Protein elongation rates in tissues of growing and adult sheep

Journal of Animal Science

Volumn 86, Issue 9, 2008, Pages 2288-2295

  Connors, M T ^a   Poppi, D P ^a   Cant, J P ^b  

^a UNIVERSITY OF QUEENSLAND   (Australia)

^b UNIVERSITY OF GUELPH   (Canada)

Author keywords

Age; Intake; Protein synthesis; Ribosome transit time; Sheep

Indexed keywords

DNA; MESSENGER RNA; MUSCLE PROTEIN; NITROGEN;

ANIMAL; ANIMAL DISEASE; ANIMAL FOOD; ARTICLE; BIOPSY; BIOSYNTHESIS; EATING; FEMALE; GENETICS; GROWTH, DEVELOPMENT AND AGING; METABOLISM; PROTEIN SYNTHESIS; RANDOMIZATION; RIBOSOME; SHEEP; SKELETAL MUSCLE;

ANIMAL NUTRITION PHYSIOLOGY; ANIMALS; BIOPSY; DNA; EATING; FEMALE; MUSCLE PROTEINS; MUSCLE, SKELETAL; NITROGEN; PROTEIN BIOSYNTHESIS; RANDOM ALLOCATION; RIBOSOMES; RNA, MESSENGER; SHEEP;

ANIMALIA; OVIS; OVIS ARIES;

EID: 52649118053     PISSN: 00218812     EISSN: None     Source Type: Journal    
DOI: 10.2527/jas.2007-0159     Document Type: Article

References (44)

