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1989 | 40 | 4 |

Tytuł artykułu

Changes in cathepsin D, acid autolypic activity, RNA, DNA in skeletal muscle and liver of mouse kept on high protein, carbohydrate and lipid diets

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Języki publikacji

EN

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EN
Rosochacki, S. J.: Changes in cathepsin D, acid autolytic activity, RNA, DNA in skeletal muscle and liver of mouse kept on high protein, carbohydrate and lipid diets. Acta physiol, pol., 1989 40 (4): 363-373. The influence was studied of different diets on the activity of cathepsin D (PSCatD), pepstatin (PIA) and leupeptin (LIA) insensitive acid autolytic activity (AAA), RNA, DNA and protein in skeletal leg muscle (LM) and liver of 37 mice. The diets affected the weight of the liver and content of protein in the liver and LM. The protein : DNA ratio was lowest on high carbohydrate (HC) and commercial (C) diets in both tissues and about 3 times higher in LM than in the liver. The RNA : protein ratio was highest in the high proteinfat (HPF) and recommended (R) diet fed groups. The RNA : DNA ratio was lowest on HC and C diets. In the liver, PSCatD, AAA, LIA were lowest on HPF, and highest on HC diets, but for PIA on high fat-protein (HFP) and C diets, respectively. The highest activities were correlated with the lowest percentage of protein and fat in the diets (low energy diets). For LM, the highest activities were found on a C diet and lowest for PSCatD on HEP but for AAA, PIA, LIA on HC diets. Cathepsin D occounted for about 70% of hemoglobin degradation in the liver and 66% in LM. In AAA, cathepsin D participates in 58.5% and 50.5% in the liver and LM inhibition, respectively, but leupeptin accounted for about 15% and 27% (in the presence of Mg⁺⁺) of inhibition.

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-

Rocznik

Tom

40

Numer

4

Opis fizyczny

p.363-373,ref.

Twórcy

  • Institute of Genetics and Animal Breeding, Polish Academy of Sciences, Jastrzebiec, Poland

Bibliografia

  • 1. Antoszewska, B., Rosochacki, S. J., Keller, J. S. (1983) The effect of feeding level on some lysosomal proteolytic activities in liver of growing chicken. Arch Geflügelk. 47. 124-127.
  • 2. Bird, J. W. C., Bird, T., Leathern, J. L. (1968) Cathepsin activity of liver and muscle fractions of adrenalectomized rats. Proc. Soc. Exp. Med. 127. 182-188.
  • 3. Cheek, D. B., Holt, A. B., Hill, D. E., Talbert, J. C. (1971) Skeletal muscle cell mass and growth: the concept of the deoxyribonucleic acid unit. Pediatr. Res. 5. 312-328.
  • 4. Dayton, W. R., Goll, D. E., Stromer, SM. H., Reville, W. J., Zeece, M. G., Robson, R. M. (1975) Calcium activated protease - calpain. In Cold Spring Harbour Conferences on Cell Proliferation, eds. R. Goldman, T., Pollard, J. Rosenbaum, pp. 551-577, New York.
  • 5. Dean, R. T. (1978) Lysosomal mechanisms of protein degradation In Protein Turnover and Lysosomal Function, eds. H. L. Segal, D. J. Doyle, pp. 29-41. Academic Press, New York - San Francisco – London.
  • 6. Kameyama, T., Etlinger, J, D. (1979) Calcium-dependent regulation of protein synthesis and degradation in muscle. Nature 279. 355-346.
  • 7. Kay, J., Siemankowski, R. F., Greweling, L. M.. Siemankowski, L. M., Goll, D. E. (1981) Proteolysis of myofibrillar proteins at neutral pH. In Intracellular Protein Catabolism, eds. H. Aurich, B. Wiederanders, P. Bohley, pp. 66-67, Martin-Luther Universität, Halle.
  • 8. Kirschke, H., Kembhavi, A. A., Bohley, P., Barrett, A. J. (1982) Action of rat liver cathepsin L on collagen and other substrates. Biochem. J. 201. 367-372.
  • 9. Laurent, G. J., Sparrow, M. P., Bates, P. C., Millward, D. J., (1978) Turnover of muscle protein in the fowl (Gallus domesticus). Rates of protein synthesis in fast and slow skeletal, cardiac and smooth muscle of the adult fowl. Biochem. J. 176. 393-405.
  • 10. Lenney, J. F. (1981) Endogenous inhibitors of mammalian intracellular proteinases. In Intracellular Protein Catabolism, eds. H. Aurich, B. Wiederanders, P. Bohley, pp. 83, Martin-Luther Universität, Halle.
  • 11. Lowry, О. H., Rosenbrough, N. J., Farr, A. L., Randall, R. J. (1951) Protein measurement with Folin phenol reagent. J. Biol. Chem. 193. 265-275.
  • 12. Millward, D. J. (1978) Regulation of muscle protein turnover in growth and development. Biochem. Soc. Trans. 6. 494-499.
  • 13. Millward, D. J. (1980) Protein degradation in muscle and liver. In Comprehensive Biochemistry, vol. 19B. eds. M. Florkin, A. Neuberger, L. L. M., vanDeenan, pp. 153-232, Elsevier/North Holland, Amsterdam.
  • 14. Millward, D. J., Bates, P. C., Brown, J. T., Rosochacki, S., Rennie, M. J. (1980) Protein degradation and the regulation of protein balance in muscle. In Protein Degradation in Health and Disease, pp. 302-329, eds. Excerpta Medica, Elsevier/North Holland, Amsterdam.
  • 15. Millward, D. J., Bates, P. C., Rosochacki, S. J. (1981) The extent and nature of protein degradation in the tissues during development. Reprod. Nutr. Develop. 21. 265-277.
  • 16. Rosochacki, S. J., Millward, D. J. (1979) Cathepsin D and acid autolytic activity in skeletal muscle of protein deficient, severly protein-energy restricted and refed rats. Proc. Nutr. Soc. 38. 137A.
  • 17. Rosochacki, S. J. (1985) Changes in cathepsin D, proteolytic activity and RNA and DNA content in the anterior and posterior latissimus dorsi muscle of the adult fowl as affected by the induced hypertrophy. Arch. Geflügelk. 49. 81-90.
  • 18. Rosochacki, S. J., Grosley, B., Keller, J. S. (1986) Effect of feed intake on some lysosomal proteolytic activities in pectoral and leg muscles of growing chicken. Arch. Gellügelk. 50. 7-12.
  • 19. Schwartz, W. N., Bird, J. W. C. (1977) Degradation of myofibrillar proteins by cathepsin В and D. Biochem: J. 167. 818-820.
  • 20. Tashiro, T., Ishizaki, Y. (1982) A calcium-dependent protease selectively degrading the 160 000 MW component of neurofilaments is associated with the cytoskeletal preparation of the spinal cord and has an endogenous inhibitory factor. FEBS Letters 141. 41-44.
  • 21. Waterlow, J. C., Garlick, P. J., Millward, D. J. (1978) The effects of nutrition and hormones on protein turnover in muscle and liver. In Protein Turnover in Mammalian Tissues and in the Whole Body, eds. J. C. Waterlow, P. J., Garlick, D. J, Millward, pp. 625-746, North Holland Publishing Company, Amsterdam - New York – Oxford.
  • 22. Yoshida, H. Murachi, T., Tsukahara, I. (1984) Limited proteolysis of bovine lens α-crystallin by caplain, a Ca²⁺ -dependent cysteine proteinase, isolated from the same tissue. Bioch. Biophys. Acta 798. 252-259.

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Bibliografia

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