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Characterization of ATP and ADP hydrolysis activity in rat gastric mucosa
Author(s) -
Savegnago Lucielli,
Nogueira Cristina W.,
Fachinetto Roselei,
Rocha Joao Batista Teixeira
Publication year - 2005
Publication title -
cell biology international
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.932
H-Index - 77
eISSN - 1095-8355
pISSN - 1065-6995
DOI - 10.1016/j.cellbi.2005.03.010
Subject(s) - atp hydrolysis , gastric mucosa , hydrolysis , chemistry , biochemistry , microbiology and biotechnology , biology , enzyme , stomach , atpase
The degradation of nucleotides is catalyzed by the family of enzymes called nucleoside triphosphate diphosphohydrolases (NTPDases). The aim of this work was to demonstrate the presence of NTPDase in the rat gastric mucosa. The enzyme was found to hydrolyze ATP and ADP at an optimum pH of 8.0 in the presence of Mg 2+ and Ca 2+ . The inhibitors ouabain (0.01–1 mM), N ‐ethylmaleimide (0.01–4 mM), levamisole (0.10–0.2 mM) and Ap 5 A (0.03 mM) had no effect on NTPDase 1 activity. Sodium azide (0.03–30 mM), at high concentrations (>0.1 mM), caused a parallel hydrolysis inhibition of ATP and ADP. Suramin (50–300 μM) inhibited ATP and ADP hydrolysis at all concentrations tested. Orthovanadate slightly inhibited (15%) Mg 2+ and Ca 2+ ATP/ADPase at 100 μM. Lanthanum decreased Mg 2+ and Ca 2+ ATP/ADPase activities. The presence of NTPDase as ecto‐enzyme in the gastric mucosa may have an important role in the extracellular metabolism of nucleotides, suggesting that this enzyme plays a role in the control of acid and pepsin secretion, mucus production, and contractility of the stomach.