Please use this identifier to cite or link to this item: http://www.repositorio.ufop.br/handle/123456789/7427
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dc.contributor.authorBrandão, Rogélio Lopes-
dc.contributor.authorRocha, Neuza Maria de Magalhaes-
dc.contributor.authorAlijo, Rafael-
dc.contributor.authorRamos, José-
dc.contributor.authorThevelein, Johan Maria-
dc.date.accessioned2017-03-22T17:00:11Z-
dc.date.available2017-03-22T17:00:11Z-
dc.date.issued1994-
dc.identifier.citationBRANDÃO, R. L. et al. Possible involvement of a phosphatidylinositol-type signaling pathway in glucose-induced activation of plasma membrane ATPase and cellular proton in the yeast Sacchamyces cerevisiae. Biochimica et Biophysica Acta. Molecular Cell Research, v. 1223, p. 117-124, 1994. Disponível em: <http://www.sciencedirect.com/science/article/pii/0167488994900809?np=y>. Acesso em: 10 jan. 2017.pt_BR
dc.identifier.issn1097-0061-
dc.identifier.urihttp://www.repositorio.ufop.br/handle/123456789/7427-
dc.description.abstractAddition of glucose to cells of the yeast Saccharomyces cerevisiae causes rapid activation of plasma membrane H+-ATPase and a stimulation of cellular H ÷ extrusion. We show that addition of diacylglycerol and other activators of protein kinase C to intact cells also activates the H+-ATPase and causes at the same time a stimulation of H ÷ extrusion from the cells. Both effects are reversed by addition of staurosporine, a protein kinase C inhibitor. Addition of staurosporine or calmidazolium, an inhibitor of Ca2+/calmodulin-dependent protein kinases, separately, causes a partial inhibition of glucose-induced H+-ATPase activation and stimulation of cellular H + extrusion; together they cause a more potent inhibition. Addition of neomycin, which complexes with phosphatidylinositol 4,5-bisphosphate, or addition of compound 48/80, a phospholipase C inhibitor, also causes near complete inhibition. Diacylglycerol and other protein kinase C activators had no effect on the activity of the K+-uptake system and the activity of trehalase and glucose-induced activation of the K+-uptake system and trehalase was not inhibited by neomycin, supporting the specificity of the effects observed on the H+-ATPase. The results support a model in which glucose-induced activation of H+-ATPase is mediated by a phosphatidylinositol-type signaling pathway triggering phosphorylation of the enzyme both by protein kinase C and one or more Ca2+/calmodulin-dependent protein kinases.pt_BR
dc.language.isoen_USpt_BR
dc.rightsrestritopt_BR
dc.subjectSignal transductionpt_BR
dc.subjectProtein kinase Cpt_BR
dc.subjectNeomycinpt_BR
dc.subjectMedium acidificationpt_BR
dc.titlePossible involvement of a phosphatidylinositol-type signaling pathway in glucose-induced activation of plasma membrane ATPase and cellular proton in the yeast Sacchamyces cerevisiae.pt_BR
dc.typeArtigo publicado em periodicopt_BR
dc.identifier.uri2http://www.sciencedirect.com/science/article/pii/0167488994900809?np=ypt_BR
dc.identifier.doihttps://doi.org/10.1016/0167-4889(94)90080-9-
Appears in Collections:DEFAR - Artigos publicados em periódicos

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