Abnormal expression of lysosomal cysteine proteinases in muscle wasting diseases

  • Nobuhiko Katunuma
  • Eiki Kominami
Part of the Reviews of Physiology, Biochemistry and Pharmacology book series (volume 108)


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  1. Ballard FJ, Thomas FM, Sterun LM (1979) Increased turnover of muscle contractile proteins in Duchenne muscular dystrophy as assessed by 3-methylhistidine and creatinine excretion. Clin Sci 56:347–352PubMedGoogle Scholar
  2. Bando Y, Kominami E, Katunuma N (1986) Purification and tissue distribution of rat cathepsin L. J Biochem (Tokyo) 100:35–42PubMedGoogle Scholar
  3. Bird JWC, Carter JH (1980) Proteolytic enzymes in striated and non-striated muscle. In: Wildenthal K (ed) Degradative processes in heart and skeletal muscle. Elsevier, Amsterdam, pp 51–85Google Scholar
  4. Bird JWC, Roisen FJ (1986) Lysosomes in muscle: developmental aspects, enzyme activities, and role in protein turnover. In: Engel AG, Banker BQ (eds) Myology. McGraw-Hill, New York, pp 745–767Google Scholar
  5. Bird JWC, Roisen FJ, Yorke G, Lee JA, McElligott MA, Triemer DJ, St. John A (1981) Lysosomes and proteolytic activities in cultured striated muscle cells. J Histochem Cytochem 29:431–439PubMedGoogle Scholar
  6. Bodensteiner JB, Engel AG (1978) Intracellular accumulation in Duchenne dystrophy and other myopathies: a study of 567,000 muscle fibers in 114 biopsies. Neurology (Minneapolis) 28:439–448PubMedGoogle Scholar
  7. Busch WA, Stromer MH, Goll DE, Suzuki A (1972) Ca2+ specific removal of Z-line from rabbit skeletal muscle. J Cell Biol 52:367–381CrossRefPubMedGoogle Scholar
  8. Bahlmann B, Kuehn L, Rutschmann M, Reinauer H (1985) Purification and characterization of a multicatalytic high-molecular-mass proteinase from rat skeletal muscle. Biochem J 228:161–170PubMedGoogle Scholar
  9. Decker RS, Decker M, Pool AR (1980) The distribution of lysosomal cathepsin D in cardiac myocytes. J Hitochem Cytochem 28:231–237Google Scholar
  10. Denke SM, Fanburg JL (1980) Normobasic oxygen toxicity of the lung. N Engl J Med 303:76–86PubMedGoogle Scholar
  11. Fingerman E, Campisi J, Pardee AB (1984) Defective Ca2+ metabolism in Duchenne muscular dystrophy: effects on cellular and viral growth. Proc Natl Acad Sci USA 81:7617–7621PubMedGoogle Scholar
  12. Fong D, Calhoun DH, Hsieh WT, Lee B, Wells RT (1986) Isolation of a c-DNA clone for the human lysosomal proteinase cathepsin B. Proc Natl Acad Sci USA 83:2909–2913PubMedGoogle Scholar
  13. Furuno K, Ishikawa T, Kato K (1982) Appearance of autolysosomes in rat liver after leupeptin treatment. J Biochem (Tokyo) 91:1485–1494PubMedGoogle Scholar
  14. Furuno K, Miwa N, Kato K (1983) Receptor-mediated introduction of pepstatin-asialofetuin conjugate into lysosomes of rat hepatocytes. J Biochem (Tokyo) 93:249–256PubMedGoogle Scholar
  15. Gelard KW, Schneider DL (1979) Evidence for degradation of myofibrillar proteins in lysosomes. J Biol Chem 254:11798–11805PubMedGoogle Scholar
  16. Goldberg AL, Baracos V, Rodemann HP, Dianarello CA, Waxman L (1984) Control of protein degradation in muscle by prostaglandins, Ca2+, and leukocyte pyrogen (interleukin 1). Fed Proc 43:1301–1306PubMedGoogle Scholar
  17. Goldspink DF, Goldspink G (1977) Age related changes in protein turnover and ribonucleic acid of diaphragm muscle of normal and dystrophic hamsters. Biochem J 162:191–194PubMedGoogle Scholar
