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Volumn 579, Issue 5, 2005, Pages 1285-1290

Recombinant human procathepsin S is capable of autocatalytic processing at neutral pH in the presence of glycosaminoglycans

Author keywords

Autocatalytic activation; Cathepsin; Glycosaminoglycan; Ionic strength; Lysosomal cysteine protease; Processing

Indexed keywords

CATHEPSIN S; CHONDROITIN 4 SULFATE; CHONDROITIN SULFATE; DERMATAN SULFATE; DEXTRAN SULFATE; ENZYME PRECURSOR; GLYCOSAMINOGLYCAN; POLYSACCHARIDE; RECOMBINANT ENZYME;

EID: 13844276525     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2004.12.093     Document Type: Article
Times cited : (98)

References (43)
  • 1
    • 0034615570 scopus 로고    scopus 로고
    • Lysosomal cysteine proteases: More than scavengers
    • B. Turk, D. Turk, and V. Turk Lysosomal cysteine proteases: more than scavengers Biochim. Biophys. Acta 1477 2000 98 111
    • (2000) Biochim. Biophys. Acta , vol.1477 , pp. 98-111
    • Turk, B.1    Turk, D.2    Turk, V.3
  • 2
    • 0035801514 scopus 로고    scopus 로고
    • Lysosomal cysteine proteases: Facts and opportunities
    • V. Turk, B. Turk, and D. Turk Lysosomal cysteine proteases: facts and opportunities EMBO J. 2001 20 33
    • (2001) EMBO J. , pp. 20-33
    • Turk, V.1    Turk, B.2    Turk, D.3
  • 3
    • 0035986219 scopus 로고    scopus 로고
    • Regulating cysteine protease activity: Essential role of protease inhibitors as guardians and regulators
    • B. Turk, D. Turk, and G.S. Salvesen Regulating cysteine protease activity: essential role of protease inhibitors as guardians and regulators Curr. Pharm. Des. 8 2002 1623 1637
    • (2002) Curr. Pharm. Des. , vol.8 , pp. 1623-1637
    • Turk, B.1    Turk, D.2    Salvesen, G.S.3
  • 4
    • 0033966413 scopus 로고    scopus 로고
    • Cathepsins and compartmentalization in antigen presentation
    • R.J. Riese, and H.A. Chapman Cathepsins and compartmentalization in antigen presentation Curr. Opin. Immunol. 12 2000 107 113
    • (2000) Curr. Opin. Immunol. , vol.12 , pp. 107-113
    • Riese, R.J.1    Chapman, H.A.2
  • 5
    • 0037805704 scopus 로고    scopus 로고
    • Lysosomal cysteine proteases regulate antigen presentation
    • K. Honey, and A.Y. Rudensky Lysosomal cysteine proteases regulate antigen presentation Nat. Rev. Immunol. 3 2003 472 482
    • (2003) Nat. Rev. Immunol. , vol.3 , pp. 472-482
    • Honey, K.1    Rudensky, A.Y.2
  • 12
    • 0030970119 scopus 로고    scopus 로고
    • Emerging roles for cysteine proteases in human biology
    • H.A. Chapman, R.J. Riese, and G.P. Shi Emerging roles for cysteine proteases in human biology Annu. Rev. Physiol. 59 1997 63 88
    • (1997) Annu. Rev. Physiol. , vol.59 , pp. 63-88
    • Chapman, H.A.1    Riese, R.J.2    Shi, G.P.3
  • 13
    • 0028927279 scopus 로고
    • The lysosomal cysteine protease, cathepsin S, is increased in Alzheimer's disease and Down syndrome brain. An immunocytochemical study
    • C.A. Lemere, J.S. Munger, G.P. Shi, L. Natkin, C. Haass, H.A. Chapman, and D.J. Selkoe The lysosomal cysteine protease, cathepsin S, is increased in Alzheimer's disease and Down syndrome brain. An immunocytochemical study Am. J. Pathol. 146 1995 848 860
    • (1995) Am. J. Pathol. , vol.146 , pp. 848-860
    • Lemere, C.A.1    Munger, J.S.2    Shi, G.P.3    Natkin, L.4    Haass, C.5    Chapman, H.A.6    Selkoe, D.J.7
  • 14
    • 0035914268 scopus 로고    scopus 로고
