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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© 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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