paralogs. The deduced amino acid sequences share apyrase conserved regions, conserved cysteine residues, putative N-glycosylation, phosphorylation, N-acetylation sites, and different numbers of transmembrane domains. RT-PCR experiments revealed the existence of a distinct relative entpd1-6 and entpd8 expression profile in brain, liver, and heart. Taken together, these results indicate that several NTPDase members might contribute to a tight regulation of nucleotide hydrolysis in zebrafish tissues.
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