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Gene Expression and Protein Degradation

Holly Van Remmen, Walter F. Ward, Robert V. Sabia, Arlan Richardson

10.1002/cphy.cp110109

Source: Supplement 28: Handbook of Physiology, Aging

Originally published: 1995

Published online: January 2011

Full Article on Wiley Online Library



Abstract

The sections in this article are:

1 Transcription
1.1 RNA Synthesis
1.2 mRNA Levels
1.3 Transcriptional and Posttranscriptional Processing of mRNA
1.4 Factors That Regulate Transcription
1.5 Effect of Dietary Restriction on Transcription
2 Translation
2.1 Protein Synthesis
2.2 Effect of Dietary Restriction on Protein Synthesis
2.3 Fidelity of Protein Synthesis
2.4 Various Steps of Protein Synthesis
3 Protein Degradation
3.1 Degradation of Mixed Protein Populations
3.2 Degradation of Individual Proteins
3.3 Degradation of Abnormal Proteins
3.4 Effect of Dietary Restriction on Protein Degradation
4 Summary and Conclusions
Figure 1. Figure 1.

Effect of age on RNA synthesis by rat liver. The graph on the left shows the rate of RNA synthesis by nuclei isolated from the livers of rats of various ages, and the graph on the right shows the rate of total RNA synthesis (•) and poly(A)+ RNA synthesis (○) by hepatocytes isolated from rats of various ages.

data taken from Castle et al. 46 data taken from Richardson et al. 320]
Figure 2. Figure 2.

Effect of donor age on RNA synthesis in human fibroblasts. Fibroblasts were obtained from the foreskin of normal white males of various ages and RNA synthesis measured as the incorporation of radioactive UTP into RNA.

data taken from Chen et al. 55 and figure taken from Richardson et al. 319, with permission
Figure 3. Figure 3.

Effect of age on the degradation of hsp70 mRNA. Levels of hsp70 transcript were measured in hepatocytes isolated from 6‐ (□) and 26‐ (▪) month‐old rats after a brief heat shock.

data taken from Heydari et al. 138
Figure 4. Figure 4.

Effect of age on the expression of albumin. Synthesis (▪) and mRNA levels (□) of albumin were measured in the livers of rats of various ages.

data taken from Horbach et al. 145
Figure 5. Figure 5.

Effect of age on the expression of α2u‐globulin. Synthesis (•), mRNA levels (○), and nuclear transcription (○) of α2u‐globulin were measured in hepatocytes isolated from rats of various ages.

data taken from Richardson et al. 321
Figure 6. Figure 6.

Effect of age on the expression of genes by spleen lymphocytes. The biological activity (□) and mRNA levels (▪) of interleukin 2 (IL2), IL3, and granulocyte/macrophage colony‐stimulating factor (GMCSF) in mitogen‐stimulated lymphocytes isolated from the spleen of mice of various ages is shown.

data taken from Li et al. 201 and Cai et al. 42
Figure 7. Figure 7.

Effect of age on the induction of tyrosine hydroxylase expression in the adrenal gland. The enzyme activity and the level of the mRNA transcript for tyrosine hydroxylase were determined in the adrenal gland of rats of various ages before (shaded bars) and after (solid bars) treatment with reserpine.

data taken from Strong et al. 380
Figure 8. Figure 8.

Effect of age on the expression of Gsα and c‐myc. The left graph shows the levels of Gsα protein, mRNA, and nuclear transcription by the renal cortex of 6‐(shaded bars) and 24‐ (solid bars) month‐old rats. The graph on the right shows the levels of the mRNA transcript and the nuclear transcription of c‐myc in lymphocytes isolated from young and old human subjects before (shaded bars) and after (solid bars) mitogen stimulation.

data taken from Hanai et al. 132 and Liang et al. 201 data taken from Gamble et al. 109
Figure 9. Figure 9.

Effect of age on DNA methylation. The percentage of 5mC in DNA isolated from the mucosa of the small intestine of Mus musculus (▪) and Peromyscus leucopus (□) of various ages is shown.

data taken from Wilson et al. 434
Figure 10. Figure 10.

