Age Differences in Lactic and Malic Dehydrogenases in the Rat

Schmukler, Morton; Barrows, Charles H.

doi:10.1093/geronj/21.1.109

Cited by 29 publications

(7 citation statements)

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“…The latter tissue is a target organ for androgens, suggesting that hormonal control differences may also modify enzymes in their response to age [Mainwaring, 1967], Species differences were evident on comparison with enzyme levels reported in human arterial tissue [Kirk 1958[Kirk , 1959[Kirk , 1962b and c] and rat liver and kidneys [Barrows and Roeder, 1961;Schmukler and Barrows, 1966],…”

Section: Discussionmentioning

confidence: 99%

Enzyme Patterns in Young and Old Mouse Livers and Lungs

Wilson¹

1972

Gerontology

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Enzyme assays in young (3–10 days), adult (6 months), middle-aged (18 months) and old (30 months) male and female C57 and C3H (6 and 12 months) mouse livers and lungs revealed complex patterns of change. Alkaline phosphatase, acid phosphatase, β-glucuronidase, G6PDH, LDH, SDH, cytochrome oxidase, glucose-6-phosphatase, 5′-nucleotidase, glycogen phosphorylase, phosphoglucomutase, ATPase and NAD dia-phorase were measured. In livers of males glycogen phosphorylase was unchanged; acid phosphatase and phosphoglucomutase increased; and glucose-6-phosphatase decreased with age. In livers of females similar patterns of change were found except that 5′-nucleo-tidase was constant; ATPase increased with age. In lungs of males glycogen phosphorylase was unchanged, alkaline phosphatase and phosphoglucomutase increased while acid phosphatase and NAD diaphorase decreased with age. In lungs of females many enzymes showed a different pattern. Acid and alkaline phosphatases, G6PDH, LDH and 5′-nucleotidase were constant and ATPase increased with age. Many enzymes showed either a high peak of activity at 18 months or a decrease in activity with age until 18 months followed by an increase. Light and electron microscope histochemistry showed no changes in enzyme localisation with age. The most common quantitative changes with age were found in the mitochondrial enzymes SDH which showed peak activity at 18 months and LDH which showed peak activity at 6 months.

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Section: Discussionmentioning

confidence: 99%

Enzyme Patterns in Young and Old Mouse Livers and Lungs

Wilson¹

1972

Gerontology

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“…Although the changes are specific to the type of muscle studied, there appears overall to be a reduction in the activities of various enzymes in the skeletal muscles of diabetic and aged animals. In addition to a generalized reduction in protein synthesis lactate dehydrogenase, α‐glycerol‐3‐phosphate dehydrogenase, hexokinase and citrate synthase activities are reduced in both aging and diabetes 63–71 . Some similarities in the histological changes, such as single fiber atrophy, are also occasionally noted.…”

Section: Other Tissues and Cell Products With Slow Turnover Ratementioning

confidence: 99%

Tissue Specificity of Premature Aging in Diabetes Mellitus The Role of Cellular Replicative Capacity

Mooradian

1988

J American Geriatrics Society

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“…aldolase [21], enzymes of the aerobic part of glucose degradation, namely SDH1 [21], but also PDH [38] and MDH [57], are reduced in activity up to 50%. LDH, which could be considered functionally as being inbetween the anaerobic (end of glycolysis) and aerobic energy metabolism (dependence of NAD+ for oxidation of lactate to pyruvate) becomes less active as well [36,57], Perhaps, besides the in creased requirement of carbohydrate for glycolytic degradation, this is the reason why also glycogen decreases by 50% in muscles of old rats [62], Lactate augments correspondingly [2], We therefore can conclude that the aerobic part of energy metabolism is considerably reduced in its activ ity, and with it ATP synthesis. An age-dependent shift from a predomi nantly aerobic to a more anaerobic metabolism is observed also in heart muscle, and the suggestion is made that the heart adapts itself this way to the reduced aerobic ATP production [25,26].…”

Section: The a Tp-providing Systemmentioning

confidence: 99%

Ageing Changes in Mammalian Skeletal Muscle

Ermini¹

1976

Gerontology

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In the course of ageing, biochemical characteristics of mammalian skeletal muscle are shown to become altered mainly within the system of energy metabolism. The enzymatic behaviour of myofibrillar proteins remains virtually unchanged throughout life, but a gradual loss of fibres causes a decrease in muscular strength. Working capacity, however, in terms of prolonged muscular work is considerably reduced with age, because of a less efficient energy metabolism. Enzymes, particularly of the Krebs cycle, show diminished specific activities, and consequently, ATP and phosphocreatine concentrations are lowered. Possible primary and secondary factors responsible for these changes are discussed.

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Age Differences in Lactic and Malic Dehydrogenases in the Rat

Cited by 29 publications

References 0 publications

Enzyme Patterns in Young and Old Mouse Livers and Lungs

Enzyme Patterns in Young and Old Mouse Livers and Lungs

Tissue Specificity of Premature Aging in Diabetes Mellitus The Role of Cellular Replicative Capacity

Ageing Changes in Mammalian Skeletal Muscle

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