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D Gershon

Publications and source records attributed to D Gershon.

At least 199 records · Page 11Linked to original sources

The effect of age on the protein degradation system in the nematode Turbatrix aceti.

The administration of 0.2% of the amino acid analogues canavanine and 6-fluorotryptophan to young nematode cultures caused the appearance of inactive but antigenically reactive aldolase molecules at levels comparable to those found in old untreated cultures. Concomitant with the rapid appearance of inactive enzyme molecules a rapid rate of mortality could be detected. Mortality, however, ceased when a massive disappearance of inactive molecules could be observed. Subsequently, mortality resumed at a rate similar to that found in untreated cultures. The NaH14CO3 method of Swick and Ip (J. Biol. Chem., 249 (1974) 6836-6841) was used to estimate the half-life of proteins. The half-life of total soluble proteins in old and intermediate age animals was 4 times and 2.5 times longer, respectively, than that of young nematodes. No differences could be discerned in the half-lives of total proteins between analogue-treated and control animals of young and intermediate ages. However, the rate of disposal of inactive molecules was slower in intermediate age as compared to young animals as it was closely related to the general rate of protein degradation in the different age groups. The results suggest that (a) the proportion of inactive enzyme molecules encountered in old animals is potentially detrimental, (b) the decline in efficiency of the degradation system in older animals may account for the accumulation of altered protein molecules in aging organisms.

Aging↗

Current status of age altered enzymes: alternative mechanisms.

The occurrence of inactive enzyme molecules in a variety of tissues and animal species has been shown to be of a general nature. The levels of inactive enzyme molecules found in old animals were produced by amino acid analogs in young animals. These levels have been shown to be initially detrimental but subsequently the young system shows recovery by efficiently disposing of the analog-modified proteins. In old animals this disposal is considerably less efficient. Evidence is presented which suggests that post-translational modifications of proteins are the main cause of enzyme inactivation in old animals. Amino acid substitutions and modifications involving charge differences apparently do not contribute significantly to this phenomenon.

Acetylation↗

Rat-liver superoxide dismutase. Purification and age-related modifications.

Cytoplasmic superoxide dismutase has been purified from livers of young (6 months) and old (27 months) rats. The enzyme purified from old animals shows an age-related reduction in the specific activity, accumulation of antigenically cross-reacting material and increased sensitivity to temperature. No differences were found in the molecular weight, electrophoretic mobility, antigenicity and Ki between enzymes purified from young and old rats. This is the first demonstration of age-related alterations in a purified form of a non-metabolic enzyme, which can be related to reduced activity. The possible role of this reduced activity in age-dependent deterioration of cellular functions is discussed.

Aging↗

Inactive enzyme molecules in aging mice: liver aldolase.

Evidence is presented that there is a considerable accumulation of inactive fructose-1,6-diphosphate aldolase (EC 4.1.2.7) in the liver of senescent mice. Liver aldolase was purified from 3-month-old mice and used to immunize rabbits. It was demonstrated with the monospecific antibody thus produced that the liver aldolase of young adult (3 month) and aged (31 month) mice are antigenically identical. With the antibody, inactive enzyme molecules (crossreacting material) in liver homogenate of old mice were detected. The liver aldolase of senescent mice had half as much active enzyme per mg of protein, as well as per antigenic unit, as did the liver aldolase of young adult mice. The accumulation of faulty enzyme molecules may be one of the causes of debilitation leading to senescence and death.

Aging↗