Effect of age on the induction of c‐fos and c‐jun in rat heart. The levels of the mRNA transcripts for c‐fos and c‐jun were measured in the hearts of 9‐ and 18‐month‐old rats 90 (▪) and 180 (▪) minutes after acute pressure overload or in sham (▪)‐operated rats.

data taken from Takahashi et al. 386
Figure 11. Figure 11.

Effect of dietary restriction on the expression of α2u — globulin. The synthesis, mRNA levels, and nuclear transcription of α2a — globulin by hepatocytes isolated from 18–month‐old rats fed ad libitum (shaded bars) and a calorie‐restricted diet (solid bars) are shown.

data taken from Richardson et al. 321
Figure 12. Figure 12.

Effect of age on protein synthesis by invertebrates. Cell‐free incorporation of [3H]‐leucine into protein by microsomes from D. melanogaster [○, data taken from Webster 420] and the in vivo incorporation of [3H]‐leucine into protein by nematodes [•, data taken from Sharma et al. 346] are shown.

Figure taken from Richardson and Birchenall‐Sparks 315 with permission
Figure 13. Figure 13.

Effect of age on protein synthesis by various tissues of rats. The left graph shows the relative protein synthetic activity of liver [○, data taken from Coniglio et al. 65], brain [Δ, data taken from Ekstrom et al. 86], kidney [•, data taken from Hardwick et al. 133], testes [▴, data taken from Liu et al. 208], and mitogen‐stimulated spleen lymphocytes [, data taken from Cheung et al. 57] of Fischer 344 rats. The right graph shows the relative protein synthetic activity of liver [, data taken from Bolla and Greenblatt 32], pancreas [•, data taken from Kim et al. 175], parotid gland [○, data taken from Kim et al. 176], heart mitochondria [Δ, data taken from Starnes et al. 376], and testes [▴, data taken from Richardson and Myers 317] of Sprague‐Dawley rats.

Figure taken from Richardson and Birchenall‐Sparks 315 with permission
Figure 14. Figure 14.

Variation in the age‐related decline in the synthesis of individual proteins by rat liver. A comparison of the decrease in the rate of synthesis of 35 proteins between 5 and 30 months of age is shown for rat hepatocytes.

data taken from Butler et al. 39
Figure 15. Figure 15.

Effect of dietary restriction on protein synthesis by rat liver. The rate of protein synthesis by hepatocytes isolated from rats fed ad libitum (□) or a calorie‐restricted diet (▪) is shown.

data were taken from Birchenall‐Sparks et al. 23
Figure 16. Figure 16.

Effect of age on ribosome aggregation to mRNA. The sedimentation of polyribosomes in sucrose gradients is shown for skeletal muscle], liver], and brain of rats.

data taken from Pluskal et al. 296 data taken from Layman et al. 194 data taken from Fando et al. 89
Figure 17. Figure 17.

Effect of age on the elongation of protein synthesis in rat liver. The ribosomal half‐transit times for hepatocytes isolated from 4‐month‐old (A) and 18–month‐old (B) rats are shown.

Figure taken rom Coniglio et al. 65 with permission
Figure 18. Figure 18.

Effect of age on the activity of EF‐1α. The activity of EF‐1α is shown for D. melanogaster

A, data taken from Webster and Webster 422], nematodes [B, data taken from Bolla and Brot 29], and rat liver [C, data taken from Moldave et al. 254
Figure 19. Figure 19.

Pathway of protein degradation in mammalian cells.
Figure 20. Figure 20.

Effect of age on protein degradation in rat liver. The rate of protein degradation by perfused liver from rats fed ad libitum (○) or a calorie‐restricted diet (•) is shown as a function of age.

data taken from Ward 416 with permission
Figure 21. Figure 21.

Effect of age on the accumulation of oxidized proteins in rat liver. Left: levels of carbonyl groups in soluble proteins in the livers of rats of various ages is shown [data taken from Starke‐Reed and Oliver 375]. Right: levels of carbonyl groups in the frontal pole (FP) and occipital pole (OP) of brain obtained from 16 patients at autopsy.

data taken from Smith et al. 361 with permission
Figure 22. Figure 22.

Effect of age on the degradation of abnormal peptides by rat liver. After rats received an injection of [3H]‐puromycin, they were given unlabeled puromycin (•) or saline (▪). The radioactivity in puromycinyl peptides in the liver of 6‐month‐old (a) and 24–25‐month‐old (b) rats is shown.

