dc.creatorMORENO, SNJ
dc.creatorDOCAMPO, R
dc.creatorVERCESI, AE
dc.date1992
dc.date45717
dc.date2014-12-16T11:36:29Z
dc.date2015-11-26T16:23:02Z
dc.date2014-12-16T11:36:29Z
dc.date2015-11-26T16:23:02Z
dc.date.accessioned2018-03-28T23:04:25Z
dc.date.available2018-03-28T23:04:25Z
dc.identifierJournal Of Biological Chemistry. Amer Soc Biochemistry Molecular Biology Inc, v. 267, n. 9, n. 6020, n. 6026, 1992.
dc.identifier0021-9258
dc.identifierWOS:A1992HK31800048
dc.identifierhttp://www.repositorio.unicamp.br/jspui/handle/REPOSIP/78293
dc.identifierhttp://www.repositorio.unicamp.br/handle/REPOSIP/78293
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/78293
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1268198
dc.descriptionWhen Trypanosoma brucei procyclic trypomastigotes were permeabilized with digitonin in a reaction medium containing MgATP, succinate, and 3.5-mu-M free Ca2+, they lowered the medium Ca2+ concentration to the submicromolar level (0-05-0.1-mu-M), a range that correlates favorably with that detected in the intact cells with fura-2. The carbonyl cyanide p-trifluoromethoxyphenylhydrazone-insensitive Ca2+ uptake, certainly represented by the endoplasmic reticulum, was completely inhibited by 500-mu-M vanadate. When vanadate instead of carbonyl cyanide p-trifluoromethoxyphenylhydrazone was present, the Ca2+ set point was increased to 0.6-0.7-mu-M. The succinate dependence and carbonyl cyanide p-trifluoromethoxyphenylhydrazone sensitivity of the later Ca2+ uptake indicate that it may be exerted by the mitochondria. When bloodstream trypomastigotes were used, neither succinate nor alpha-glycerophosphate stimulated the mitochondrial Ca2+ uptake. The mitochondrial Ca2+ transport could be measured only in the presence of ATP and 500-mu-M vanadate to inhibit the endoplasmic reticulum uptake. Bloodstream trypomastigotes have a lower cytosolic Ca2+ Concentration, as detected with fura-2 and a smaller extramitochondrial Ca2+ pool than procyclic trypomastigotes. Despite the presence of inositol phosphates, as determined by [H-3]inositol incorporation, and the large extramitochondrial Ca2+ pool of procyclic trypomastigotes (61.7 nmol of Ca2+/mg of protein), no inositol 1,4,5-trisphosphate-sensitive Ca2+ release could be detected in these parasites.
dc.description267
dc.description9
dc.description6020
dc.description6026
dc.languageen
dc.publisherAmer Soc Biochemistry Molecular Biology Inc
dc.publisherBethesda
dc.relationJournal Of Biological Chemistry
dc.relationJ. Biol. Chem.
dc.rightsfechado
dc.sourceWeb of Science
dc.subjectBlood-stream Forms
dc.subjectEpidermal Growth-factor
dc.subjectLeydig Tumor-cells
dc.subjectProtein Kinase-c
dc.subjectIntracellular Calcium
dc.subjectPartial-purification
dc.subjectSurface-coat
dc.subjectArsenazo-iii
dc.subjectCa-2+
dc.subjectMembrane
dc.titleCALCIUM HOMEOSTASIS IN PROCYCLIC AND BLOOD-STREAM FORMS OF TRYPANOSOMA-BRUCEI - LACK OF INOSITOL 1,4,5-TRISPHOSPHATE-SENSITIVE CA2+ RELEASE
dc.typeArtículos de revistas


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