Human placental ecto-enzymes: Studies on theplasma membrane anchorage and effect of inhibitors of ATP-metabolizing enzymes

Chayet L.; Collados, L; Kettlun A.M.; Traverso-Cori A.; Garcia, L.; Valenzuela M.. A; Campos, E.

Keywords: inhibition, enzyme, membrane, placenta, degradation, binding, protein, cell, caffeine, alkaline, apyrase, humans, human, nucleotides, female, lidocaine, inhibitors, article, phosphatase, 5'-nucleotidase, analysis, c, phospholipase, microvilli, fluphenazine, priority, journal, D, phosphatidylinositol, Endopeptidases, amitriptyline, Glycosylphosphatidylinositols, Diacylglycerol-Lyase


The human placental microvillar membrane contains several ectoenzymes, including 5'-nucleotidase, alkaline phosphatase and ATP-diphosphohydrolase (ATP-DPH), which might be involved in the extracellular metabolism of nucleotides. The type of anchorage to the plasma membrane of the two first enzymes has been shown to be via a glycosyl-phosphatidylinositol. In the present study, using an enzymatic approach, we show that the ATP-DPH should be attached to the plasma membrane through a different type of anchorage. We were also interested in the search of compounds which could interact differentially with this enzyme to be used as a tool for studying the other two hydrolytic enzymes in the presence of ATP-DPH. Here we report several inhibitors of ecto-ATPases which seem to be a useful tool for studying these three enzymes.

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Título de la Revista: Research Communications in Molecular Pathology and Pharmacology
Volumen: 96
Número: 1
Fecha de publicación: 1997
Página de inicio: 14
Página final: 24