Chapter 1 creation: The category of Proteinases (pages 1–13): Alan J. Barrett
Chapter 2 Lysosomal Cysteine Proteinases (pages 15–35): H. Kirschke, J. Langner, S. Riemann, B. Wiederanders, S. Ansorge and P. Bohley
Chapter three Cathepsin D: The Lysosomal Aspartic Proteinase (pages 37–50): Alan J. Barrett
Chapter four Human Leucocyte Elastase and Cathepsin G: Structural and practical features (pages 51–68): James Travis, P.J. Giles, L. Porcelli, C.F. Reilly, R. Baugh and J. Powers
Chapter five Human Collagenases: Comparative and Immunolocalization stories (pages 69–86): David E. Woolley
Chapter 6 Proteinases in Connective Tissue Breakdown (pages 87–103): David J. Etherington
Chapter 7 mobile Mechanisms of Proteinase unencumber from Inflammatory Cells and the Degradation of Extracellular Proteins (pages 105–121): Marco Baggiolini, Jorg Schnyder, Ursula Bretz, Beatrice Dewald and Walter Ruch
Chapter eight Inactivation of Cytosol Enzymes through a Liver Membrane Protein (pages 123–137): G.L. Francis, S.E. Knowles and F.J. Ballard
Chapter nine Lysosomes and Protein Degradation (pages 139–149): Roger T. Dean
Chapter 10 Insights into Mechanisms of Intracellular Protein Turnover from reports on Pinocytosis (pages 151–165): J.B. Lloyd
Chapter eleven Turnover and Degradation of Mitochondria and Their Proteins (pages 167–188): Santiago Grisolia, Erwin Knecht, Jose Hernandez?Yago and Ruth Wallace
Chapter 12 Protein Degradation in Cells in tradition (pages 189–203): Brian Poole, Shoji Ohkuma and Michael Warburton
Chapter thirteen legislation of Protein Breakdown in Hepatocyte Monolayers (pages 205–218): M.F. Hopgood and F.J. Ballard
Chapter 14 a potential function for impartial Proteolysis within the Degradation of Intracellular Proteins (pages 219–225): John Kay
Chapter 15 reviews of the ATP Dependence of Protein Degradation in Cells and telephone Extracts (pages 227–251): Alfred L. Goldberg, Nina P. Strnad and K.H. Sreedhara Swamy
Chapter sixteen Coordination of Protein Synthesis and Degradation (pages 253–280): R. John Mayer, Susan M. Russell, Rowland J. Burgess, Colin J. Wilde and Norman Paskin
Chapter 17 software of Liver Perfusion as an in vitro version in reviews of Intracellular Protein Degradation (pages 281–305): Glenn E. Mortimore and Charles M. Schworer
Chapter 18 Protein Degradation and the legislation of Protein stability in Muscle (pages 307–329): D.J. Millward, %. Bates, J.G. Brown, S.R. Rosochacki and M.J. Rennie
Chapter 19 Protein Degradation in Metabolic and dietary issues (pages 331–350): J. Fred cube and Carlos D. Walker
Chapter 20 Proteinase Inhibitors in serious Inflammatory techniques (Septic surprise and Experimental Endotoxaemia): Biochemical, Pathophysiological and healing points (pages 351–379): Hans Fritz
Chapter 21 impartial Proteinases of Leucocytes and the Inflammatory strategy (pages 381–402): J.?D. Vassalli, A. Granelli?Piperno and E. Reich
Chapter 22 Concluding feedback (pages 403–406): Alan J. Barrett
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Extra info for Ciba Foundation Symposium 75 - Protein Degradation in Health and Disease
26 H . K I R S C H K E ET AL Phe-Phe are powerful inhibitors of cathepsin L (Table 6). In contrast, and in accordance with its substrate specificity, namely hydrophobic amino acids in P2 and P3, cathepsin L is less sensitive to inhibition by the diazomethyl ketones of Z-Gly-Gly-Pro, Z-Pro-Gly, Z-Gly-Gly-Val, Z-Gly-Gly-Phe, ZGly-Gly-Ala, Z-Gly-Gly-Leu, Z-Ala-Ala and Z-Lys. In contrast to their action on cathepsin L, diazomethyl ketones inhibit cathepsin B at decreased rates: Z-Phe-Ala, Z-Phe-Gly, Z-Ala-Ala, Z-Lys and Z-Phe-Phe.
Barrett: The only good data are for rabbit (Lapresle 1971, Jasani et al 1978). A Japanese study (Yamamoto et a1 1978) has been published on rat spleen cathepsin E.
By far the best inhibitor of the breakdown of added proteins is leupeptin. It is slightly better than antipain, which is better than chymostatin. Pepstatin (the cathepsin D inhibitor) is the least effective of the inhibitors tested. We find the same order of effectiveness of the inhibitors when we measure the breakdown of intracellular protein, so that even if these particular cells have a lot of cathepsin D, it doesn’t seem to have an important role in degrading exogenous protein. The yolk sac may be entirely different from Kupffer cells, of course.
Ciba Foundation Symposium 75 - Protein Degradation in Health and Disease