An electrophoretic study of protein synthesis in brain regions of senescent male mice

doi:10.1016/0531-5565(74)90024-2

Experimental Gerontology

Volume 9, Issues 5–6, November 1974, Pages 269-270

https://doi.org/10.1016/0531-5565(74)90024-2 Get rights and content

Abstract

C57BL/6J male mice of characterized health status were injected i.p. with ³H-leucine. Incorporation of ³H-leucine into 1 per cent Triton-saline soluble proteins of liver and brain regions did not change with age. In contrast, the patterns of ³H-leucine after gel electrophoresis indicated selective and regionally specific patterns of changes of protein synthesis during ageing.

Résumé

On injecte par voie i.p. de la leucine ³H à des souris mâles C57BL/6J en état de santé connu. L'incorporation de la leucine ³H dans les protéines de plusieurs régions du foie et du cervau, solubles dans une solution saline à 1% de triton, n'est pas modifiée avec l'âge. Au contraire, les pics de leucine ³H après électrophorèse sur gel indiquent qu'il y a avec l'âge des types de changement de la synthèse protéique qui sont sélectifs et variables selon la localisation.

Zusammenfassung

Männliche C57BL/6J-Mäuse vonbekanntem Gesundheitszustand erhielten intraperitoneale Injektionen von ³H-Leuzin. Der Einbau von ³H-Leuzin in Leber- und Hirnregionsproteine, welche in 1% Triton-Salzlösungen löslich waren, änderte sich nicht mit dem Alter. Im Gegensatz dazu waren die ³H-Leuzinmuster nach Gelelektrophorese ein Hinweis auf selektive und regional spezifische Muster der Veränderungen der Proteinsynthese mit dem Alter.

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Absence of age differences in protein synthesis by rat brain, measured with an initiating cell-free system
1987, Neurobiology of Aging
A cell-free protein synthesis system was derived from brains of young (3 month) and old (>23 month) male Fischer-344 rats in order to examine brain protein synthesis in relation to age. The system was shown to be capable of reinitiating protein synthesis in vitro, and of synthesizing protein from exogenously added mRNA. Optimal ionic conditions for amino acid incorporation were 200 mM potassium ion and 5 mM magnesium ion, and amino acid incorporation depended on addition of ATP, GTP, and an energy-generating system (creatine phosphate and creatine phosphokinase). Amino acid incorporation was sensitive to the initiation inhibitors aurintricarboxylic acid and sodium fluoride. Optimal conditions were independent of the age of the rat from which the brain was taken. There was no statistically significant relation (p>0.05) between capacity of amino acid incorporation and age. The aggregation state of brain polyribosomes also did not differ between young (3 month) and old (30 month) rats. The results suggest that overall brain protein synthesis capacity is age-invariant in the rat.
Regional analysis of rat brain proteins during senescence
1987, Experimental Gerontology
Brains of male Fischer-344 rats aged 3–4 months and 28–30 months were dissected into 11 regions, and the patterns of brain proteins in these regions were analyzed using two dimensional gel electrophoresis in conjunction with a sensitive silver stain detection method. Several hundred abundant and moderately abundant brain proteins were detected in each region using this method. At 3–4 months, most proteins were present in approximately equal amounts in each of the 11 regions. On the whole, this distribution was maintained as a function of age. One protein of 21 kdal pI 5.1 was present in the cerebellum in greater amount than the other regions at both 3–4 months and 28–30 months. Two proteins, 44 kdal pI 5.4 and 47 kdal pI 5.2 were present at increased levels in the inferior colliculus of 28–30 month animals compared to 3–4 month animals. Of the abundant and moderately abundant brain proteins detected by this method, there were none which showed major decreases in levels as a function of age. These results provide support for the concept that the molecular mechanisms which result in differential gene expression in different regions of the young adult rat brain are operative and are maintained in the brains of senescent rats.
Analysis of the translational capacity of the male accessory gland during aging in Acheta domesticus
1979, Mechanisms of Ageing and Development
The protein synthesizing capacity of the male cricket accessory gland was inspected for changes associated with aging by analysis of organs from young (2 weeks post-imaginal molt), middle-aged (4 and 6 weeks) and senescent (8 weeks) animals. Total RNA content and the percentage of ribosomes in polysomes show an increase up to 4 weeks and then a steady decline. The rates of protein synthesis by young and old glands incubated in vitro were comparable, although the old glands were significantly less efficient in precursor uptake and therefore showed lower incorporation levels. The overall picture appears to be one of a steady but unspectacular decline in protein synthesizing capacity in aging animals.
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Glutamine and ammonia metabolism in the brains of senescent mice
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The steady state levels of glutamine, glutamate, other amino acids, and ammonia were determined in the brains of mature and senescent C57B1/6J mice. Glutamine was the only amino acid which showed an age-related change. The glutamine concentration in the senescent mouse brain was approximately 50% greater than that in the mature mouse brain. The brain ammonia concentration was increased 60% in the old mice. Alos the activities of glutaminase and γ-glutamyltransferase were determined. These activities were changed very slightly as a function of age, and thus their levels probably do not account for the observed differences in glutamine and ammonia levels. These results indicate that in the brains of senescent mice, more glutamine is synthesized in an attempt to detoxify the higher levels of ammonia.

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^∗: Present address: Division of Medical Genetics, Cornell University Medical College, New York City, New York 10021, U.S.A.

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An electrophoretic study of protein synthesis in brain regions of senescent male mice

Abstract

Résumé

Zusammenfassung

Exp. Geront.

Brain Res.

Brain Res.

Brain Res.

J. Neurochem.

J. Neurochem.

Ann. N.Y. Acad. Sci.

J. Gen. Physiol.