  18. Higuchi I, Ishiura S, Sugita H, Ii K, Katunuma N (1986) The therapeutic effect of cysteine proteinase inhibitor. EST, on experimental chloroquine myopathy. (In Japanese, abstract) English. Clin Neurol 26:928–936Google Scholar
  19. Huston RB, Krebs EG (1968) Activation of skeletal muscle phosphorylase kinase by Ca2+. II. Identification of the kinase activating factor as a proteolytic enzyme. Biochemistry 7:2116–2122CrossRefPubMedGoogle Scholar
  20. Ii K, Hizawa K, Kominami E, Bando Y, Katunuma N (1985) Different immunolocalization of cathepsins B, H and L in the liver. J Histochem Cytochem 33:1173–1175PubMedGoogle Scholar
  21. Ii K, Hizawa K, Nonaka L, Sugita H, Kominami E, Katunuma N (1986) Abnormal increases of lysosomal cysteine proteinases in rimmed vacuoles in the skeletal muscle. Am J Pathol 122:193–198PubMedGoogle Scholar
  22. Iodice AA, Clin J, Perker S, Weinstock IM (1972) Cathepsins A, B, C D and autolysis during development of breast muscle of normal and dystrophic chickens. Arch Biochem Biophys 152:166–174CrossRefPubMedGoogle Scholar
  23. Ishiura S, Nonaka I, Nakase H, Tada A, Sugita H (1984) Two step mechanism of myofibrillar protein degradation in acute plasmocid-induced muscle necrosis. Biochim Biophys Acta 798:333–342PubMedGoogle Scholar
  24. Jackson MJ, Johnes DA, Edwards RHT (1984) Techniques for studying radical damage in muscular dystrophy. Med Biol 62:135–138PubMedGoogle Scholar
  25. Kar NC, Pearson CM (1978) Dipeptidyl peptidases in human muscle diseases. Clin Chim Acta 82:185–192CrossRefPubMedGoogle Scholar
  26. Kar NC, Pearson CM (1979b) Catalase, superoxide dismutase, glutathione reductase and thiobarbituric acid reactive products in normal and dystrophic human muscle. Clin Chim Acta 94:277–280CrossRefPubMedGoogle Scholar
  27. Katunuma N, Kominami E (1983) Structures and functions of lysosomal thiol proteinases and their endogenous inhibitors. In: Horecker BL, Stadtman ER (eds) Current topics in cellular regulation, vol 22, Academic, New York, pp 71–101Google Scholar
  28. Katunuma N, Kominami E (1986) Molecular basis of intracellular regulation of thiol proteinase inhibitors. In: Horecker BL, Stadtman ER (eds) Current topics in cellular regulation, vol 27. Academic, New York, pp 345–360Google Scholar
  29. Katunuma N, Noda T (1980) Cathepsin B, H and L and intracellular protein degradation in atrophic muscle of muscular dystrophy. In: Ebashi S (ed) Muscular dystrophy. University of Tokyo Press, Tokyo, pp 225–237Google Scholar
  30. Katunuma N, Kominami E, Kobayashi K, Banno Y, Suzuki K, Chichibu K, Hamaguchi Y, Katsunuma T (1975) Studies on new intracellular proteases in various organs of rat I. Purification and comparison of their properties. Eur J Biochem 52:37–50CrossRefPubMedGoogle Scholar
  31. Katunuma N, Yasogawa N, Kito K, Sanada Y, Miyoshi K (1978) Abnormal expression of a serine protease in human dystrophic muscle. J Biochem (Tokyo) 83:625–628PubMedGoogle Scholar
  32. Katunuma N, Kominami E, Noda T, Isogai K (1983) Lysosomal thiol proteinases and muscular dystrophy. In: Ebashi S, Ozawa E (eds) Muscular dystrophy: biomedical aspects. Springer, Berlin Heidelberg New York Tokyo, pp 247–256Google Scholar
  33. Kitchin SE, Watts DC (1973) Comparison of the turnover patterns of total and individual muscle proteins in normal mice and those with hereditary muscular dystrophy. Biochem J 136:1017–1028PubMedGoogle Scholar
  34. Kominami E, Katunuma N (1983) Lysosomal thiol proteinases in plasmocid-induced myopathy. In: Annual report of clinical research group of muscular dystrophy, Japan, pp 195–197 (In Japanese, author's translation)Google Scholar