Figure taken from Lavie et al. 192 with permission
Figure 23. Figure 23.

Effect of age on the degradation of oxidized proteins. A: comparison of levels of carbonyl groups in soluble protein in livers of rats of various ages to activity of alkaline protease activity [taken from Starke‐Reed and Oliver 375 with permission]. B: carbonyl content of protein, glutamine synthetase activity, and alkaline protease activity of brains from old (15–18 months) gerbils compared to brains of young (3 months) gerbils as 100%.

data taken from Carney et al. 43 with permission


Figure 1.

Effect of age on RNA synthesis by rat liver. The graph on the left shows the rate of RNA synthesis by nuclei isolated from the livers of rats of various ages, and the graph on the right shows the rate of total RNA synthesis (•) and poly(A)+ RNA synthesis (○) by hepatocytes isolated from rats of various ages.

data taken from Castle et al. 46 data taken from Richardson et al. 320]


Figure 2.

Effect of donor age on RNA synthesis in human fibroblasts. Fibroblasts were obtained from the foreskin of normal white males of various ages and RNA synthesis measured as the incorporation of radioactive UTP into RNA.

data taken from Chen et al. 55 and figure taken from Richardson et al. 319, with permission


Figure 3.

Effect of age on the degradation of hsp70 mRNA. Levels of hsp70 transcript were measured in hepatocytes isolated from 6‐ (□) and 26‐ (▪) month‐old rats after a brief heat shock.

data taken from Heydari et al. 138


Figure 4.

Effect of age on the expression of albumin. Synthesis (▪) and mRNA levels (□) of albumin were measured in the livers of rats of various ages.

data taken from Horbach et al. 145


Figure 5.

Effect of age on the expression of α2u‐globulin. Synthesis (•), mRNA levels (○), and nuclear transcription (○) of α2u‐globulin were measured in hepatocytes isolated from rats of various ages.

data taken from Richardson et al. 321


Figure 6.

Effect of age on the expression of genes by spleen lymphocytes. The biological activity (□) and mRNA levels (▪) of interleukin 2 (IL2), IL3, and granulocyte/macrophage colony‐stimulating factor (GMCSF) in mitogen‐stimulated lymphocytes isolated from the spleen of mice of various ages is shown.

data taken from Li et al. 201 and Cai et al. 42


Figure 7.

Effect of age on the induction of tyrosine hydroxylase expression in the adrenal gland. The enzyme activity and the level of the mRNA transcript for tyrosine hydroxylase were determined in the adrenal gland of rats of various ages before (shaded bars) and after (solid bars) treatment with reserpine.

data taken from Strong et al. 380


Figure 8.

Effect of age on the expression of Gsα and c‐myc. The left graph shows the levels of Gsα protein, mRNA, and nuclear transcription by the renal cortex of 6‐(shaded bars) and 24‐ (solid bars) month‐old rats. The graph on the right shows the levels of the mRNA transcript and the nuclear transcription of c‐myc in lymphocytes isolated from young and old human subjects before (shaded bars) and after (solid bars) mitogen stimulation.

data taken from Hanai et al. 132 and Liang et al. 201 data taken from Gamble et al. 109


Figure 9.

Effect of age on DNA methylation. The percentage of 5mC in DNA isolated from the mucosa of the small intestine of Mus musculus (▪) and Peromyscus leucopus (□) of various ages is shown.

data taken from Wilson et al. 434


Figure 10.

Effect of age on the induction of c‐fos and c‐jun in rat heart. The levels of the mRNA transcripts for c‐fos and c‐jun were measured in the hearts of 9‐ and 18‐month‐old rats 90 (▪) and 180 (▪) minutes after acute pressure overload or in sham (▪)‐operated rats.

data taken from Takahashi et al. 386


Figure 11.

Effect of dietary restriction on the expression of α2u — globulin. The synthesis, mRNA levels, and nuclear transcription of α2a — globulin by hepatocytes isolated from 18–month‐old rats fed ad libitum (shaded bars) and a calorie‐restricted diet (solid bars) are shown.

data taken from Richardson et al. 321


Figure 12.

Effect of age on protein synthesis by invertebrates. Cell‐free incorporation of [3H]‐leucine into protein by microsomes from D. melanogaster [○, data taken from Webster 420] and the in vivo incorporation of [3H]‐leucine into protein by nematodes [•, data taken from Sharma et al. 346] are shown.

