Cell-free protein synthesis by kidney from the aging female Fischer F344 RAT

Hardwick, James P.; Hsieh, Wen Hao; Liu, Daniel S H; Richardson, Arlan

doi:10.1016/0005-2787(81)90223-9

Cited by 28 publications

(7 citation statements)

References 32 publications

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“…Our system, therefore, allowed us to measure the rates of protein synthesis accurately in suspensions of whole kidney cells. The rates of protein synthesis that we measured in the suspensions of kidney cells were approximately 100-fold greater than the rates of cell-free protein synthesis reported by Hardwick et al (1981). We found that a 63% decline in the rate of total kidney cell protein synthesis occurred between 4 and 23 months of age with no significant decline thereafter (Table 1).…”

Section: Discussioncontrasting

confidence: 62%

“…To measure accurately protein synthesis in vivo or in tissue slices by the incorporation of radioactively-labelled amino acids into protein, one must measure the specific activity of the amino acid precursor pool. In order to minimize or eliminate the problems encountered in measuring protein synthesis in vivo, Hardwick et al (1981) measured the protein synthetic activity of kidneys from female Fischer F344 rats of various ages using a cell-free system. A 72% decline in kidney protein synthesis was observed between 4.5 and 31 months of age.…”

Section: Discussionmentioning

confidence: 99%

“…Despite the extensive characterization of the effect of aging on the physiological function and histological structure of the kidney, very little information is currently available on kidney protein synthesis as a function of age. Hardwick et al (1981) reported that the cell-free protein synthetic activity of kidney tissue from Fischer F344 rats decreases dramatically with age. Because cell-free protein synthesis systems have only about one percent of the protein synthetic activity of cells in vivo (Henshaw et al, 1971;Waterlow, 19751, we were interested in studying the effect of aging on protein synthesis i n a system that would more closely reflect the in vivo situation.…”

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Effect of age and dietary restriction on protein synthesis by isolated kidney cells

Ricketts

Birchenall-Sparks

Hardwick

et al. 1985

Journal Cellular Physiology

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The influence of age and food restriction on kidney protein synthesis was studied in Fischer F344 rats. The rate of total protein synthesis by suspensions of kidney cells declined 60% between 4 and 31 months of age. The rate of protein synthesis by kidney cells isolated from 19-month old rats fed a restricted diet (60% of diet consumed by rats fed ad libitum) was 45% higher than the rate of protein synthesis by kidney cells isolated from 19-month old rats fed ad libitum. The excretion of protein in the urine was measured to assess the effect of the age related decline in protein synthesis on kidney function. A dramatic increase in proteinuria was observed with increasing age, and rats fed the restricted diet excreted significantly less protein in the urine than rats fed ad libitum.

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Section: Discussioncontrasting

confidence: 62%

Section: Discussionmentioning

confidence: 99%

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confidence: 99%

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Effect of age and dietary restriction on protein synthesis by isolated kidney cells

Ricketts

Birchenall-Sparks

Hardwick

et al. 1985

Journal Cellular Physiology

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“…Recently, cell-free protein synthesis was examined in whole kidneys from female Fischer 344 rats of ages 4 5 , 7-5, 22 and 31 months (Hardwick et al, 1981). A 73-87 yo decline in [3H]valine incorporation into protein was observed between 4-5 and 3 I months of age.…”

Section: Rationale For the Study Of Protein Metabolism During Agingmentioning

confidence: 99%

“…Recently, Hardwick et al (1981) examined translational fidelity by measuring poly( U)-directed [l4C]pheny1alanine and [3H]leucine incorporation by kidney ribosomes isolated from female Fischer 344 rats of various ages; no age-dependent change in the fidelity of translation was found.…”