  35. Kominami E, Wakamatsu N, Katunuma N (1982) Purification and characterization of thiol proteinase inhibitor from rat liver. J Biol Chem 257:14648–14652PubMedGoogle Scholar
  36. Kominami E, Hashida S, Kahirallah EA, Katunuma N (1983) Sequestration of cytoplasmic enzymes in an autophagic vacuole-lysosomal system induced by injection of leupeptin. J Biol Chem 258:6093–6100PubMedGoogle Scholar
  37. Kominami E, Bando Y, Ii K, Hizawa K, Katunuma N (1984a) Increases in cathepsin B and L thiol proteinase inhibitors in muscle of dystrophic hamsters. Their localization in invading phagocytes. J Biochem (Tokyo) 96:1941–1948Google Scholar
  38. Kominami E, Bando Y, Wakamatsu N, Katnunuma B (1984b) Different tissue distributions of two types of thiol proteinase inhibitors from rat liver and epidermis. J Biochem (Tokyo) 96:1437–1442PubMedGoogle Scholar
  39. Kominami E, Tsukahara T, Bando Y, Katunuma N (1985) Distribution of cathepsins B and H in rat tissues and peripheral blood cells. J Biochem (Tokyo) 98:87–93PubMedGoogle Scholar
  40. Kominami E, Ii K and Katunuma N (1987) Activation of the intramyofibral autophagic lysosomal system in muscular dystrophy. Am J Pathol 127(3):21–26Google Scholar
  41. Kunkel LM et al. (1986) Analysis of deletions in DNA from patients with Becker and Duchenne muscular dystrophy. Nature 322:73–77PubMedGoogle Scholar
  42. Matkovicks B, Laszlo A, Szabo L (1982) A comparative study of superoxide dismutase, catalase and lipid peroxidation in red blood cells from muscular dystrophy patients and normal controls. Clin Chim Acta 118:289–292CrossRefPubMedGoogle Scholar
  43. Matsukura U, Okitani A, Nishimoto T, Kato H (1981) Mode of degradation of myofibrillar proteins by endogenous protease, cathepsin L. Biochim Biophys Acta 662;41–47PubMedGoogle Scholar
  44. McCord JM (1974) Free radicals and inflammation: protection of synovial fluid by superoxide dismutase. Science 195:529–531Google Scholar
  45. Millward D, Bates P, Brown JG, Cox M, Jepson M, Pell J (1985) In: Khairallah E, Bond JS, Bird JWC (eds) Intracellular protein catabolism. Liss, New York, pp 531–542Google Scholar
  46. Mitch WE, Clark AS (1984) Specificity of the effects of leucine and its metabolism on protein degradation in sekeletal muscle. Biochem J 222:579–586PubMedGoogle Scholar
  47. Mizuno Y (1984) Changes in superoxide dismutase, catalase, glutathione peroxidase, and glutathione reductase activities and thiobarbituric reactive product levels in early stage of development in dystrophic chickens. Exp Neurol 84:58–73CrossRefPubMedGoogle Scholar
  48. Mortimore GE, Schworer CM (1977) Induction of autophagy by amino acid depriation in perfused rat liver. Nature 270:174–176CrossRefPubMedGoogle Scholar
  49. Monaco AP, Bertelson CJ, Middlesworth W, Colletti CA, Aldridge J, Fischbeck KH, Barlett R, Pericak-Vance MA, Roses AD, Kunkel LM (1985) Detection of deletions spanning the Duchenne muscular dystrophy locus using a tightly linked DNA segment. Nature 316:842–845CrossRefPubMedGoogle Scholar
  50. Noda T, Isogai K, Hayashi H, Katunuma N (1981) Susceptibilities of various myofibrillar proteins to cathepsin B and morphological alteration of isolated myofibrils by this enzyme. J Biochem (Tokyo) 90:371–379PubMedGoogle Scholar
  51. Ohno S, Emori Y, Imajoh S, Kawasaki H, Kisaragi M, Suzuki K (1984) Evolutionary origin of a calcium dependent protease by fusion of genes for a thiol protease and a calcium-binding protein? Nature 313:566–570CrossRefGoogle Scholar
