Cysteine Proteinases and their Inhibitors : : Proceedings of the International Symposium Portoroz, Yugoslavia, September 15–18, 1985 / / ed. by Vito Turk.

• Superior document: Title is part of eBook package: De Gruyter DGBA Reference Works <1990
• MitwirkendeR: Abrahamson, M.,; Alavaikko, M.,; Aragon-Ortiz, F.,; Arbanas, V.,; Arnason, A.,; Asbóth, B.,; Babnik, J.,; Bando, Y.,; Barrett, A.J.,; Bieth, Joseph G.,; Bige, L.,; Bird, J.W.C.,; Blanc, C.,; Blondal, H.,; Bláha, I.,; Bots, G.T.A.M.,; Bourgarit, J.J.,; Brocklehurst, K.,; Brown, M.A.,; Brzin, J.,; Buttle, D.J.,; Casali, B.,; Cattaneo, A.,; Chappell, C.L.,; Chatterjee, R.,; Cimerman, N.,; Colle, A.,; Cordova, A.,; Dahlmann, B.,; Davinič, S.,; Day, N.A.,; Denteš, J.,; Deval, C.,; Dittmer, H.,; Dolinar, M.,; Donati, M.B.,; Dresden, H.H.,; Dunn, A.D.,; Duswald, K.H.,; Délaissé, J.M.,; Eeckhout, Y.,; El Moujahed, A.,; Emori, F.,; Engler, R.,; Epstein, W.L.,; Esnard, F.,; Etherington, D.J.,; Falanga, A.,; Fekete, E.,; Fossati, G.,; Frangione, B.,; Fritz, H.,; Fritz, Hans,; Fukuyama, K.,; Gauthier, F.,; Gay, N.,; Gilles, A.-M.,; Gordon, S.G.,; Grab, D.J.,; Graham Knight, C.,; Grubb, A.,; Gubenšek, F.,; Gudmundsson, G.,; Gutman, N.,; Hanada, K.,; Higashiyama, S.,; Honn, K.V.,; Hopsu-Havu, V.K.,; Imahori, K.,; Imajoh, S.,; Inomata, M.,; Isemura, M.,; Isemura, S.,; Ishiguro, H.,; Ishiura, S.,; Ito, S.,; Ivanoff, L.,; Jensson, O.,; Jochum, M.,; Järvinen, M.,; Kaji, H.,; Kalnitsky, G.,; Kannagi, R.,; Kato, Y.,; Katunuma, N.,; Kawasaki, H.,; Kawashima, G.,; Kawashima, S.,; Keil, B.,; Kellermann, Josef,; Kembhavi, A.A.,; Kettner, C.,; Kokalj, M.,; Kominami, E.,; Korant, B.,; Korbelik, M.,; Kortmann, H.,; Kos, J.,; Kostka, V.,; Kotnik, M.,; Kotnik, Matjaž,; Koyama, I.,; Kuehn, L.,; Kunimatsu, M.,; Kurachi, K.,; Kóródi, I.,; Lacourt, A.,; Lah, T.T.,; Lang, H.,; Ledent, P.,; Lenarčič, B.,; Leung-Tack, J.,; Levy, H.,; Lipperheide, C.,; Lofberg, H.,; Lones, M.,; Lonsdale-Eccles, J.D.,; Lottspeich, Friedrich,; Luyendijk, W.,; Machleidt, I.,; Machleidt, W.,; Machleidt, Werner,; Maciewicz, R.A.,; Maksimenko, A.V.,; Manuel, Y.,; Mason, Robert W.,; Matsumoto, K.,; Mege, J.L.,; Meloun, B.,; Mignatti, P.,; Mihara, H.,; Moreau, T.,; Mort, J.S.,; Muller-Esterl, W.,; Murachi, T.,; Murrills, R.A.,; Müller-Esterl, W.,; Müller-Esterl, Werner,; Nakagawa, H.,; Nakamura, M.,; Nakano, S.,; Namikawa, C.,; Neumann, S.,; Nishida, Y.,; Obled, A.,; Obshita, T.,; Oguma, K.,; Ohkubo, I.,; Ohno, S.,; Ohtaki, S.,; Omura, S.,; Otto, K.,; Ouali, A.,; Pagano, M.,; Parkes, C.,; Passerini, C.G.,; Petrovic, D.,; Petteway, S.,; Petursdottir, I.,; Pohl, J.,; Polgár, L.,; Popovic, T.,; Popović, T.,; Popovič, Tatjana,; Poulik, M.D.,; Prevot, D.,; Pugh, D.,; Rawlings, N.D.,; Recklies, A.D.,; Reinauer, H.,; Rifkin, D.B.,; Rinne, A.,; Ritonja, A.,; Rohrlich, S.T.,; Roisen, F.J.,; Rozhin, J.,; Saitoh, E.,; Sakihama, T.,; Salvesen, G.,; Samejima, T.,; Sanada, K.,; Sansot, J.L.,; Sasaki, M.,; Schauer, P.,; Seigfried, Z.,; Sekine, T.,; Semeraro, N.,; Shiokawa, H.,; Silver, I.A.,; Skrk, J.,; Sloane, B.F.,; Sohár, I.,; Sugita, H.,; Suhar, A.,; Sumi, H.,; Suzuki, K.,; Takasawa, T.,; Takeda, A.,; Tamai, M.,; Taylor, M.A.J.,; Thorsteinsson, L.,; Toki, N.,; Toku, S.,; Towatari, T.,; Trstenjak, M.,; Tsushima, H.,; Turk, V.,; Turk, Vito,; Türk, Vito,; Vaes, G.,; Valin, C.,; Vitale, Lj.,; Walker, J.,; Wardale, R.J.,; Wood, L.,; Yamamoto, K.,; Yamato, Susumu,; Yorke, G.,; Čurin, V.,; Šali, A.,; Štrop, P.,