Section: ( I ) Ribosome Structure and Polyribosomesmentioning

confidence: 99%

Protein Synthesis and Degradation During Aging and Senescence

Makrides

1983

Biological Reviews

171

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Summary 1. The published results on protein synthesis during aging are contradictory. Possible sources of error and variability include: an insufficient number of different animal ages used; use of whole organs that are cytologically highly heterogeneous; different animal strains; neglecting to measure the specific activity of the precursor pool for protein synthesis; and inadequate methodology for measurement of in vivo rates of protein synthesis. 2. In general, protein synthesis rates in mammals have been reported to decline 4–70% with age. In insects and other organisms, greater losses (60–90%) have been observed. 3. Limited evidence indicates that in some systems a decline in the rate of protein synthesis may be due to alterations (as yet of unknown nature) in the initiation components of the protein synthetic apparatus. Futhermore, some studies suggest that in some organisms aging affects the expression of specific parts of the genome. 4. The significance of results on protein metabolism obtained from some studies with nematodes is at present unknown, owing to problems associated with age‐synchronization methods. Also, the in vitro fibroblast system for the study of human cellular aging has not been met with universal acceptance; it is generally believed that this system has not yet been established as a valid analogy to mammalian aging in vivo. 5. Failure to detect defective enzymes in many old organisms indicates at least that not all proteins are altered during aging. The complete thermal stability of purified enzymes from old organisms suggests that the observed thermolability of the same enzymes in crude cell extracts is not an intrinsic property of those enzymes. Post‐translational modifications (partial denaturation) may constitute the primary mechanism for the production of altered cell polypeptides during aging. 6. The available evidence does not support the concept of an age‐dependent decline in translational accuracy. The future purification to absolute homogeneity of an altered enzyme and its ‘young’ (unaltered) counterpart, and their sequencing, should resolve the question of translational errors. 7. Some degree of age‐related ribosome loss appears to occur in fixed postmitotic cells. In general, the published polyribosomal profiles may represent artefacts due to insufficiently suppressed ribonuclease activity during extraction. 8. The published studies on protein degradation during aging are also contradictory. Some investigators have neglected the possibility of reutilization of labelled amino acid. It is possible that some of the observed age‐related alterations in protein degradation rates are due to altered endocrine status of the animals used, rather than to defects in the protein degradative pathways. The studies utilizing cell culture systems are also contradictory, probably due to different experimental designs. 9. Limited evidence suggests that protein degradation may slow down with age in mammals and nematodes. An inefficient protein degradation system in old organisms could provide a...

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Gene Expression and Protein Degradation

Remmen¹,

Ward²,

Sabia³

et al. 1995

Comprehensive Physiology

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Chromatin proteins and cellular aging The relationship between aging and protein synthesis RNA synthesis Protein synthesis and degradation during aging and senescence Aging and transcription Age-related changes in protein synthesis Enzymes, enzyme alteration, and protein turnover Age-related changes in the structure and function of chromatin Macromolecular methylation during aging The effect of age and nutrition on protein synthesis by cells and tissues from mammals Levels of specific messenger RNA species as a function of age Aging and gene expression Age-related changes of transcription and RNA processing Age-related changes in the synthesis of individual liver-specific proteins Effect of aging on translation and transcription Implication of protein oxidation in protein turnover, aging, and oxygen toxicity Biochemical markers of aging Protein oxidation and aging DNA methylation in aging and cancer RNA and protein metabolism in the aging brain Alterations in gene expression with aging Protein synthesis and the components of protein synthetic machinery during cellular ageing Effect of age on liver protein synthesis and degradation The next frontier: studies of the effects of age and diet on mammalian gene expression Protein synthesis, posttranslational modifications, and aging Gene expression and aging ~ TABLE 9.3. Effect of Age on the mRNA Levels in Liver

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Cell-free protein synthesis by kidney from the aging female Fischer F344 RAT

Cited by 28 publications

References 32 publications

Effect of age and dietary restriction on protein synthesis by isolated kidney cells

Effect of age and dietary restriction on protein synthesis by isolated kidney cells

Protein Synthesis and Degradation During Aging and Senescence

Gene Expression and Protein Degradation

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