References
- Barrett A J, Rawlings N D, Davies M E, Machleidt W, Salvesen G, Turk V. Cysteine proteinase inhibitors of the cystatin superfamily. Proteinase Inhibitors, A J Barrett, G Salvesen. Elsevier Scientific Publishing Co., Amsterdam 1986; 515–69
- Barrett A J, Kirschke H. Cathepsin B, cathepsin H, cathepsin L. Methods Enzymol 1981; 80: 535–61
- Marks N, Berg M J, Benuck M. Preferential action of rat brain cathepsin B as a peptidyl dipeptidase converting pro-opioid oligopeptides. Arch Bio-chem Biophys 1986; 249: 489–99
- Taugner R, Bührle C P, Nobiling R, Kirschke H. Coexistence of renin and cathepsin B in epithelioid cell secretory granules. Histochemistry 1985; 83: 103–8
- Poole A R. Tumour lysosomal enzymes and invasive growth. Lysosomes in Biology and Pathology vol. 3, J T Dingle. North-Holland Publishing Co., Amsterdam 1973; 303–7
- Sloane B F, Honn K V. Cysteine proteinases and metastasis. Cancer Mets Reviews 1984; 3: 249–63
- Burleigh M C, Barrett A J, Lazarus G S, Cathepsin B L. A lysosomal enzyme that degrades native collagen. Biochem J 1974; 137: 387–98
- Delaissé J-M, Eeckhout Y, Vaes G. In vivo and in vitro evidence for the involvement of cysteine proteinases in bone resorption. Biochem Biophys Res Commun 1984; 125: 441–7
- Suzuki K. Calcium activated neutral protease: Domain structure and activity regulation. Trends Biochem Sci 1987; 12: 103–5
- Tai J Y, Kortt A A, Liu T-Y, Elliott S D. Primary structure of streptococcal proteinase. III. Isolation of cyanogen bromide peptides: Complete covalent structure of the polypeptide chain. J Biol Chem 1976; 251: 1955–9
- Lonsdale-Eccles J D, Grab D J. Proteases in African trypanosomes. Cysteine proteinases and their inhibitors, V Turk. Walter de Gruyter, Berlin 1986; 189–97
- Korant B D, Brzin J, Turk V. Cystatin, a protein inhibitor of cysteine proteases alters viral protein cleavages in infected human cells. Biochem Biophys Res Commun 1985; 127: 1072–6
- Abrahamson M, Salvesen G, Barrett A J, Grubb A. Isolation of six cysteine proteinase inhibitors from human urine. Their physicochemical and enzyme kinetic properties and concentrations in biological fluids. J Biol Chem 1986; 261: 11282–9
- Barrett A J, Fritz H, Grubb A, Isemura S, Järvinen M, Katunuma N, Machleidt W, Müller-Esterl W, Sasaki M, Turk V. Nomenclature and classification of the proteins homologous with the cysteine-proteinase inhibitor chicken cystatin. Biochem J 1986; 236: 312
- Bieth J G. Patophysiological interpretation of kinetic constants of protease inhibitors. Bull Eur Physiopathol Respir 1980; 16(suppl)183–95
- Müller-Esterl W, Iwanaga S, Nakanishi S. Kininog-ens revisited. Trends Biochem Sci 1986; 11: 336–9
- Machleidt W, Borchart U, Fritz H, Brzin J, Ritonja A, Turk V. Protein inhibitors of cysteine proteinases. II. Primary structure of stefin, a cytosolic protein inhibitor of cysteine proteinases from human polymorphonuclear granulocytes. Hoppe-Seyler's Z Physiol Chem 1983; 364: 1481–6
- Ritonja A, Machleidt W, Barrett A J. Amino acid sequence of the intracellular cysteine proteinase inhibitor cystatin B from human liver. Biochem Biophys Res Commun 1985; 131: 1187–92
- Grubb A, Löfberg H. Human γ-trace, a basic mi-croprotein: amino acid sequence and presence in the adenohypophysis. Proc Natl Acad Sci USA 1982; 79: 3024–7
- Isemura S, Saitoh E, Sanada K. Isolation and ami-no-acid sequence of SAP-1, an acidic protein of human whole saliva, and sequence homology with human γ-trace. J Biochem 1984; 96: 489–98
- Ohkubo I, Kurachi K, Takasawa T, Shiokawa H, Sasaki M. Isolation of a human cDNA for α2-thiol proteinase inhibitor and its identity with low molecular weight kininogen. Biochemistry 1984; 23: 5691–7
- Salvesen G, Parkes C, Abrahamson M, Grubb A, Barrett A J. Human low molecular weight kininogen contains three copies of a cystatin sequence that are divergent in structure and in inhibitory activity for cysteine proteinases. Biochem J 1986; 234: 429–34
