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Volumn 385, Issue 6, 2004, Pages 505-509

Human cathepsin F: Expression in baculovirus system, characterization and inhibition by protein inhibitors

Author keywords

Cathepsin; Cystatin; Cysteine protease; Thyropin

Indexed keywords

CATHEPSIN F; CYSTATIN; CYSTATIN C; KININOGEN; PEPSIN A; PROTEIN INHIBITOR; PROTEINASE; STEFIN A;

EID: 3242745349     PISSN: 14316730     EISSN: None     Source Type: Journal    
DOI: 10.1515/BC.2004.059     Document Type: Article
Times cited : (12)

References (33)
  • 1
    • 0029924123 scopus 로고    scopus 로고
    • Major histocompatibility complex class II associated p41 invariant chain fragment is a strong inhibitor of lysosomal cathepsin L
    • Bevec, T., Stoka, V., Pungerčič, G., Dolenc, I., and Turk, V. (1996). Major histocompatibility complex class II associated p41 invariant chain fragment is a strong inhibitor of lysosomal cathepsin L. J. Exp. Med. 183, 1331-1338.
    • (1996) J. Exp. Med. , vol.183 , pp. 1331-1338
    • Bevec, T.1    Stoka, V.2    Pungerčič, G.3    Dolenc, I.4    Turk, V.5
  • 2
    • 0141815490 scopus 로고    scopus 로고
    • Human proteoglycan testican-1 inhibits the lysosomal cysteine protease cathepsin L
    • Bocock, J.P., Edgell, C.J., Marr, H.S., and Erickson, A.H. (2003). Human proteoglycan testican-1 inhibits the lysosomal cysteine protease cathepsin L. Eur. J. Biochem. 270, 4008-4015.
    • (2003) Eur. J. Biochem. , vol.270 , pp. 4008-4015
    • Bocock, J.P.1    Edgell, C.J.2    Marr, H.S.3    Erickson, A.H.4
  • 4
    • 0029379775 scopus 로고
    • The baculovirus cysteine protease has a cathepsin B-like S2-subsite specificity
    • Brömme, D., and Okamoto, K. (1995). The baculovirus cysteine protease has a cathepsin B-like S2-subsite specificity. Biol. Chem. 376, 611-615.
    • (1995) Biol. Chem. , vol.376 , pp. 611-615
    • Brömme, D.1    Okamoto, K.2
  • 5
    • 0345862190 scopus 로고    scopus 로고
    • Production and activation of recombinant papain-like cysteine proteases
    • Brömme, D., Nallaseth, F.S., and Turk, B. (2004). Production and activation of recombinant papain-like cysteine proteases. Methods 32, 199-206.
    • (2004) Methods , vol.32 , pp. 199-206
    • Brömme, D.1    Nallaseth, F.S.2    Turk, B.3
  • 6
    • 0036669602 scopus 로고    scopus 로고
    • Production of recombinant proteins in fermenter cultures of the yeast Pichia pastoris
    • Cereghino, G.P.L., Cereghino, J.L., Ilgen, C., and Cregg, J.M. (2002). Production of recombinant proteins in fermenter cultures of the yeast Pichia pastoris. Curr. Opin. Biotechnol. 13, 329-332.
    • (2002) Curr. Opin. Biotechnol. , vol.13 , pp. 329-332
    • Cereghino, G.P.L.1    Cereghino, J.L.2    Ilgen, C.3    Cregg, J.M.4
  • 7
    • 0028874448 scopus 로고
    • Advances in the use of recombinant baculoviruses for the expression of heterologous proteins
    • Davies, A.H. (1995). Advances in the use of recombinant baculoviruses for the expression of heterologous proteins. Curr. Opin. Biotechnol. 6, 543-547.
    • (1995) Curr. Opin. Biotechnol. , vol.6 , pp. 543-547
    • Davies, A.H.1
  • 8
    • 0018787723 scopus 로고
    • Evaluation of methods for estimating the dissociation constant of tight binding inhibitors
    • Greco W.R., and Hakala, M.T. (1979). Evaluation of methods for estimating the dissociation constant of tight binding inhibitors. J. Biol. Chem. 254, 12104-12109.
    • (1979) J. Biol. Chem. , vol.254 , pp. 12104-12109
    • Greco, W.R.1    Hakala, M.T.2
  • 10
    • 0039547996 scopus 로고    scopus 로고
    • Crystal structure of MHC class II-associated p41 Ii fragment bound to cathepsin L reveals the structural basis for differentiation between cathepsins L and S