    • Cathepsin S in tumours, regional lymph nodes and sera of patients with lung cancer: Relation to prognosis
    • J. Kos, A. Sekirnik, G. Kopitar, N. Cimerman, K. Kayser, A. Stremmer, W. Fiehn, and B. Werle Cathepsin S in tumours, regional lymph nodes and sera of patients with lung cancer: relation to prognosis Br. J. Cancer 85 2001 1193 1200
    • (2001) Br. J. Cancer , vol.85 , pp. 1193-1200
    • Kos, J.1    Sekirnik, A.2    Kopitar, G.3    Cimerman, N.4    Kayser, K.5    Stremmer, A.6    Fiehn, W.7    Werle, B.8
  • 16
    • 0033848068 scopus 로고    scopus 로고
    • Identification of the increased expression of monocyte chemoattractant protein-1, cathepsin S, UPIX-1, and other genes in dystrophin-deficient mouse muscles by suppression subtractive hybridization
    • J. Fang, G.P. Shi, and P.L. Vaghy Identification of the increased expression of monocyte chemoattractant protein-1, cathepsin S, UPIX-1, and other genes in dystrophin-deficient mouse muscles by suppression subtractive hybridization J. Cell. Biochem. 79 2000 164 172
    • (2000) J. Cell. Biochem. , vol.79 , pp. 164-172
    • Fang, J.1    Shi, G.P.2    Vaghy, P.L.3
  • 18
    • 0028068405 scopus 로고
    • Multi-step processing of procathepsin L in vitro
    • K. Ishidoh, and E. Kominami Multi-step processing of procathepsin L in vitro FEBS Lett. 352 1994 281 284
    • (1994) FEBS Lett. , vol.352 , pp. 281-284
    • Ishidoh, K.1    Kominami, E.2
  • 19
    • 0029935616 scopus 로고    scopus 로고
    • Folding and activation of human procathepsin S from inclusion bodies produced in Escherichia coli
    • G. Kopitar, M. Dolinar, B. Štrukelj, J. Pungerčar, and V. Turk Folding and activation of human procathepsin S from inclusion bodies produced in Escherichia coli Eur. J. Biochem. 236 1996 558 562
    • (1996) Eur. J. Biochem. , vol.236 , pp. 558-562
    • Kopitar, G.1    Dolinar, M.2    Štrukelj, B.3    Pungerčar, J.4    Turk, V.5
  • 20
    • 0032859935 scopus 로고    scopus 로고
    • Autocatalytic processing of recombinant human procathepsin B is a bimolecular process
    • J. Rozman, J. Stojan, R. Kuhelj, V. Turk, and B. Turk Autocatalytic processing of recombinant human procathepsin B is a bimolecular process FEBS Lett. 459 1999 358 362
    • (1999) FEBS Lett. , vol.459 , pp. 358-362
    • Rozman, J.1    Stojan, J.2    Kuhelj, R.3    Turk, V.4    Turk, B.5
  • 21
    • 0028871804 scopus 로고
    • How to measure and predict the molar absorption coefficient of a protein
    • C.N. Pace, F. Vajdos, L. Fee, G. Grimsley, and T. Gray How to measure and predict the molar absorption coefficient of a protein Protein Sci. 4 1995 2411 2423
    • (1995) Protein Sci. , vol.4 , pp. 2411-2423
    • Pace, C.N.1    Vajdos, F.2    Fee, L.3    Grimsley, G.4    Gray, T.5
  • 23
    • 0345254939 scopus 로고    scopus 로고
    • Recombinant human cathepsin H lacking the mini chain is an endopeptidase
    • O. Vasiljeva, M. Dolinar, V. Turk, and B. Turk Recombinant human cathepsin H lacking the mini chain is an endopeptidase Biochemistry 42 2003 13522 13528
    • (2003) Biochemistry , vol.42 , pp. 13522-13528
    • Vasiljeva, O.1    Dolinar, M.2    Turk, V.3    Turk, B.4
  • 24
    • 0032438791 scopus 로고    scopus 로고
    • The influence of Ala205 on the specificity of cathepsin L produced by dextran sulfate assisted activation of the recombinant proenzyme
    • D. Barlič-Maganja, M. Dolinar, and V. Turk The influence of Ala205 on the specificity of cathepsin L produced by dextran sulfate assisted activation of the recombinant proenzyme Biol. Chem. 379 1998 1449 1452
