Gastrointestinal tract protein synthesis and mRNA levels for proteolytic systems in adult fasted rats

American Journal of Physiology - Endocrinology and Metabolism

Volumn 271, Issue 2 34-2, 1996, Pages

  Samuels, Susan E ^a   Taillandier, Daniel ^d   Aurousseau, Eveline ^d   Cherel, Yves ^b   Le Maho, Yvon ^d   Arnal, Maurice ^d   Attaix, Didier ^c  

^a UNIVERSITY OF BRITISH COLUMBIA   (Canada)

^b CENTRE D ETUDES BIOLOGIQUES DE CHIZÉ   (France)

^c CEMAGREF   (France)

^d NONE

Author keywords

colon; protein degradation; small intestine; starvation; stomach

Indexed keywords

CALPAIN; CATHEPSIN B; CATHEPSIN D; GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE; LYSOSOME ENZYME; MESSENGER RNA; PROTEASOME; UBIQUITIN; VALINE;

ANIMAL EXPERIMENT; ANIMAL TISSUE; ARTICLE; COLON; CONTROLLED STUDY; DIET RESTRICTION; ENZYME ACTIVATION; GASTROINTESTINAL TRACT; MALE; NONHUMAN; PRIORITY JOURNAL; PROTEIN CONTENT; PROTEIN DEGRADATION; PROTEIN SYNTHESIS; RAT; SMALL INTESTINE; STOMACH;

EID: 0029783852     PISSN: 01931849     EISSN: None     Source Type: Journal    
DOI: 10.1152/ajpendo.1996.271.2.e232     Document Type: Article

References (33)

