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© 1993 SAGE Publications Localization and Characterization of a Parotid Ca2+-Dependent Ecto-ATPaseDepartment of Pharmacology, School of Medicine, Creighton University, California at 24th Street, Omaha, NE 68178
Department of Pharmacology, School of Medicine, Creighton University, California at 24th Street, Omaha, NE 68178
Department of Pharmacology, School of Medicine, Creighton University, California at 24th Street, Omaha, NE 68178
Department of Molecular Pathology, Box 89, M.D. Anderson Cancer Center, 1515 Holcombe Blvd, Houston, TX 77030 Parotid acini were isolated and tested to further establish the presence of ecto-ATPase in the intact cells. Inhibitors were used to determine if the inhibitor profile of the ATPase was similar to that of a Ca2+-ATPase from parotid membranes identified previously as an ecto-ATPase. The Ca 2+-ATPase of intact cells was insensitive to oligomycin (10 µg/ml), N-ethylmaleimide (NEM) (0.1 mM), ruthenium red (0.1 mM), sodium azide (1 mM), and was inhibited approximately 22% by sodium orthovanadate (Na3VO4) (1 mM). This profile was similar to the Ca2+-ATPase of intact cells. Trifluoperazine (TFP) (0.1 m M) inhibited the enzyme in intact cells by approximately 32%. The nucleotide substrate specificity of the enzyme also reflected very closely the pattern seen in isolated membranes.
Key Words: ecto-ATPase • calcium • ATP.
Critical Reviews in Oral Biology & Medicine, Vol. 4, No. 3,
415-419 (1993) This article has been cited by other articles:
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