PMID- 10510450
OWN - NLM
STAT- MEDLINE
DCOM- 20000104
LR  - 20181113
IS  - 0007-1188 (Print)
IS  - 0007-1188 (Linking)
VI  - 128
IP  - 2
DP  - 1999 Sep
TI  - Functional expression of a cDNA encoding a human ecto-ATPase.
PG  - 396-402
AB  - 1 The metabolism of extracellular nucleotides plays an important role in
      nucleotide signalling mediated by P2 receptors. The nucleotide sequence encoding 
      a putative human ecto-ATPase named CD39L1 was reported recently. However, the
      biological activity of this protein has not been established. 2 Based on the
      sequence of CD39L1 we isolated from mRNA from human ECV-304 cells a sequence
      encoding a 495 amino acid protein that is identical to CD39L1, with the exception
      that this sequence contains a 23 amino acid stretch in the putative extracellular
      loop that is missing in CD39L1. Partial sequence of a genomic DNA clone indicates
      that the CD39L1 gene corresponds to an alternative spliced form of the human
      ecto-ATPase. 3 Stable expression of isolated sequence in NIH-3T3 mouse
      fibroblasts conferred a marked nucleotide hydrolytic activity consistent with the
      activity of an ecto-ATPase. 4 The human ecto-ATPase hydrolyzed all naturally
      occurring nucleoside triphosphates in a Ca(2+)- or Mg(2+)-dependent manner.
      Nucleoside diphosphates were hydrolyzed at a rate approximately 5% of that of the
      corresponding triphosphates. The apparent Km and Vmax values were: 394+/-62
      microM and 107+/-7 nmol Pi min-1 10(6) cells-1 for the hydrolysis of ATP, and
      102+/-33 microM and 4+/-0.4 nmol Pi min-1 10(6) cells-1 for the hydrolysis of
      ADP, respectively. 5 In conclusion, we report here the cloning and functional
      expression of a human ecto-ATPase. The study of the biochemical properties and
      the regulatory mechanisms of ecto-ATPases of defined sequence will be valuable in
      the definition of their role in nucleotide signalling.
FAU - Mateo, J
AU  - Mateo J
AD  - Department of Pharmacology, The School of Medicine, University of North Carolina,
      Chapel Hill, North Carolina, NC 27599, USA.
FAU - Harden, T K
AU  - Harden TK
FAU - Boyer, J L
AU  - Boyer JL
LA  - eng
GR  - R29 HL054889/HL/NHLBI NIH HHS/United States
GR  - P01 HL034322/HL/NHLBI NIH HHS/United States
GR  - HL 34322/HL/NHLBI NIH HHS/United States
GR  - R01 HL054889/HL/NHLBI NIH HHS/United States
GR  - R01 GM038213/GM/NIGMS NIH HHS/United States
GR  - GM 38213/GM/NIGMS NIH HHS/United States
GR  - HL54889/HL/NHLBI NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - England
TA  - Br J Pharmacol
JT  - British journal of pharmacology
JID - 7502536
RN  - 0 (DNA, Complementary)
RN  - 0 (Phosphates)
RN  - EC 3.6.1.- (Adenosine Triphosphatases)
RN  - EC 3.6.1.- (ectoATPase)
SB  - IM
MH  - Adenosine Triphosphatases/*biosynthesis/genetics
MH  - Amino Acid Sequence
MH  - Animals
MH  - Base Sequence
MH  - Chickens
MH  - Chromatography, High Pressure Liquid
MH  - Cloning, Molecular
MH  - DNA, Complementary/*biosynthesis/genetics
MH  - Fibroblasts/metabolism
MH  - Humans
MH  - Liver Neoplasms, Experimental/enzymology
MH  - Mice
MH  - Molecular Sequence Data
MH  - Open Reading Frames
MH  - Phosphates/metabolism
MH  - Rats
MH  - Substrate Specificity
MH  - Tumor Cells, Cultured
PMC - PMC1571647
EDAT- 1999/10/08 00:00
MHDA- 1999/10/08 00:01
CRDT- 1999/10/08 00:00
PHST- 1999/10/08 00:00 [pubmed]
PHST- 1999/10/08 00:01 [medline]
PHST- 1999/10/08 00:00 [entrez]
AID - 10.1038/sj.bjp.0702805 [doi]
PST - ppublish
SO  - Br J Pharmacol. 1999 Sep;128(2):396-402. doi: 10.1038/sj.bjp.0702805.