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dc.contributor.authorRichards, Jeffrey G.-
dc.contributor.authorWang, Yuxiang S.-
dc.contributor.authorBrauner, Colin John-
dc.contributor.authorGonzalez, Richard J.-
dc.contributor.authorPatrick, Marjorie L.-
dc.contributor.authorSchulte, Patricia-
dc.contributor.authorChoppari-Gomes, A. R.-
dc.contributor.authorVal, Vera Maria Fonseca Almeida e-
dc.contributor.authorVal, Adalberto Luis-
dc.date.accessioned2020-06-15T22:02:30Z-
dc.date.available2020-06-15T22:02:30Z-
dc.date.issued2007-
dc.identifier.urihttps://repositorio.inpa.gov.br/handle/1/18676-
dc.description.abstractWe examined the metabolic and ionoregulatory responses of the Amazonian cichlid, Astronotus ocellatus, to 20 h exposure to severe hypoxia (0.37 ± 0.19 mg O2/l; 4.6% air saturation) or 8 h severe hypoxia followed by 12 h recovery in normoxic water. During 20 h exposure to hypoxia, white muscle [ATP] was maintained at normoxic levels primarily through a 20% decrease in [creatine phosphate] (CrP) and an activation of glycolysis yielding lactate accumulation. Muscle lactate accumulation maintained cytoplasmic redox state ([NAD+]/[NADH]) and was associated with an inactivation of the mitochondrial enzyme pyruvate dehydrogenase (PDH). The inactivation of PDH was not associated with significant changes in cytoplasmic allosteric modulators ([ADPfree], redox state, or [pyruvate]). Hypoxia exposure caused a ∼65% decrease in gill Na+/K+ ATPase activity, which was not matched by changes in Na+/K+ ATPase α-subunit protein abundance indicating post-translational modification of Na+/K+ ATPase was responsible for the decrease in activity. Despite decreases in gill Na+/K+ ATPase activity, plasma [Na+] increased, but this increase was possibly due to a significant hemoconcentration and fluid shift out of the extracellular space. Hypoxia caused an increase in Na+/K+ ATPase α-subunit mRNA abundance pointing to either reduced mRNA degradation during exposure to hypoxia or enhanced expression of Na+/K + ATPase α-subunit relative to other genes. © 2007 Springer-Verlag.en
dc.language.isoenpt_BR
dc.relation.ispartofVolume 177, Número 3, Pags. 361-374pt_BR
dc.rightsRestrito*
dc.subjectAdenosine Triphosphatase (potassium Sodium)en
dc.subjectAdenosine Triphosphateen
dc.subjectCreatineen
dc.subjectCreatine Phosphateen
dc.subjectGlycogenen
dc.subjectHemoglobinen
dc.subjectIonen
dc.subjectLactate Dehydrogenaseen
dc.subjectLactic Aciden
dc.subjectRna, Messengeren
dc.subjectOxygenen
dc.subjectPyruvate Dehydrogenase Complexen
dc.subjectPyruvic Aciden
dc.subjectAdaptationen
dc.subjectAnimalsen
dc.subjectAnoxiaen
dc.subjectBlooden
dc.subjectCichliden
dc.subjectEnzymologyen
dc.subjectFast Muscle Fiberen
dc.subjectGeneticsen
dc.subjectGillen
dc.subjectGlucose Blood Levelen
dc.subjectHematocriten
dc.subjectKidneyen
dc.subjectLiveren
dc.subjectMean Corpuscular Volumeen
dc.subjectMetabolismen
dc.subjectPathophysiologyen
dc.subjectPhen
dc.subjectPhysiologyen
dc.subjectAdaptation, Physiologicalen
dc.subjectAdenosine Triphosphateen
dc.subjectAnimalen
dc.subjectAnoxiaen
dc.subjectBlood Glucoseen
dc.subjectCichlidsen
dc.subjectCreatineen
dc.subjectErythrocyte Indicesen
dc.subjectGillsen
dc.subjectGlycogenen
dc.subjectHematocriten
dc.subjectHemoglobinsen
dc.subjectHydrogen-ion Concentrationen
dc.subjectIonsen
dc.subjectKidneyen
dc.subjectL-lactate Dehydrogenaseen
dc.subjectLactic Aciden
dc.subjectLiveren
dc.subjectMuscle Fibers, Fast-twitchen
dc.subjectOxygenen
dc.subjectPhosphocreatineen
dc.subjectPyruvate Dehydrogenase Complexen
dc.subjectPyruvic Aciden
dc.subjectRna, Messengeren
dc.subjectSodium-potassium-exchanging Atpaseen
dc.subjectAstronotus Ocellatusen
dc.subjectCichlidaeen
dc.titleMetabolic and ionoregulatory responses of the Amazonian cichlid, Astronotus ocellatus, to severe hypoxiaen
dc.typeArtigopt_BR
dc.identifier.doi10.1007/s00360-006-0135-2-
dc.publisher.journalJournal of Comparative Physiology B: Biochemical, Systemic, and Environmental Physiologypt_BR
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