1. Anthony, J. C., C. H. Lang, S. J. Crozier, T. G. Anthony, D. A. Mac-Leam, S. R. Kimball, and L. S. Jefferson. 2002. Contribution of insulin to the translational control of protein synthesis in skeletal muscle by leucine. Am. J. Physiol. 282:E1092-E1101.
2. Attaix, D., and M. Arnal. 1987. Protein synthesis and growth in the gastrointestinal tract of the young preruminant lamb. Br. J. Nutr. 58:159-169.
3. Attaix, D., E. Aurousseau, G. Bayle, A. Manghebati, and M. Arnal. 1988. Contribution of liver, skin and skeletal muscle to whole-body protein synthesis in the young lamb. Br. J. Nutr. 60:77-84.
4. Ayuso-Parrilla, M. S., M. Martin-Requero, J. Perez-Diaz, and R. Parrilla. 1976. Role of glucagon on the control of hepatic protein synthesis and degradation in the rat in vivo. J. Biol. Chem. 251:7785-7790.
5. Blazejowski, C. A., and G. C. Webster. 1983. Decreased rates of protein synthesis by cell-free preparations from different organs of aging mice. Mech. Ageing Dev. 21:345-356.
6. Castañeda, M., R. Vargas, and S. C. Galvan. 1986. Stagewise decline in the activity of brain protein synthesis factors and relationship between this decline and longevity in two rodent species. Mech. Ageing Dev. 36:197-210.
7. Cohen, S. A., and D. J. Strydom. 1988. Amino acid analysis utilizing phenylisothiocyanate derivatives. Anal. Biochem. 174:1-16.
8. Davis, T. A., D. G. Burrin, M. L. Fiorotto, and H. V. Nguyen. 1996. Protein synthesis in skeletal muscle and jejunum is more responsive to feeding in 7-than in 26-day-old pigs. Am. J. Physiol. 270:E802-E809.
9. Davis, T. A., M. L. Fiorotto, D. G. Burrin, P. J. Reeds, H. V. Nguyen, P. R. Beckett, R. C. Vann, and P. M. J. O'Connor. 2002. Stimulation of protein synthesis by both insulin and amino acids is unique to skeletal muscle in neonatal pigs. Am. J. Physiol. 282:E880-E890.
10. Davis, T. A., H. V. Nguyen, A. Suryawan, J. A. Bush, L. S. Jefferson, and S. R. Kimball. 2000. Developmental changes in the feeding-induced stimulation of translation initiation in muscle of neonatal pigs. Am. J. Physiol. 279:E1226-E1234.
11. El Haj, A. J., S. E. M. Lewis, D. F. Goldspink, B. J. Merry, and A. M. Holehan. 1986. The effect of chronic and acute dietary restriction of the growth and protein turnover of fast and slow types of rat skeletal muscle. Comp. Biochem. Physiol. 85A:281-287.
12. Frerichs, K. U., C. B. Smith, M. Brenner, D. J. DeGracia, G. S. Krause, L. Marrone, T. E. Dever, and J. M. Hallenbeck. 1998. Suppression of protein synthesis in brain during hibernation involves inhibition of protein initiation and elongation. Proc. Natl. Acad. Sci. USA 95:14511-14516.
13. Gabius, H.-J., R. Engelhardt, F. Deerberg, and F. Cramer. 1983. Agerelated changes in different steps of protein synthesis of liver and kidney of rats. FEBS Lett. 160:115-118.
14. Hagan, S. R., J. Augustin, E. Grings, and P. Tassinari. 1993. Precolumn phenylisothiocyanate derivatization and liquid chromatography of free amino acids in biological samples. Food Chem. 46:319-323.
15. Khasigov, P. Z., and A. Y. Nikolaev. 1987. Age-related changes in the rates of polypeptide chain elongation. Biochem. Int. 15:1171-1178.
16. Kikuchi, T., H. Okamoto, K. Chiku, and Y. Natori. 1986. Effects of glucose and amino acid depletions on protein synthetic parameters in liver and skeletal muscle of rats during parenteral nutrition. J. Nutr. Sci. Vitaminol. (Tokyo) 32:601-612.
17. Kimball, S. R., J. P. O'Malley, J. C. Anthony, S. J. Crozier, and L. J. Jefferson. 2004. Assessment of biomarkers of protein anabolism in skeletal muscle during the life span of the rat: sarcopenia despite elevated protein synthesis. Am. J. Physiol. 287:E772-E780.
18. Kimball, S. R., T. C. Vary, and L. S. Jefferson. 1992. Age-dependent decrease in the amount of eukaryotic initiation factor 2 in various rat tissues. Biochem. J. 286:263-268.
19. Ku, Z., and D. B. Thomason. 1994. Soleus muscle nascent polypeptide chain elongation slows protein synthesis rate during non-weight-bearing activity. Am. J. Physiol. 267:C115-C126.
20. Labarca, C., and K. Paigen. 1980. A simple, rapid, and sensitive DNA assay procedure. Anal. Biochem. 102:344-352.
