Abstract
It is well established that in protein metabolism protein synthesis as well as protein degradation are equally important for maintaining cellular viability. Thus, a basal level of intracellular proteolysis is measurable in living cell 1 , which comprises post-translational processing of newly synthesized proteins 2, degradation of missense proteins 3 as well as breakdown of inactivated proteins having lost their functions 4,5. In addition to the ’basal degradation ‘ an ’accelerated proteolysis‘ takes place in the cells living under conditions of nutrition deprivation as well as hormone or amino acid deficiency 6,7. For catalysis of these various intracellular proteolytic events multiple proteolytic pathways exist in a mammalian cell 8-11. One of the major sites of intracellular proteolysis is the lysosomal compartment. However, since the lysosomal cathepsins have no free access to the protein substrates, initial rate-limiting steps of intracellular proteolysis probably proceed extra-lysosomally. The aim of our investigations is to identify, isolate and characterize the enzymes catalyzing steps of these extra-lysosomal pathways.
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References
Amenta,J.S. & Brocher,S.C.: Mechanisms of protein turnover in cultured cells. Life Sciences 28: 1195–1208 (1981)
Dean,R.T. & Judah,J.D.: Post–translational proteolytic processing of polypeptides. Comp. Biochem. 19B: 233–298 (1980)
Klemes,Y., Etlinger,J.D. & Goldberg,A.L.: Properties pf abnormal proteins degraded rapidly in reticulocytes. J.Biol.Chem. 256: 8436–8444 (1981)
Ballard,F.J.: Intracellular protein degradation. Essays Biochem. 13: 1–37 (1978)
Holzer,H. & Heinrich,P.C.: Control of proteolysis. Ann.Rev.Biochem. 49: 63–91 (1980)
Mortimore,G.E.: Mechanisms of cellular protein catabolism. Nutr. Rev. 40: 1–12 (1982)
Ballard,F.J. & Gunn,J.M.: Nutritional and hormonal effects on intracellular protein catabolism. Nutr.Rev. 40: 33–42 (1982)
Glaumann,H., Ericsson,J.L.E. & Marzella,L.: Mechanisms of intralysosomal degradation with special reference to autophagocytosis and heterophagocytosis of cell organelles. Int.Rev.Cvtol. 73: 149–182 (1981)
Hershko,A. & Ciehanover,A.: Mechanisms of intracellular protein breakdown. Ann.Rev.Biochem. 51: 335–364 (1982)
Ciehanover,A., Finley,D. & Varshavsky,A.: The ubiquitin–mediated proteolytic pathway and mechanisms of energy-dependent intracellular protein degradation. J.Cell.Biochem. 24: 27–53 (1984)
Pontremoli,S. & Melloni,E.: Extralysosomal protein degradation. Ann. Rev.Biochem. 55: 455–481 (1986)
Dahlmann,B.: High–Mr cysteine proteinases from rat skeletal muscle. Biochem.Soc.Trans. 13: 1021–1023 (1985)
Dahlmann,B., Kuehn,L., Rutschmann,M. & Reinauer,H.: Purification and characterization of a multicatalytic, high-molecular-mass proteinase from rat skeletal muscle. Biochem.J. 228: 161–170 (1985)
Dahlmann,B., Kuehn,L. & Reinauer,H.: Identification of two alkaline cysteine proteinases from rat skeletal muscle. in: Cysteine Proteinases and their Inhibitors. (Turk,V., ed.) pp. 133–146 Walter de Gruyter & Co. Berlin, New York (1986)
Kopp,F., Steiner,R., Dahlmann,B., Kuehn,L. & Reinauer,H.:Size and shape of the multicatalytic proteinase from rat skeletal muscle. Biochim.Biophys.Acta 872: 253–260 (1986)
Hartley,B.S.: Proteolytic enzymes. Ann. Rev.Biochem. 29: 45–72 (1960)
Dahlmann,B., Rutschmann,M., Kuehn,L. & Reinauer,H.: Activation of the multicatalytic proteinase from rat skeletal muscle by fatty acids or sodium dodecyl sulphate. Biochem.J. 228: 171–177 (1985)