  52. Ohshita T, Kominami E, Ii K, Katunuma N (1986) Effect of starvation and refeeding on autophagy and heterophagy in rat liver. J Biochem (Tokyo) 100:623–632PubMedGoogle Scholar
  53. Pearson CH, Kar NC (1979) Muscle breakdown and lysosomal activation. (Biochemistry). Ann NY Acad Sci 317:465–477PubMedGoogle Scholar
  54. Pennington RJ (1977) Proteinases in muscle. In: Barrett AJ (ed) Proteinases in mammalian cells and tissues. Elsevier, Amsterdam, pp 515–543Google Scholar
  55. Pennington RJ, Robinson CM (1968) Cathepsin activity in normal and dystrophic human muscle. Enzymol Biol Clin 9:175–182Google Scholar
  56. Poso AR, Mortimore EG (1984) Requirement for alanine in the amino acid control of deprivation-induced protein degradation in liver. Proc Natl Acad Sci USA 81:4270–4274PubMedGoogle Scholar
  57. Rodemann HP, Bayreuther K (1986) Differential degradation of (35S)-methionine polypeptides in Duchenne muscular dystrophy skin fibroblasts in vitro. Proc Natl Acad Sci USA 83:2086–2090PubMedGoogle Scholar
  58. Rouke AW (1975) Myosin in developing normal and dystrophic chicken pectoralis. I. Synthesis and degradation. J Cell Physiol 86:343–352CrossRefPubMedGoogle Scholar
  59. Sanada Y, Yasogawa N, Katunuma N (1978) Serine protese in mice with hereditary muscular dystrophy. J Biochem (Tokyo) 83:27–33PubMedGoogle Scholar
  60. Sano M (1985) Biochemical studies in experimental chloroquine myopathy (In Japanese, English abstract). Clin Neurol 25:627–636Google Scholar
  61. Seglen PO, Gordon PB, Poli A (1980) Amino acid inhibition of the autophagic/lysosomal pathway of protein degradation in isolated rat hepatocytes. Biochem Biophys Acta 630:103–118PubMedGoogle Scholar
  62. Segundo BS, Chan SJ, Steiner DF (1985) Identification of cDNA clones encoding a precursor of rat liver cathepsin B. Proc Natl Acad Sci USA 82:2320–2324PubMedGoogle Scholar
  63. Takeichi S, Tokunaga I, Yoshima K, Maeiwa M, Bando Y, Kominami E, Katunuma N (1984) Mechanisms of postmortem autolysis of sekeletal muscle. Biochem Med 32:341–348CrossRefPubMedGoogle Scholar
  64. Takio K, Towatari T, Katunuma N, Teller DC, Titani K (1983a) Homology of amino acid sequences of rat liver cathepsins B and H with that of papain. Proc Natl Acad Sci USA 80:3666–3670PubMedGoogle Scholar
  65. Takio K, Kominami E, Wakamatsu N, Katunuma N, Titani K (1983b) Amino acid sequence of rat liver thiol proteinase inhibitor. Biochem Biophys Res Commun 115:902–908CrossRefPubMedGoogle Scholar
  66. Takio K, Kominami E, Bando Y, Katunuma N, Titani K (1984) Amino acid sequence of rat epidermis thiol proteinase inhibitor. Biochem Biophys Res Commun 121:149–154PubMedGoogle Scholar
  67. Tawa NE Jr, Goldberg AL (1986) Protein and amino acid metabolism in muscle. In: Engel AG, Banker BQ (eds) Myology. McGraw-Hill, New York, pp 721–743Google Scholar
  68. Weinstock IM, Iodice AA (1969) Acid hydrolase activity in muscular dystrophy and denervation atrophy. In: Dingle JT, Fell FB (eds) Lysosomes in biology and pathology. Elsevier, New York, pp 450–468Google Scholar
  69. Woodbury RG, Everitt M, Sanada Y, Katunuma N, Lagunoff D, Neurath H (1978) A major serine protease in rat sekeletal muscle; evidence for its mast cell origin. Proc Natl Acad Sci USA 75:5311–5313PubMedGoogle Scholar

Copyright information

© Springer-Verlag 1987

Authors and Affiliations

  • Nobuhiko Katunuma
    • 1
  • Eiki Kominami
    • 1
  1. 1.Department of Enzyme Chemistry, Institute for Enzyme Research, School of Medicinethe University of TokushimaTokushimaJapan

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