• HerausgeberIn: Turk, Vito,
• Place / Publishing House: Berlin ;, Boston : : De Gruyter, , [2019]; ©1986
• Year of Publication: 2019
• Edition: Reprint 2019
• Language: English
• Physical Description: 1 online resource (846 p.) :; Num. figs

Table of Contents

• Frontmatter
• PREFACE
• ACKNOWLEDGEMENT
• ORGANIZING COMMITTEE
• CONTENTS
• NOMENCLATURE AND CLASSIFICATION OF THE PROTEINS HOMOLOGOUS WITH THE CYSTEINE PROTEINASE INHIBITOR CHICKEN CYSTATIN
• GENERAL CYSTEINE PROTEINASES
• Isolation, properties , primary structure and cloning
• Human cathepsins B, H and L: characterization by amino acid sequences and some kinetics of inhibition by the kininogens
• Tentative amino acid sequence of bovine spleen cathepsin B
• Inhibition of human liver cathepsins B, H and L by the human α2 cysteine proteinase inhibitor
• Human kidney cathepsin L
• Latent human cathepsin L
• Cloning of a bovine protein homologous with cysteine proteinases and identification of the gene
• Immunological studies on the secreted forms of cathepsin B
• A study of the peptidyldipeptidase activity of bovine spleen cathepsin B using synthetic substrates
• Comparison of characteristics and drug-induced modifications of rat spleen cathepsins B and H
• Cystein proteinase activities in embryonic chicken sekeletal muscle
• Histone degradation by lysosomal proteases
• Properties of a cysteine proteinase from human thyroids
• Primary structure and function of calcium activated neutralprotease
• Identification of two alkaline cysteine proteinases from rat skeletal muscle
• Multiple forms, structure and specificity of clostripain
• Enzymatic and immunological identification of a cysteine proteinase procoagulant in human melanoma
• Thyroid cysteine proteinases that catalyze release of thyroxine from thyroglobulin and thyroxine-containing peptide
• Proteases in African trypanosomes
• Characterization of a cysteinyl proteinase from the human parasite, Schistosoma mansoni
• Studies on a proteinase inactivating enzyme from the basidiomycete Coprinus atramentarius
• GENERAL CYSTEINE PROTEINASES OF DIFFERENT ORIGIN
• Localization and biological role
• Distributions and localizations of lysosomal cysteine proteinases and cystatins
• Functional shares of cathepsins B, H and L in autophagy and heterophagy
• Post mortem localization of lysosomal peptide hydrolase, cathepsin B
• Bifunctional derivatives of L-trans-epoxysuccinyl-L- -leucylamido-(4-amino)butane (Ep-459) as potential localization agents for cysteine proteinases
• Cysteine proteinases and bone resorption
• The role of collagen-degrading cysteine proteinases in connective tissue metabolism
• The role of cathepsins H and B, and inhibitors leupeptin and CPI in proliferative activities of non-malignant cells in culture
• Viruses as vectors for cysteine proteases
• MECHANISM OF ACTION OF CYSTEINE PROTEINASES
• Natural structural variation in the cysteine proteinases as an aid to the study of mechanism by reactivity probe kinetics, catalysis kinetics and spectroscopic methods
• Mechanism of action of cysteine proteases: 1/ differences from serine enzymes;2/ the second thiol group of chymopapain