Dahlmann,B., Kuehn,L. & Reinauer,H.: Identification of three high molecular mass cysteine proteinases from rat skeletal muscle. FEBS-Lett. 160: 243–247 (1983)
Stauber,W.T., Fritz,V.K., Dahlmann,B., Kay,J., Heath,R. & Mayer,M.: Alkaline proteinase localization in myoblasts. J.Histochem.Cytochem. 35: 83–86 (1987)
Fagan,J.M., Waxman,L. & Goldberg,A.L.: Skeletal muscle and liver contain a soluble ATP+ubiquitin-dependent proteolytic system. Biochem.J. 243: 335–343 (1987)
Dahlmann,B., Kopp,F., Kuehn,L., Reinauer,H. & Schwenen,M.: Studies on the multicatalytic proteinase from rat skeletal muscle. Biomed. Biochim.Acta 45: 1493–1501 (1986)
Dahlmann,B., Kuehn,L., Reinauer,H. & Kay.J.: Multicatalytic proteinase activity in skeletal muscle from starving rat. Biochem.Soc.Trans. (1987) in the press
Kuehn,L., Dahlmann,B. & Reinauer,H.: Tissue distribution of the multicatalytic proteinase in the rat: An immunological and enzymic study. Cienc.Biol. 11: 101–107 (1986)
Wilk,S. & Orlowski,M.: Cation sensitive neutral endopeptidase:Isolatian and specificity of the bovine pituitary enzyme. J.Neurochem. 35: 1172–1182 (1980)
Edmunds,T. & Pennington,R.J.T.: A high molecular weight peptide hydrolase in erythrocytes. Int.J.Biochem. 14: 701–703 (1982)
Hardy,M.F., Mantle,D. & Pennington,R.J.T.: Characteristics of a new muscle protease. Biochem.Soc.Trans. 11: 348–349 (1983)
Ray,K. & Harris,H.: Purification of a neutral lens endopeptidase: close similarity to a neutral proteinase in pituitary. Proc.Natl.Acad.Sci. U.S.A. 82; 7545–7549 (1985)
Rivett,A.J.: Purification of a liver alkaline protease which degrades oxidatively modified glutamine synthetase. J.Biol.Chem. 260: 12600–12606 (1985)
Ishiura,S., Sano,M., Kamakura,K..& Sugita,H.: Isolation of two forms of the high molecular mass serine protease, ingensin, from porcine skeletal muscle. FEBS-Lett. 189: 119–123 (1985)
Ishiura,S., Yamamoto,T., Nojima,M. & Sugita,H.: Ingensin, a fatty acid activated serine proteinase from rat liver cytosol. Biochim.Biophys. Acta 882: 305–310 (1986)
Nojima,M., Ishiura,S., Yamamoto,T., Okuyama,T., Furuya,H. & Sugita,H.: Purification and characterization of a high molecular weight protease, ingensin, from human placenta. J.Biochem. 99: 1605–1611 (1986)
Ishiura,S. & Sugita,H.: Ingensin, a high molecular mass alkaline protease from rabbit reticulocyte. J.Biochem. 100: 753–763 (1986)
McGuire,M.J. & DeMartino,G.N.: Purification and characterization of a high molecular weight proteinase (macropain) from human erythrocytes. Biochim.Biophys.Acta 873: 279–289 (1986)
Tanaka,K., Ii,K., Ichihara,A., Waxman,L. & Goldberg,A.L.: A high molecular weight protease in the cytosol of rat liver. I. Purification, enzymological properties and tissue distribution. J.Biol.Chem. 261: 15197–15203 (1986)
Zolfaghari,R., Baker,C.R.F., Canizaro,P.C., Amirgholami,A. & Behal,F.J.: A high molecular mass neutral endopeptidase-24.5 from human lung. Biochem.J. 241: 129–135 (1987)
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© 1988 Plenum Press, New York
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Dahlmann, B., Kuehn, L., Kopp, F., Reinauer, H., Stauber, W.T. (1988). Non - Lysosomal, High - Molecular - Mass Cysteine Proteinases from Rat Skeletal Muscle. In: Hörl, W.H., Heidland, A. (eds) Proteases II. Advances in Experimental Medicine and Biology, vol 240. Springer, Boston, MA. https://doi.org/10.1007/978-1-4613-1057-0_26
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DOI: https://doi.org/10.1007/978-1-4613-1057-0_26
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