Identification and characterization of an ecto-ATPase activity in rat Sertoli cells.
A membrane associated extracellular ATPase (ecto) has been identified on rat Sertoli cells. Sertoli cell ecto-ATPase demonstrated a Km for ATP of 114 muM and a V(max) of 1.79 mumol/min/2 x 10(5) cells and was activated by either Mg2+ or Ca2+. This ecto-ATPase hydrolyzes other nucleoside triphosphates, but is inactive with ADP. The effects of some possible inhibitors of ectonucleotidases on the breakdown of extracellular ATP by Sertoli cells were also investigated.
Barbacci
E
E
Institute of Histology and General Embryology, School of Medicine, La Sapienza University of Rome, Italy.
Filippini
A
A
De Cesaris
P
P
Ziparo
E
E
D000251:Adenosine Triphosphatases / Q000302:isolation & purification / Q000378:metabolism*; D000818:Animals; D002118:Calcium / Q000494:pharmacology; D002478:Cells, Cultured; D004492:Edetic Acid / Q000494:pharmacology; D004789:Enzyme Activation; D004791:Enzyme Inhibitors / Q000494:pharmacology; D007700:Kinetics; D008274:Magnesium / Q000494:pharmacology; D008297:Male; D051381:Rats; D017208:Rats, Wistar; D012708:Sertoli Cells / Q000201:enzymology*; D013379:Substrate Specificity
D004791:Enzyme Inhibitors; D004492:Edetic Acid; D000251:Adenosine Triphosphatases; C027201:ectoATPase; D008274:Magnesium; D002118:Calcium