PMID: 11332599May 3, 2001Paper

Inhibition of the ecto-ATPdiphosphohydrolase of Schistosoma mansoni by thapsigargin

Bioscience Reports
S M MartinsS T Ferreira

Abstract

ATPdiphosphohydrolases (ATPDases) are ubiquitous enzymes capable of hydrolyzing nucleoside di- and triphosphates. Although a number of possible physiological roles have been proposed for ATPDases, detailed studies on structure-function relationships have generally been hampered by the lack of specific inhibitors of these enzymes. We have previously characterized a Ca2+-activated ATPDase on the external surface of the tegument of Schistosoma mansoni, the etiologic agent of human schistosomiasis. In the present work, we have examined the effects of thapsigargin, a sesquiterpene lactone known as a high affinity inhibitor of sarco-endoplasmic reticulum calcium transport (SERCA) ATPase, on ATPDase activity. Whereas other lactones tested had little or no inhibitory action, thapsigargin inhibited ATP hydrolysis by the ATPDase (K(i) approximately 20 microM). Interestingly, hydrolysis of ADP was not inhibited by thapsigargin. The lack of inhibition of ATPase activity by orthovanadate, a specific inhibitor of P-type ATPases, and the inhibition of the Mg2+-stimulated ATP hydrolysis by thapsigargin ruled out the possibility that the observed inhibition of the ATPDase by thapsigargin could be due to the presence of contaminating SERCA ATPas...Continue Reading

Citations

Nov 10, 2013·Future Microbiology·Cornelia SpethGünter Rambach
Jan 6, 2017·Molecules : a Journal of Synthetic Chemistry and Natural Product Chemistry·Chonny Herrera AcevedoMarcus Tullius Scotti
Jul 6, 2019·Current Protein & Peptide Science·Lara Soares Aleixo de CarvalhoAdemar Alves da Silva Filho
Jul 15, 2020·International Journal of Biological Macromolecules·Priscila Silva Grijó FaraniPriscila Faria-Pinto

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