Role of matrix metalloprotease-2 in oxidant activation of Ca2+ ATPase by hydrogen peroxide in pulmonary vascular smooth muscle plasma membrane.

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dc.contributor.authorMandal, Malayen_US
dc.contributor.authorDas, Sudipen_US
dc.contributor.authorChakraborti, Tapatien_US
dc.contributor.authorMandal, Amritlalen_US
dc.contributor.authorChakraborti, Sajalen_US
dc.date.accessioned2003-03-25en_US
dc.date.accessioned2009-06-01T14:33:23Z
dc.date.available2003-03-25en_US
dc.date.available2009-06-01T14:33:23Z
dc.date.issued2003-03-25en_US
dc.description.abstractExposure of bovine pulmonary artery smooth muscle plasma membrane suspension with the oxidant H2O2 (1 mM) stimulated Ca2+ATPase activity. We sought to determine the role of matrix metalloprotease-2 (MMP-2) in stimulating Ca2+ATPase activity by H2O2 in the smooth muscle plasma membrane. The smooth muscle membrane possesses a Ca2+-dependent protease activity in the gelatin containing zymogram having an apparent molecular mass of 72 kDa. The 72 kDa protease activity was found to be inhibited by EGTA, 1 : 10-phenanthroline, a2-macroglobulin and tissue inhibitor of metalloprotease-2 (TIMP-2) indicating that the Ca2+-dependent 72 kDa protease is the MMP-2. Western immunoblot studies of the membrane suspension with polyclonal antibodies of MMP-2 and TIMP-2 revealed that MMP-2 and TIMP-2, respectively, are the ambient matrix metalloprotease and the corresponding tissue inhibitor of metalloprotease in the membrane. In addition to increasing the Ca2+ATPase activity, H2O2 also enhanced the activity of the smooth muscle plasma membrane associated protease activity as evidenced by its ability to degrade 14C-gelatin. The protease activity and the Ca2+ATPase activity were prevented by the antioxidant, vitamin E, indicating that the effect produced by H2O2 was due to reactive oxidant species(es). Both basal and H2O2 stimulated MMP-2 activity and Ca2+ATPase activity were inhibited by the general inhibitors of matrix metalloproteases: EGTA, 1 : 10-phenanthroline, a2-macroglobulin and also by TIMP-2 (the specific inhibitor of MMP-2) indicating that H2O2 increased MMP-2 activity and that subsequently stimulated Ca2+ATPase activity in the plasma membrane. This was further confirmed by the following observations: (i) adding low doses of MMP-2 or H2O2 to the smooth muscle membrane suspension caused submaximal increase in Ca2+ATPase activity, and pretreatment with TIMP-2 prevents the increase in Ca2+ATPase activity; (ii) combined treatment of the membrane with low doses of MMP-2 and H2O2 augments further the Ca2+ATPase activity caused by the respective low doses of either H2O2 or MMP-2; and (iii) pretreatment with TIMP-2 prevents the increase in Ca2+ATPase activity in the membrane caused by the combined treatment of MMP-2 and H2O2.en_US
dc.description.affiliationDepartment of Biochemistry and Biophysics, University of Kalyani, Kalyani 741 235, India.en_US
dc.identifier.citationMandal M, Das S, Chakraborti T, Mandal A, Chakraborti S. Role of matrix metalloprotease-2 in oxidant activation of Ca2+ ATPase by hydrogen peroxide in pulmonary vascular smooth muscle plasma membrane. Journal of Biosciences. 2003 Mar; 28(2): 205-13en_US
dc.identifier.urihttps://imsear.searo.who.int/handle/123456789/110910
dc.language.isoengen_US
dc.source.urihttps://www.ias.ac.in/jbiosci/index.htmlen_US
dc.subject.meshAnimalsen_US
dc.subject.meshCalcium-Transporting ATPases --metabolismen_US
dc.subject.meshCattleen_US
dc.subject.meshCell Membrane --drug effectsen_US
dc.subject.meshEnzyme Activationen_US
dc.subject.meshHydrogen Peroxide --pharmacologyen_US
dc.subject.meshLung --blood supplyen_US
dc.subject.meshMatrix Metalloproteinase 2 --metabolismen_US
dc.subject.meshMuscle, Smooth, Vascular --drug effectsen_US
dc.titleRole of matrix metalloprotease-2 in oxidant activation of Ca2+ ATPase by hydrogen peroxide in pulmonary vascular smooth muscle plasma membrane.en_US
dc.typeJournal Articleen_US
dc.typeResearch Support, Non-U.S. Gov'ten_US
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