    • (1998) Biol. Chem. , vol.379 , pp. 1449-1452
    • Barlič-Maganja, D.1    Dolinar, M.2    Turk, V.3
  • 25
    • 0035896612 scopus 로고    scopus 로고
    • Identification of internal autoproteolytic cleavage sites within the prosegments of recombinant procathepsin B and procathepsin S. Contribution of a plausible unimolecular autoproteolytic event for the processing of zymogens belonging to the papain family
    • O. Quraishi, and A.C. Storer Identification of internal autoproteolytic cleavage sites within the prosegments of recombinant procathepsin B and procathepsin S. Contribution of a plausible unimolecular autoproteolytic event for the processing of zymogens belonging to the papain family J. Biol. Chem. 276 2001 8118 8124
    • (2001) J. Biol. Chem. , vol.276 , pp. 8118-8124
    • Quraishi, O.1    Storer, A.C.2
  • 28
    • 0026630108 scopus 로고
    • Molecular cloning and expression of human alveolar macrophage cathepsin S, an elastinolytic cysteine protease
    • G.P. Shi, J.S. Munger, J.P. Meara, D.H. Rich, and H.A. Chapman Molecular cloning and expression of human alveolar macrophage cathepsin S, an elastinolytic cysteine protease J. Biol. Chem. 267 1992 7258 7262
    • (1992) J. Biol. Chem. , vol.267 , pp. 7258-7262
    • Shi, G.P.1    Munger, J.S.2    Meara, J.P.3    Rich, D.H.4    Chapman, H.A.5
  • 29
    • 0026770758 scopus 로고
    • Phylogenetic conservation of cysteine proteinases. Cloning and expression of a cDNA coding for human cathepsin S
    • B. Wiederanders, D. Brömme, H. Kirschke, K. von Figura, B. Schmidt, and C. Peters Phylogenetic conservation of cysteine proteinases. Cloning and expression of a cDNA coding for human cathepsin S J. Biol. Chem. 267 1992 13708 13713
    • (1992) J. Biol. Chem. , vol.267 , pp. 13708-13713
    • Wiederanders, B.1    Brömme, D.2    Kirschke, H.3    Von Figura, K.4    Schmidt, B.5    Peters, C.6
  • 30
    • 0025876252 scopus 로고
    • The complete amino acid sequence of bovine cathepsin S and a partial sequence of bovine cathepsin L
    • A. Ritonja, A. Čolić, I. Dolenc, T. Ogrinc, M. Podobnik, and V. Turk The complete amino acid sequence of bovine cathepsin S and a partial sequence of bovine cathepsin L FEBS Lett. 283 1991 329 331
    • (1991) FEBS Lett. , vol.283 , pp. 329-331
    • Ritonja, A.1    Čolić, A.2    Dolenc, I.3    Ogrinc, T.4    Podobnik, M.5    Turk, V.6
  • 31
    • 0345862190 scopus 로고    scopus 로고
    • Production and activation of recombinant papain-like cysteine proteases
    • D. Brömme, F.S. Nallaseth, and B. Turk Production and activation of recombinant papain-like cysteine proteases Methods 32 2004 199 206
    • (2004) Methods , vol.32 , pp. 199-206
    • Brömme, D.1    Nallaseth, F.S.2    Turk, B.3
  • 34
    • 0025875756 scopus 로고
    • Proteoglycans: Structures and interactions
    • L. Kjellen, and U. Lindahl Proteoglycans: structures and interactions Annu. Rev. Biochem. 60 1991 443 475
    • (1991) Annu. Rev. Biochem. , vol.60 , pp. 443-475
    • Kjellen, L.1    Lindahl, U.2
  • 35
    • 0038486742 scopus 로고    scopus 로고
    • Procongopain from Trypanosoma congolense is processed at basic pH: An unusual feature among cathepsin L-like cysteine proteases
    • C. Serveau, A. Boulange, F. Lecaille, F. Gauthier, E. Authie, and G. Lalmanach Procongopain from Trypanosoma congolense is processed at basic pH: an unusual feature among cathepsin L-like cysteine proteases Biol. Chem. 384 2003 921 927