• Proposal of the double regulation mechanism for the action of calpain
• Control mechanism of calcium-activated neutral protease (CANP) activity
• GENERAL CYSTEINE PROTEINASE INHIBITORS
• Isolation, properties and primary structure
• The mammalian cysteine proteinase inhibitors. Structural diversity and evolutionary origin
• Kininogens as thiol proteinase inhibitors
• Cystatin-like domains of LMW-kininogen, and speculations on the evolution of cystatins
• Human stefins and cystatins: their properties and structural relationships
• Isolation of kininogens using affinity chromatography
• Characterization of low molecular mass cysteine proteinase inhibitors from human amniotic fluid
• Properties and structure of human spleen stefin B - a low molecular weight protein inhibitor of cysteine proteinases
• Amino acid sequence of the cysteine proteinase inhibitor cystatin B from human liver
• Cystatin S and the related cysteine proteinase inhibitors in human saliva
• Cystatin C (Post γ Globulin) in serum from patients with autoimmune diseases
• Differential actions of human cystatin C on different functions of granulocytes
• Potentiation of excretion of canine cystatin-C (Post-gamma globulin)
• The 43 kDa papain inhibitor in human tissues
• Small and high molecular weight proteinase inhibitors from bovine muscle
• Low molecular weight protein inhibitors of cysteine proteinases from bovine parotid glands
• The interaction of papain molecule with thiol proteinase inhibitors from newborn rat epidermis
• Chicken egg white cystatin as a ligand for affinity chromatography
• Distribution of the egg white cystatin in chicken
• Isolation and characterization of chicken egg white low-Mr kininogen
• Papain inhibition by snake venoms
• Cysteine proteinase inhibitors from fish liver
• Cysteine proteinase inhibitors from sea anemone
• Characterization of low molecular weight and high molecular weight endogenous inhibitors of calcium activated neutral protease
• Calpain inhibition by peptide epoxides and the effect of autolysis
• EST, a new analog of E-64, can prolong the life span of dystrophic hamsters, UM-X7.1
• GENERAL CYSTEINE PROTEINASE INHIBITORS
• Localization, biological function and kinetics
• Cystatins A and B in normal and pathologically altered human tissues
• Chicken and rat muscle cystatins and their localization in cultured myoblasts
• Distribution and solubilization of a high molecular weight cysteine proteinase inhibitor from rat epidermis
• Possible biological functions of protein proteinase inhibitors
• A curve-fitting approach to the determination of kinetic constants of proteinase inhibitors
• Inhibition of cathepsins B, H and L by rat thiostatin, the circulating α1 cysteine proteinase inhibitor, and by an active fragment
• CYSTEINE PROTEINASES AND THEIR INHIBITORS IN TUMORS
• Tumor cysteine proteinases and their inhibitors
• Thiol protease inhibitor released from human malignant melanoma
• PROTEINASES AND THEIR INHIBITORS
• Medical aspects
• Cystatin C (α-trace) amyloidosis
• Some biochemical aspects of chymopapain treatment of sciatica
• Granulocyte proteinases as mediators of unspecific proteolysis in inflammation: a review
• LIST OF PARTICIPANTS
• AUTHOR INDEX
• SUBJECT INDEX
• Backmatter