Proteases II pp 411-419 | Cite as

Nutrition and Protease Activity

  • Joel D. Kopple
Conference paper
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 240)


The influence of nutritional intake and nutritional status on the activity of tissue proteases has been the subject of research for many years. In general, two different aspects of this subject have been investigated: 1) The effects of protein malnutrition, calorie malnutrition and proteincalorie malnutrition on protease activity and the contribution of proteases to wasting in starvation; and 2) The effect of specific nutrient deficiencies on specific proteases. This manuscript will briefly review these two areas of research.


Protease Activity Protein Malnutrition Angiotensin Converting Enzyme Activity Increase Plasma Renin Activity Serum Angiotensin Converting Enzyme Activity 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.


Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.


  1. 1.
    N.H. Munro, and M.C. Crim, The proteins and amino acids, in: Modern Nutrition in Health and Disease, 7th Edition, M.E.Shils, V.R.Young (eds.), Lea & Febiger, Philadelphia, pp. 1 (1988).Google Scholar
  2. 2.
    L.J. Hoffer, Starvation, in: Modern Nutrition in Health and Disease, 7th Edition, M.E.Shils, V.R.Young, Lea & Febiger, Philadelphia, pp. 774 (1988).Google Scholar
  3. 3.
    G.F. Cahill Jr., Starvation in man, N. Engl. J. Med. 282: 668 (1970).PubMedCrossRefGoogle Scholar
  4. 4.
    P. Felig, O.E. Owen, J. Wahren, and G.F. Cahill Jr., Amino acid metabolism during prolonged starvation, J. Clin. Invest. 48: 584 (1969).PubMedCrossRefGoogle Scholar
  5. 5.
    D.J. Millward, and J.C. Waterlow, Effect of nutrition on protein turnover in skeletal muscle, Federation Proc. 37: 2283 (1978).Google Scholar
  6. 6.
    D.J. Millward, The effect of diet on proteolytic activity in rat skeletal muscle, Proc. Nutr. Soc. 31: 3A (1972).CrossRefGoogle Scholar
  7. 7.
    S. Rosochacki, and D.J. Millward, Cathepsin D and acid autolytic activity in skeletal muscle of protein deficient, severely protein-energy restricted and refed rats. Proc. Nutr. Soc. 38(3): 137A (1979).Google Scholar
  8. 8.
    A. Roobol, and G.A.O. Alleyne, Changes in lysosomal hydrolase activity associated with malnutrition in young rats. Br. J. Nutr. 32: 189 (1974).PubMedCrossRefGoogle Scholar
  9. 9.
    K. Wildenthal, A.R. Poole, A.M Glauert, and J.T. Dingle, Dietary Control of cardiac lysosomal enzyme activities. Recent Adv. Studies Cardiac Struct. Metab. 8: 519 (1975).Google Scholar
  10. 10.
    I.D. Desai, Regulation of lysosomal enzymes. I. Adaptive changes in enzyme activities during starvation and refeeding. Can. J. Biochem. 47: 785 (1969).PubMedGoogle Scholar
  11. 11.
    A.M. Samarel, E.A. Ogunro, A.G. Ferguson, P. Allenby, and M. Lesch, Rabbit cardiac immunoreactive cathepsin D content during starvationinduced atrophy. Am. J. Physiol. 240: H222 (1981).Google Scholar
  12. 12.
    A.L.N. Smith, Effects of starvation on vacuolar apparatus of cardiac muscle tissue determined by electron microscopy, marker-enzyme assays and electrolyte studies. Cytobios 18: 111 (1977).PubMedGoogle Scholar
  13. 13.
    R.S. Decker, J.S. Crie, A.R. Poole, J.T. Dingle, and K. Wildenthal, Resistance to ischemic damage in hearts of starved rabbits - Relation with lysosomal alterations and delayed release of cathepsin D. Lab. Invest. 43: 197 (1980).PubMedGoogle Scholar
  14. 14.
    A.L. Goldberg, The regulation of protein turnover by endocrine and nutritional factors, in: Plasticity of Muscle, D. Pette (ed.), Walter de Gruyter & Co., Berlin, p. 469 (1980).Google Scholar
  15. 15.
    M.D. Thompson, and H.C. Trowell, Pancreatic enzyme activity in duodenal contents of children with a type of kwashiorkor, The Lancet 1: 1031 (1952).CrossRefGoogle Scholar
  16. 16.