    • (2003) Biol. Chem. , vol.384 , pp. 921-927
    • Serveau, C.1    Boulange, A.2    Lecaille, F.3    Gauthier, F.4    Authie, E.5    Lalmanach, G.6
  • 36
    • 0027068057 scopus 로고
    • Potent slow-binding inhibition of cathepsin B by its propeptide
    • T. Fox, E. de Miguel, J.S. Mort, and A.C. Storer Potent slow-binding inhibition of cathepsin B by its propeptide Biochemistry 31 1992 12571 12576
    • (1992) Biochemistry , vol.31 , pp. 12571-12576
    • Fox, T.1    De Miguel, E.2    Mort, J.S.3    Storer, A.C.4
  • 37
    • 0030038759 scopus 로고    scopus 로고
    • Potency and selectivity of the cathepsin L propeptide as an inhibitor of cysteine proteases
    • E. Carmona, E. Dufour, C. Plouffe, S. Takebe, P. Mason, J.S. Mort, and R. Menard Potency and selectivity of the cathepsin L propeptide as an inhibitor of cysteine proteases Biochemistry 35 1996 8149 8157
    • (1996) Biochemistry , vol.35 , pp. 8149-8157
    • Carmona, E.1    Dufour, E.2    Plouffe, C.3    Takebe, S.4    Mason, P.5    Mort, J.S.6    Menard, R.7
  • 38
    • 0024814219 scopus 로고
    • Cathepsin S from bovine spleen. Purification, distribution, intracellular localization and action on proteins
    • H. Kirschke, B. Wiederanders, D. Bromme, and A. Rinne Cathepsin S from bovine spleen. Purification, distribution, intracellular localization and action on proteins Biochem. J. 264 1989 467 473
    • (1989) Biochem. J. , vol.264 , pp. 467-473
    • Kirschke, H.1    Wiederanders, B.2    Bromme, D.3    Rinne, A.4
  • 39
    • 0027050951 scopus 로고
    • The specificity and elastinolytic activities of bovine cathepsins S and H
    • X.Q. Xin, B. Gunesekera, and R.W. Mason The specificity and elastinolytic activities of bovine cathepsins S and H Arch. Biochem. Biophys. 299 1992 334 339
    • (1992) Arch. Biochem. Biophys. , vol.299 , pp. 334-339
    • Xin, X.Q.1    Gunesekera, B.2    Mason, R.W.3
  • 40
    • 4344670363 scopus 로고    scopus 로고
    • Cathepsin V, a novel and potent elastolytic activity expressed in activated macrophages
    • Y. Yasuda, Z. Li, D. Greenbaum, M. Bogyo, E. Weber, and D. Bromme Cathepsin V, a novel and potent elastolytic activity expressed in activated macrophages J. Biol. Chem. 279 2004 36761 36770
    • (2004) J. Biol. Chem. , vol.279 , pp. 36761-36770
    • Yasuda, Y.1    Li, Z.2    Greenbaum, D.3    Bogyo, M.4    Weber, E.5    Bromme, D.6
  • 41
    • 0035852855 scopus 로고    scopus 로고
    • Human recombinant pro-dipeptidyl peptidase I (cathepsin C) can be activated by cathepsins L and S but not by autocatalytic processing
    • S.W. Dahl, T. Halkier, C. Lauritzen, I. Dolenc, J. Pedersen, V. Turk, and B. Turk Human recombinant pro-dipeptidyl peptidase I (cathepsin C) can be activated by cathepsins L and S but not by autocatalytic processing Biochemistry 40 2001 1671 1678
    • (2001) Biochemistry , vol.40 , pp. 1671-1678
    • Dahl, S.W.1    Halkier, T.2    Lauritzen, C.3    Dolenc, I.4    Pedersen, J.5    Turk, V.6    Turk, B.7
  • 43
    • 1542495341 scopus 로고    scopus 로고
    • Cathepsin B and its roles in cancer progression
    • I. Podgorski, and B.F. Sloane Cathepsin B and its roles in cancer progression Biochem. Soc. Symp. 70 2003 263 276
    • (2003) Biochem. Soc. Symp. , vol.70 , pp. 263-276
    • Podgorski, I.1    Sloane, B.F.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.