- Sasaki M, Taniguchi K, Suzuki K. Human plasma a1- and a2-thiol proteinase inhibitors strongly inhibit calcium-activated neutral proteinase from muscle. Biochem Biophys Res Commun 1983; 110: 256–61
- Anastasi A, Brown M A, Kembhavi A A, Nicklin M JH, Sayers C A, Sunter D C, Barrett A J. Cystatin, a protein inhibitor of cysteine proteinases. Improved purification from egg white, characterization, and detection in chicken serum. Biochem J 1983; 211: 129–38
- Abrahamson M, Ritonja A, Brown M A, Grubb A, Machleidt W, Barrett A J. Identification of the probable inhibitory reactive sites of the cysteine proteinase inhibitors human cystatin C and chicken cystatin. J Biol Chem 1987; 262: 9688–94
- Schechter I, Berger A. On the size of the active site in proteases. I. Papain. Biochem Biophys Res Com-mun 1967; 27: 157–62
- Laskowski M, Jr, Kato J. Protein inhibitors of proteinases. Annu Rev Biochem 1980; 49: 593–626
- Teno N, Tsuboi S, Itoh N, Okamoto H, Okada Y. Significant effects of Z-Gln-Val-Val-OMe, common sequences of thiol proteinase inhibitors on thiol proteinases. Biochem Biophys Res Commun 1987; 143: 749–52
- Green G DJ, Shaw E. Peptidyl diazomethylketones are specific inactivators of thiol proteinases. J Biol Chem 1981; 256: 1923–8
- Abrahamson M, Olafsson I, Trojnar J, Grubb A. Synthetic inhibitors based upon the sequence of the substrate-like region of human cystatin C, (In preparation)
- Björck L, Åkesson P, Bohus M, Trojnar J, Abraham-Son M, Olafsson I, Grubb A. Bacterial growth inhibited by a synthetic peptide based upon the structure of a human proteinase inhibitor, (Submitted)
- Abrahamson M, Grubb A, Olafsson I, Lundwall Å. Molecular cloning and sequence analysis of cDNA coding for the precursor of the human cysteine proteinase inhibitor cystatin C. FEBS Lett 1987; 216: 229–33
- Abrahamson M, Olafsson I, Palsdottir A, Grubb A, Lundwall Å. The structure of the human cystatin C gene, (In preparation)
- Abrahamson M, Islam Q, Szpirer J, Szpirer C, Le-Wan G. Human cystatin C gene (CST3) is located on chromosome 20, (Submitted)
- Gudmundsson G, Hallgrimsson J, Jonasson T A, Bjarnason O. Hereditary cerebral hemorrhage with amyloidosis. Brain 1972; 95: 387–404
- Cohen D H, Feiner H, Jensson O, Frangione B. Amyloid fibril in hereditary cerebral hemorrhage with amyloidosis (HCHWA) is related to the gas-troentero-pancreatic neuroendocrine protein γ-trace. J Exp Med 1983; 158: 623–8
- Grubb A, Jensson O, Gudmundsson G, Arnason A, Lofberg H, Malm J. Abnormal metabolism of γ-trace alkaline microprotein: the basic defect in hereditary cerebral hemorrhage with amyloidosis. N Engl J Med 1984; 311: 1547–9
- Ghiso J, Jensson O, Frangione B. Amyloid fibrils in hereditary cerebral hemorrhage with amyloidosis of Icelandic type is a variant of γ-trace basic protein (cystatin C). Proc Natl Acad Sci USA 1986; 83: 2974–8
- Palsdottir A, Abrahamson M, Thorsteinsson L, Arnason A, Olafsson I, Grubb A, Jensson O. Mutation in cystatin C gene causes brain hemorrhage. Lancet 1988; ii: 603–4
- Abrahamson M, Dalbøge H, Olafsson I, Carlsen S, Grubb A. Efficient production of native, biologically active human cystatin C by Escherichia coli. FEBS Lett 1988; 236: 14–18
- Dalbøge H, Jensen E B, Tøttrup H, Grubb A, Abrahamson M, Olafsson I, Carlsen S. High level expression of active human cystatin C in E. coli, (Submitted)
- Grubb A. Safer proteinase treatment of sciatica: A biochemical preview of chymopapain inhibitors. Acta Orthop Scand 1988; 59: 63–5
- Buttle D, Abrahamson M, Barrett A J. The biochemistry of the action of chymopapain in relief of sciatica. Spine 1986; 11: 688–94
- Dyck P. Paraplegia following chemonucleolysis: A case report and discussion of neurotoxicity. Spine 1985; 10: 359–62
- Davis R J, North R B, Campell J N, Suss R A. Multiple cerebral hemorrhages following chymopapain chemonucleolysis. J Neurosurg 1984; 61: 169–71
- Ishiura S, Nonaka I, Sugita H. Calcium-activated neutral protease: Its degradative role in muscle cells. Muscular Dystrophy, S Ebashi. University of Tokyo Press, Tokyo 1980; 265–82