Developmental changes of the adenine nucleotide translocation in rat brain

Abstract

The perinatal development of the adenine nucleotide translocation in isolated rat brain mitochondria was studied. For that purpose the content of the adenine nucleotide translocase (ANT), the activity of adenine nucleotide translocation and the control of the ANT protein over State 3 respiration were estimated. From the newborn to the adult state there was a 4-fold increase in State 3 respiration which was paralleled by a 3-fold increase in the respiratory control ratio. The capacity of uncoupled respiration exceeded that of State 3 respiration in all developmental stages indicating that the activity of oxidative phosphorylation is influenced by that of ANT and/or ATP synthase. The content of the ANT protein, measured as bound pmoles of [3H]atractyloside per mg mitochondrial protein, increased more than 2-fold from birth to adultness in the first three postnatal weeks. The size of the exchangeable matrix (ATP + ADP)-pool was only slightly expanded during the same period. The translocation activity increased 2-fold from the newborn to the adult state and was a linear function of the ANT protein. Control of the ANT protein over State 3 respiration (quantified as flux control coefficient, CJoANT), was remarkable in brain mitochondria from newborn rats (CJoANT = 0.45 +/- 0.15), but declined during further development (CJoANT = 0.11 +/- 0.03, at the 20th day). The obtained results suggest that the postnatal enrichment of the ANT protein in rat brain mitochondria is an essential factor for the development of oxidative phosphorylation capacity in the early postnatal period.

Developmental changes in expression and subcellular localization of the DNA repair glycosylase, MYH, in the rat brain

“…1a). This is consistent with the requirement for ANT protein for mitochondrial function (Schonfeld and Bohnensack 1995). Thus, the presence of fast migrating MYH isoforms in the adult brain coincides with maturation of mitochondrial function and cessation of neuronal proliferation.…”

Changes in dihydrolipoamide dehydrogenase expression and activity during postnatal development and aging in the rat brain

“…Second, as energy demand and oxygen consumption increase postnatally, the activities of many mitochondrial enzymes involved in energy metabolism are gradually increased (Kalous, et al, 2001). These enzymes include adenine nucleotide translocase (Schonfeld and Bohnensack, 1995), creatine kinase (Holtzman, et al, 1993, Schonfeld andReiser, 2007), malic enzyme (Bukato, et al, 1992), the pyruvate dehydrogenase complex (Malloch, et al, 1986), the electron transport chain complexes (Almeida, et al, 1995, Bates, et al, 1994, Krebs cycle enzymes (Clark, et al, 1981, Leong and, glutamate dehydrogenase , as well as antioxidant enzymes such as superoxide dismutase, catalase and glutathione peroxidase (Mavelli, et al, 1982). To our knowledge, however, changes in rat brain DLDH expression and activity during postnatal development have not been reported.…”

Carnitine regulates myocardial metabolism by Peroxisome Proliferator-Activated Receptor-alpha (PPARalpha) in alcoholic cardiomyopathy

“…ADP and AMP were measured after enzymatic conversion to ATP. Phosphocreatine (Pcr) was measured using a bioluminescent technique modified according to Ellis and Gardner [16,17]. …”