Figure taken from Richardson and Birchenall‐Sparks 315 with permission


Figure 13.

Effect of age on protein synthesis by various tissues of rats. The left graph shows the relative protein synthetic activity of liver [○, data taken from Coniglio et al. 65], brain [Δ, data taken from Ekstrom et al. 86], kidney [•, data taken from Hardwick et al. 133], testes [▴, data taken from Liu et al. 208], and mitogen‐stimulated spleen lymphocytes [, data taken from Cheung et al. 57] of Fischer 344 rats. The right graph shows the relative protein synthetic activity of liver [, data taken from Bolla and Greenblatt 32], pancreas [•, data taken from Kim et al. 175], parotid gland [○, data taken from Kim et al. 176], heart mitochondria [Δ, data taken from Starnes et al. 376], and testes [▴, data taken from Richardson and Myers 317] of Sprague‐Dawley rats.

Figure taken from Richardson and Birchenall‐Sparks 315 with permission


Figure 14.

Variation in the age‐related decline in the synthesis of individual proteins by rat liver. A comparison of the decrease in the rate of synthesis of 35 proteins between 5 and 30 months of age is shown for rat hepatocytes.

data taken from Butler et al. 39


Figure 15.

Effect of dietary restriction on protein synthesis by rat liver. The rate of protein synthesis by hepatocytes isolated from rats fed ad libitum (□) or a calorie‐restricted diet (▪) is shown.

data were taken from Birchenall‐Sparks et al. 23


Figure 16.

Effect of age on ribosome aggregation to mRNA. The sedimentation of polyribosomes in sucrose gradients is shown for skeletal muscle], liver], and brain of rats.

data taken from Pluskal et al. 296 data taken from Layman et al. 194 data taken from Fando et al. 89


Figure 17.

Effect of age on the elongation of protein synthesis in rat liver. The ribosomal half‐transit times for hepatocytes isolated from 4‐month‐old (A) and 18–month‐old (B) rats are shown.

Figure taken rom Coniglio et al. 65 with permission


Figure 18.

Effect of age on the activity of EF‐1α. The activity of EF‐1α is shown for D. melanogaster

A, data taken from Webster and Webster 422], nematodes [B, data taken from Bolla and Brot 29], and rat liver [C, data taken from Moldave et al. 254


Figure 19.

Pathway of protein degradation in mammalian cells.



Figure 20.

Effect of age on protein degradation in rat liver. The rate of protein degradation by perfused liver from rats fed ad libitum (○) or a calorie‐restricted diet (•) is shown as a function of age.

data taken from Ward 416 with permission


Figure 21.

Effect of age on the accumulation of oxidized proteins in rat liver. Left: levels of carbonyl groups in soluble proteins in the livers of rats of various ages is shown [data taken from Starke‐Reed and Oliver 375]. Right: levels of carbonyl groups in the frontal pole (FP) and occipital pole (OP) of brain obtained from 16 patients at autopsy.

data taken from Smith et al. 361 with permission


Figure 22.

Effect of age on the degradation of abnormal peptides by rat liver. After rats received an injection of [3H]‐puromycin, they were given unlabeled puromycin (•) or saline (▪). The radioactivity in puromycinyl peptides in the liver of 6‐month‐old (a) and 24–25‐month‐old (b) rats is shown.

Figure taken from Lavie et al. 192 with permission


Figure 23.

Effect of age on the degradation of oxidized proteins. A: comparison of levels of carbonyl groups in soluble protein in livers of rats of various ages to activity of alkaline protease activity [taken from Starke‐Reed and Oliver 375 with permission]. B: carbonyl content of protein, glutamine synthetase activity, and alkaline protease activity of brains from old (15–18 months) gerbils compared to brains of young (3 months) gerbils as 100%.

data taken from Carney et al. 43 with permission
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Article Title: Gene Expression and Protein Degradation
 

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Holly Van Remmen, Walter F. Ward, Robert V. Sabia, Arlan Richardson. Gene Expression and Protein Degradation. Compr Physiol 2011, Supplement 28: Handbook of Physiology, Aging: 171-234. First published in print 1995. doi: 10.1002/cphy.cp110109