Constancy of the NADP-linked isocitrate dehydrogenase/transhydrogenase ratios of mitochondria of different mammalian tissues

Chico, E.; Satrústegui, Jorgina; Machado, Alberto

doi:10.1016/s0300-9084(78)80709-3

Cited by 7 publications

(1 citation statement)

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“…It has been suggested that it could function in isocitrate oxidation through NADPH/NAD+ transhydrogenase (Stein et al, 1967). However, in heart the actual transhydrogenase activity could be coupled to no more than a fraction of the total NADPH produced through NADP+-dependent isocitrate dehydrogenase (Chico et al, 1977).…”

Section: 'Malic' Enzymementioning

confidence: 99%

Development of NADPH-producing pathways in rat heart

Andrés¹,

Satrústegui²,

Machado³

1980

Biochemical Journal

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The behaviours of the principal NADPH-producing enzymes (glucose 6-phosphate dehydrogenase, 6-phosphogluconate dehydrogenase, cytoplasmic and mitochondrial 'malic' enzyme and NAPD+-dependent isocitrate dehydrogenase) were studied during the development of rat heart and compared with those in brain and liver. 1. The enzymes belonging to the pentose phosphate pathway exhibit lower activities in heart than in other tissues throughout development. 2. The pattern of induction of heart cytoplasmic and mitochondrial 'malic' enzymes does not parallel that found in liver. Heart mitochondrial enzyme is slowly induced from birth onwards. 3. NADP+-dependent isocitrate dehydrogenase has similar activities in all tissues in 18-day foetuses. 4. Heart mitochondrial NADP+-dependent isocitrate dehydrogenase is greatly induced in the adult, where it attains a 10-fold higher activity than in liver. 5. The physiological functions of mitochondrial 'malic' enzyme and NADP+-dependent isocitrate dehydrogenase are discussed.

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Section: 'Malic' Enzymementioning

confidence: 99%