21. Levenson, R. M., A. C. Nairn, and P. J. Blackshear. 1989. Insulin rapidly induces the biosynthesis of elongation factor 2. J. Biol. Chem. 264:11904-11911.
22. Lobley, G. E. 1993. Species comparisons of tissue protein metabolism: Effects of age and hormonal action. J. Nutr. 123:337-343.
23. Lobley, G. E., A. Connell, E. Milne, V. Buchan, A. G. Calder, S. E. Anderson, and H. Vint. 1990. Muscle protein synthesis in response to testosterone administration in wether lambs. Br. J. Nutr. 64:691-704.
24. Lobley, G. E., A. Connell, E. Milne, A. M. Newman, and T. A. Ewing. 1994. Protein synthesis in splanchnic tissues of sheep offered two levels of intake. Br. J. Nutr. 71:3-12.
25. Lowry, O. H., N. J. Rosebrough, A. L. Farr, and R. J. Randall. 1951. Protein measurement with the Folin phenol reagent. J. Biol. Chem. 193:265-275.
26. Martin, M. E., A. Alcazar, J. L. Fando, A. M. Garcia, and M. Salinas. 1993. Translational initiation factor eIF-2 subcellular levels and phosphorylation status in the developing rat brain. Neurosci. Lett. 156:109-112.
27. Mathews, R. W., and A. E. V. Haschemeyer. 1976. Liver protein synthesis. Molecular weight distribution of pulse-labeled polypeptide chains in normal and thyroidectomized rats. Biochim. Biophys. Acta 425:220-228.
28. McNurlan, M. A., A. M. Tomkins, and P. J. Garlick. 1979. The effect of starvation on the rate of protein synthesis in rat liver and small intestine. Biochem. J. 178:373-379.
29. Merry, B. J., and A. M. Holehan. 1991. Effect of age and restricted feeding on polypeptide chain assembly kinetics in liver protein synthesis in vivo. Mech. Ageing Dev. 58:139-150.
30. Monier, S., and Y. Le Marchand-Brustel. 1982. Insulin affects only initiation and not elongation in protein synthesis in soleus muscles of lean and obese mice. FEES Lett. 147:211-214.
31. Munro, H. N., and A. Fleck. 1966. Recent developments in the measurement of nucleic acids in biological materials. Analyst (Lond.) 91:78-88.
32. Murthy, M. R. V. 1966. Protein synthesis in growing-rat tissues II. Polyribosome concentration of brain and liver as a function of age. Biochim. Biophys. Acta 119:599-613.
33. Nagai, K., and K. Ogata. 1990. Stimulation of liver translational elongation induced by refeeding a complete diet to starved rats. Agric. Biol. Chem. 54:1661-1666.
34. Nielsen, P. J., and E. H. McConkey. 1980. Evidence for control of protein synthesis in HeLa cells via the elongation rate. J. Cell. Physiol. 104:269-281.
35. Palmiter, R. D. 1972. Regulation of protein synthesis in chick oviduct II. Modulation of polypeptide elongation and initiation rates by estrogen and progesterone. J. Biol. Chem. 247:6770-6780.
36. Pérez-Sala, D., R. Parrilla, and M. S. Ayuso. 1987. Key role of L-alanine in the control of hepatic protein synthesis. Biochem. J. 241:491-498.
37. Rattan, S. I. S. 1996. Synthesis, modifications, and turnover of proteins during aging. Exp. Gerontol. 31:33-47.
38. Rattan, S. I. S., W. F. Ward, M. Glenting, L. Svendsen, B. Riis, and B. F. C. Clark. 1991. Dietary calorie restriction does not affect the levels of protein elongation factors in rat livers during ageing. Mech. Ageing Dev. 58:85-91.
39. Scornik, O. A. 1974. In vivo rate of translation by ribosomes of normal and regenerating liver. J. Biol. Chem. 249:3876-3883.
40. Southorn, B. G., J. M. Kelly, and B. W. McBride. 1992. Phenylalanine flooding dose procedure is effective in measuring intestinal and liver protein synthesis in sheep. J. Nutr. 122:2398-2407.
41. Wang, X., W. Li, M. Williams, N. Terada, D. R. Alessi, and C. G. Proud. 2001. Regulation of elongation factor 2 kinase by p90RSK1 and p70 S6 kinase. EMBO J. 20:4370-4379.
42. Wolin, S. L., and P. Walter. 1988. Ribosomal pausing and stacking during translation of a eukaryotic mRNA. EMBO J. 7:3559-3569.
43. Yoshizawa, F., M. Endo, H. Ide, K. Yagasaki, and R. Funabiki. 1995. Translational regulation of protein synthesis in the liver and skeletal muscle of mice in response to refeeding. J. Nutr. Biochem. 6:130-136.
44. Zomzely, C. E., S. Roberts, S. Peache, and D. M. Brown. 1971. Cerebral protein synthesis III. Developmental alterations in the stability of cerebral messenger ribonucleic acid-ribosome complexes. J. Biol. Chem. 246:2097-2103.