    F. Gomez, R.R. Galvan, J. Cravioto, and S. Frenk, Studies on the undernourished child - Enzymatic activity of the duodenal contents in children affected with third degree malnutrition. Pediatrics 13: 548 (1954).Google Scholar
  17. 17.
    G.O. Barbezat, and J.D.L. Hansen, The exocrine pancreas and proteincalorie malnutrition, Pediatrics 42: 77 (1968).PubMedGoogle Scholar
  18. 18.
    J.N.P. Davies, The essential pathology of kwashiorkor. The Lancet 1 : 317 (1948).CrossRefGoogle Scholar
  19. 19.
    K. Gyr, R.H. Wolf, A.R. Imodi, and O. Felsenfeld, Exocrine pancreatic function in protein-deficient patas monkeys studied by means of a test meal and an indirect pancreatic function test. Gastroenterology 68: 488 (1975).PubMedGoogle Scholar
  20. 20.
    W.L. Seng, J.A. Glogowski, G. Wolf, M.B. Berman, K.R. Kenyon, and T.C. Kiorpes, The effect of thermal burns on the release of collagenase from corneas of vitamin A-deficient and control rats, Invest. Ophthalmol. Vis. Sci. 19: 1461 (1980).PubMedGoogle Scholar
  21. 21.
    M.C. Leonard, L.K. Maddison, and A. Pirie, A comparison between the enzymes in the cornea of the vitamin-A deficient rat and those of rat leukocytes, Exp. Eye Res. 33: 479 (1981).PubMedCrossRefGoogle Scholar
  22. 22.
    S.S. Twining, D.L. Hatchell, R.A. Hyndiuk, and K.F. Nassif, Acid proteases and histologic correlations in experimental ulceration in vitamin a deficient rabbit corneas. Invest. Ophthalmol. Vis. Sci. 26: 31 (1985).PubMedGoogle Scholar
  23. 23.
    W.L. Seng, K.R. Kenyon, and G.Wolf, Studies on the source and release of collagenase in thermally burned corneas of vitamin A-deficient and control rats. Invest. Ophthalmol. Vis. Sci. 22: 62 (1982).PubMedGoogle Scholar
  24. 24.
    I.M. Weinstock, A.D. Goldrich, and A.T. Milhorat, Enzyme studies in muscular dystrophy. I. Muscle proteolytic activity and vitamin E-deficiency. Proc. Soc. Exptl. Biol. Med. 88: 257 (1955).Google Scholar
  25. 25.
    T.R. Koszalka, K.E. Mason, and G. Krol, Relation of vitamin E to proteolytic and autolytic activity of skeletal muscle. J. Nutr. 73: 78 (1961).Google Scholar
  26. 26.
    A.M Spanier, and J.W.C. Bird, Endogenous cathepsin B inhibitor activity in normal and myopathic red and white skeletal muscle, Muscle & Nerve 5: 313 (1982).CrossRefGoogle Scholar
  27. 27.
    H. Zalkin, A.L. Tappel, K.A. Caldwell, S. Shibko, I.D. Desai, and T.A. Holliday, Increased lysosomal enzymes in muscular dystrophy of vitamin E-deficient rabbits. J. Biol. Chem. 237: 2678 (1962).PubMedGoogle Scholar
  28. 28.
    D.D. Dean, O.E. Muniz, I. Berman, J.C. Pita, M.R. Carreno, J.F. Woessner Jr., and D.S. Howell, Localization of collagenase in the growth plate of rachitic rats. J. Clin. Invest. 76: 716 (1985).PubMedCrossRefGoogle Scholar
  29. 29.
    M. Das, and R.L. Soffer, Pulmonary angiotensin-converting enzyme. Structural and catalytic properties. J. Biol. Chem. 250: 6762 (1975).PubMedGoogle Scholar
  30. 30.
    P.G. Reeves, and B.L. O’Dell, An experimental study of the effect of zinc on the activity of angiotensin converting enzyme in serum. Clin. Chem. 31: 581 (1985).PubMedGoogle Scholar
  31. 31.
    L.P. Dornfeld, M.H. Maxwell, A. Waks, and M. Tuck, Mechnanisms of hypertension in obesity, Kidney Int. 32 (Suppl.22): S254 (1987).Google Scholar
  32. 32.
    M.L. Tuck, J. Sowers, L.P. Dornfeld, G. Kledzik and M.H. Maxwell, The effect of weight reduction on blood pressure, plasma renin activity, and plasma aldosterone levels in obese patients, N. Engl. J. Med. 304: 930 (1981).PubMedCrossRefGoogle Scholar

Copyright information

© Plenum Press, New York 1988

Authors and Affiliations

  • Joel D. Kopple
    • 1
  1. 1.Divison of Nephrology and HypertensionHarbor-UCLA Medical Center and UCLA Schools of Medicine and Public HealthLos AngelesUSA

Personalised recommendations