1. Alpers, D. H. Uptake and fate of absorbed amino acids and peptides in the mammalian intestine. Federation Proc. 45: 2261-2267, 1986.
2. Attaix, D., E. Aurousseau, A. Manghebati, and M. Arnal. Contribution of liver, skin, and skeletal muscle to whole-body protein synthesis in the young lamb. Br. J. Nutr. 60: 77-84, 1988.
3. Baker, R. T., and P. G. Board. Unequal crossover generates variation in the ubiquitin coding unit number at the human UbC polyubiquitin locus. Am. J. Hum. Genet. 44: 534-542, 1989.
4. Burrin, D. G., T. A. Davis, M. L. Fiorotto, and P. J. Reeds. Stage of development and fasting affect protein synthetic activity in the gastrointestinal tissues of suckling rats. J. Nutr. 121: 1099-1108, 1991.
5. Cherel, Y., D. Attaix, D. Rosolowska-Huszcz, R. Belkhou, J.-P. Robin, M. Arnal, and Y. Le Maho. Whole-body and tissue protein synthesis during brief and prolonged fasting in the rat. Clin. Sci. Lond. 81: 611-619, 1991.
6. Ciechanover, A. The ubiquitin-proteasome proteolytic pathway. Cell 79: 13-21, 1994.
7. t-methylhistidine during fasting in the rat. Biosci. Rep. 6: 143-153, 1986.
8. Fink, M. P. Gastrointestinal mucosal injury in experimental models of shock, trauma, and sepsis Crit. Care Med. 19: 627-641, 1991.
9. Furuno, K., M. N. Goodman, and A. L. Goldberg. Role of different proteolytic systems in the degradation of muscle proteins during denervation atrophy. J. Biol. Chem. 265: 8850-8857, 1990.
10. Goodman, M. N., P. R. Larsen, M. M. Kaplan, T. T. Aoki, V. R. Young, and N. B. Ruderman. Starvation in the rat. II. Effect of age and obesity on protein sparing and fuel metabolism. Am. J. Physiol. 239 (Endocrinol. Metab. 2): E277-E286, 1980.
11. Goodman, M. N., M. A. McElaney, and N. B. Ruderman. Adaptation to prolonged starvation in the rat: curtailment of skeletal muscle proteolysis. Am. J. Physiol. 241 (Endocrinol. Metab. 4): E321-E327, 1981.
12. Harley, C. B. Hybridization of oligo(dT) to RNA on nitrocellulose. Gene Anal. Tech. 4: 17-22, 1987
13. Ibrahim, M., R. K. Upreti, and A. M. Kidwai. Calpain from rat intestinal epithelium cells: age-dependent dynamics during cell differentiation. Mol. Cell. Biol. 131: 49-59, 1994.
14. Ichihara, A., and K. Tanaka. Roles of proteasomes in cell growth. Mol Biol. Rep. 21: 49-52, 1995.
15. Johnson, P. Calpains (intracellular calcium-activated cysteine proteinases): structure-activity relationships and involvement in normal and abnormal cellular metabolism. Int. J. Biochem. 22: 811-822, 1990.
16. Lowell, B. B., N. B. Ruderman, and M. N. Goodman. Evidence that lysosomes are not involved in the degradation of myofibrillar proteins in rat skeletal muscle. Biochem J. 234: 237-240, 1986.
17. 2+-activated and ATP-ubiquitin-dependent proteolytic pathways in skeletal muscle from head trauma patients. Proc. Natl. Acad. Sci. USA 93: 2714-2718, 1996.
18. McBurney, M. I. The gut: central organ in nutrient requirements and metabolism. Can. J. Physiol. Pharmacol. 72: 260-265, 1994.
19. McNurlan, M. A., A. M. Tomkins, and P. J. Garlick. The effect of starvation on the rate of protein synthesis in rat liver and small intestine. Biochem J. 178: 373-379, 1979.
20. Medina, R., S. S. Wing, and A. L. Goldberg. Increase in levels of polyubiquitin and proteasome mRNA in rat skeletal muscle during starvation and denervation atrophy. Biochem. J. 307: 631-637, 1995.
21. Mortimore, G. E., M. Kadowaki, and S. J. Heydrick. The autophagic pathway in liver: its regulation and role in macromolecular turnover. In: Protein Metabolism in Diabetes Mellitus, edited by K. S. Nair. London: Gordon, 1992, p. 125-138.
22. Munro, H. N., and A. Fleck. Analysis of tissues and body fluids for nitrogenous constituents. In: Mammalian Protein Metabolism, edited by H. N. Munro. New York: Academic, 1969, vol. 3, p. 423-525.
23. Preedy, V. R., L. Paska, P. H. Sugden, P. S. Schofield, and M. C. Sugden. The effects of surgical stress and short-term fasting on protein synthesis in vivo in diverse tissues of the mature rat. Biochem. J. 250: 179-188, 1988.
24. Price, S. R., B. K. England, J. L. Bailey, K. Van Vreede, and W. E. Mitch. Acidosis and glucocorticoids concomitantly increase ubiquitin and proteasome subunit mRNAs in rat muscle. Am. J. Physiol. 267 (Cell Physiol. 36): C955-C960, 1994.
25. Reeds, P. J., D. G. Burrin, T. A. Davis, and M. L. Fiorotto. Postnatal growth of gut and muscle: competitors or collaborators. Proc. Nutr. Soc. 52: 57-67, 1993.
26. 2+-activated and ATP-ubiquitin-dependent proteinases in the unweighted rat soleus muscle. Biochem. J. 316: 65-72: 1996.
27. Temparis, S., M. Asensi, D. Taillandier, E. Aurousseau, D. Larbaud, A. Obled, D. Béchet, M. Ferrara, J. M. Estrela, and D. Attaix. Increased ATP-ubiquitin-dependent proteolysis in skeletal muscles of tumor-bearing rats. Cancer Res. 54: 5568-5573, 1994.
28. Tiao, G., J. M. Fagan, N. Samuels, J. H. James, K. Hudson, M. Lieberman, J. E. Fischer, and P.-O. Hasselgren. Sepsis stimulates nonlysosomal, energy-dependent proteolysis and increases ubiquitin mRNA levels in rat skeletal muscle. J. Clin. Invest. 94: 2255-2264, 1994.
29. Tokunaga, I., K. Ishimura, K. Tanaka, A. Ichihara, and M. Maeiwa. Immunohistochemical localizations of proteasomes in human intestines. Acta Histochem. Cytochem. 26: 597-599, 1993.
30. Uchiyama, Y., S. Waguri, N. Sata, T. Watanabe, K. Ishido, and E. Kominami. Review: cell and tissue distribution of lysosomal cysteine proteinases, cathepsins B, H, and L, and their biological roles. Acta Histochem. Cytochem. 27: 287-308, 1994
31. 2+-activated and ubiquitin-proteasome proteolytic pathways. J. Clin. Invest. 97: 1610-1617, 1996.
32. Wing, S. S., and D. Banville. 14-kDa ubiquitin conjugating enzyme: structure of the rat gene and regulation upon fasting and by insulin. Am. J. Physiol. 267 (Endocrinol. Metab. 30): E39-E48, 1994.
33. Wing, S. S., and A. L. Goldberg. Glucocorticoids activate the ATP-ubiquitin-dependent proteolytic system in skeletal muscle during fasting. Am. J. Physiol. 264 (Endocrinol. Metab. 27): E668-E676, 1993.