These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: Inhibition of calmodulin-stimulated (Ca2+ + Mg2+)-ATPase activity by dimethyl sulfoxide.
    Author: McConnell EJ, Wagoner MJ, Keenan CE, Raess BU.
    Journal: Biochem Pharmacol; 1999 Jan 01; 57(1):39-44. PubMed ID: 9920283.
    Abstract:
    Membrane-bound (Ca2+ + Mg2+)-ATPase activity from human erythrocyte white ghosts in the calmodulin-activated state was inhibited by DMSO in concentrations of 3% (v/v) and above. At 10%, DMSO inhibited calmodulin activation by 47.7%, while basal, calmodulin-independent (Ca2+ + Mg2+)-ATPase and (Mg2+)-ATPase activity remained unaffected. (Na+ + K+)-ATPase activity was also reduced but exhibited a greater IC50. Concentration-effect analyses showed the inhibition by 10% DMSO to be a reversible, non-competitive effect with regard to calmodulin, Ca2+, and substrate activation. Calmodulin-stimulated processes may be more susceptible to inhibition by DMSO than related enzymatic catalysis, and thus may help explain the multitude of reported cellular events caused by the solvent. Furthermore, DMSO affected membrane-associated enzymatic mechanisms opposite to those reported for purified enzyme outside its native membrane environment.
    [Abstract] [Full Text] [Related] [New Search]