Enzymatic mechanisms during temperature acclimation of the blue crab, Callinectes sapidus—II. Kinetic and thermodynamic studies of glucose-6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase

Robert, Marjorie; Gray, Irving

doi:10.1016/0305-0491(72)90255-6

Cited by 5 publications

(1 citation statement)

References 8 publications

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“…Comparing previous studies (Walford, 1964; Liu & Walford, 1966; Walford et al. , 1969; Moon & Hochachka, 1971; Robert & Gray, 1972; McCarter et al. , 1985; McDevitt & Speakman, 1994; Lane et al.…”

Section: Discussionmentioning

confidence: 71%

Ambient temperature influences aging in an annual fish (Nothobranchius rachovii)

Hsu

Chiu

2009

Aging Cell

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SummaryExtending lifespan by lowering ambient temperature in the habitat has been shown in a variety of organisms. Its mechanism, however, remains elusive. In this study, we examined the survivorship and the aging process of the annual fish (Nothobranchius rachovii) reared under high (30°C), moderate (25°C) and low (20°C) ambient temperatures. The results showed that low ambient temperatures prolong survivorship, whereas high ambient temperatures shorten survivorship. At low ambient temperature, expression of senescence-associated b-galactosidase, lipofuscin, reactive oxygen species, lipid peroxidation, protein oxidation, mitochondrial density and ADP ⁄ ATP ratio were reduced compared with those reared at high and moderate temperatures, whereas catalase activity, Mn-superoxide dismutase activities, mitochondrial membrane potential and the levels of ATP, ADP, Sirt1 and Forkhead box O expression were elevated. The expression levels of Hsp70 and CIRP showed no significant difference under any of the ambient temperatures tested. We concluded that cellular metabolism, energy utilization and gene expression are altered at lower ambient temperature, which is associated with the extension of lifespan of the annual fish.

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Section: Discussionmentioning

confidence: 71%

Ambient temperature influences aging in an annual fish (Nothobranchius rachovii)

Hsu

Chiu

2009

Aging Cell

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Adaptation ofDrosophila enzymes to temperature. III. Evolutionary conservatism in mitochondrial enzymes

Alahiotis

1980

J Mol Evol

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The evolutionary behavior of two mitochondrial enzymnes (L-glycerol 3-phosphate:cytochrome c oxidoreductase E.C.1.1.1.95, alpha GPO, and L-malate: NAD+ oxidoreductase, E.C.1.1.1.37, m-MDH) obtained from several temperate and tropical Drosophila species was examined by comparing their catalytic properties, which related to temperature (Km-Ea-Q10-Thermostability). Mitochondrial alpha GPO or m-MDH obtained either from template or from tropical species was found to exhibit similar catalytic properties while for both cytosolic enzymes, the alpha GPDH and s-MDH, Km patterns were similar among species from the same thermal habitat and different thermal habitats. In combination with other observations reported in the literature these facts support the view that the function, and probably the structure, of mitochondrial enzymes are better conserved in evolution than those of the corresponding enzymes found in the cytosol. It is proposed that the relative invariance of the mitochondrial enzymes structure is probably linked to a necessary relative invariance of molecular interactions inside the mitochondrion.

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Regulation d'activité de l'α-Amylase à différentes températures d'adaptation et en fonction de l'ablation des pédoncules oculaires et du stade de mue chez Palaemon serratus

Wormhoudt

1980

Biochemical Systematics and Ecology

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Enzymatic mechanisms during temperature acclimation of the blue crab, Callinectes sapidus—II. Kinetic and thermodynamic studies of glucose-6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase

Cited by 5 publications

References 8 publications

Ambient temperature influences aging in an annual fish (Nothobranchius rachovii)

Ambient temperature influences aging in an annual fish (Nothobranchius rachovii)

Adaptation ofDrosophila enzymes to temperature. III. Evolutionary conservatism in mitochondrial enzymes

Regulation d'activité de l'α-Amylase à différentes températures d'adaptation et en fonction de l'ablation des pédoncules oculaires et du stade de mue chez Palaemon serratus

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