    • Gunčar, G., Pungerčič, G., Klemenčič, I., Turk, V., and Turk, D. (1999). Crystal structure of MHC class II-associated p41 Ii fragment bound to cathepsin L reveals the structural basis for differentiation between cathepsins L and S. EMBO J. 18, 793-803.
    • (1999) EMBO J. , vol.18 , pp. 793-803
    • Gunčar, G.1    Pungerčič, G.2    Klemenčič, I.3    Turk, V.4    Turk, D.5
  • 11
    • 0036898570 scopus 로고    scopus 로고
    • Expression, purification, crystallization and preliminary X-ray diffraction studies of human cathepsin F complexed with an irreversible vinyl sulfone inhibitor
    • Ho, J.D., Meltser, Y., Buggy, J.J., Palmer, J.T., Elrod, K.C., Chan, H., Mortara, K.D., and Somoza, J.R. (2002). Expression, purification, crystallization and preliminary X-ray diffraction studies of human cathepsin F complexed with an irreversible vinyl sulfone inhibitor. Acta Cryst. D58, 2187-2190.
    • (2002) Acta Cryst. , vol.D58 , pp. 2187-2190
    • Ho, J.D.1    Meltser, Y.2    Buggy, J.J.3    Palmer, J.T.4    Elrod, K.C.5    Chan, H.6    Mortara, K.D.7    Somoza, J.R.8
  • 12
    • 0040020321 scopus 로고    scopus 로고
    • Equistatin, a new inhibitor of cysteine proteinasesfrom Actinia equina, is structuraly related to thyroglobulin type-1 domain
    • Lenarčič, B., Ritonja, A., Štrukelj, B., Turk, B., and Turk, V. (1997). Equistatin, a new inhibitor of cysteine proteinasesfrom Actinia equina, is structuraly related to thyroglobulin type-1 domain. J. Biol. Chem. 272, 13899-13903.
    • (1997) J. Biol. Chem. , vol.272 , pp. 13899-13903
    • Lenarčič, B.1    Ritonja, A.2    Štrukelj, B.3    Turk, B.4    Turk, V.5
  • 13
    • 0038835365 scopus 로고    scopus 로고
    • Thyropins-new structuraly related proteinase inhibitors
    • Lenarčič, B., and Bevec, T. (1998). Thyropins-new structuraly related proteinase inhibitors. Biol. Chem. 379, 105-111.
    • (1998) Biol. Chem. , vol.379 , pp. 105-111
    • Lenarčič, B.1    Bevec, T.2
  • 14
    • 0030018121 scopus 로고    scopus 로고
    • Inhibition of bovine cathepsins L and S by stefins and cystatins
    • Leonardi, A., Turk, B., and Turk, V. (1996). Inhibition of bovine cathepsins L and S by stefins and cystatins. Biol. Chem. 377, 319-321.
    • (1996) Biol. Chem. , vol.377 , pp. 319-321
    • Leonardi, A.1    Turk, B.2    Turk, V.3
  • 15
    • 0026570448 scopus 로고
    • Interaction of human cystatin C with the cysteine proteinases papain and actinidin
    • Lindahl, P., Abrahamson, M., and Björk, I. (1992). Interaction of human cystatin C with the cysteine proteinases papain and actinidin. Biochem. J. 281, 49-55.
    • (1992) Biochem. J. , vol.281 , pp. 49-55
    • Lindahl, P.1    Abrahamson, M.2    Björk, I.3
  • 16
    • 0001396685 scopus 로고
    • The slow binding and slow, tight binding inhibition of enzyme catalysed reactions
    • Morrison, J.F. (1982). The slow binding and slow, tight binding inhibition of enzyme catalysed reactions. Trends. Biochem. Sci. 7, 192-105.
    • (1982) Trends. Biochem. Sci. , vol.7 , pp. 105-192
    • Morrison, J.F.1
  • 17
    • 12044253640 scopus 로고
    • The refined 2.15 Å X-ray crystal structure of humen liver cathepsin B: The structural bases for its specificity
    • Musil, D., Zucic, D., Turk, D., Engh, R.A., Mayr, I., Huber, R., Popovic, T., Turk, V., Towatari, T., and Katunuma, N. (1990). The refined 2.15 Å X-ray crystal structure of humen liver cathepsin B: the structural bases for its specificity. EMBO J. 10, 2321-2330.
    • (1990) EMBO J. , vol.10 , pp. 2321-2330
    • Musil, D.1    Zucic, D.2    Turk, D.3    Engh, R.A.4    Mayr, I.5    Huber, R.6    Popovic, T.7    Turk, V.8    Towatari, T.9    Katunuma, N.10
  • 18
    • 0039642231 scopus 로고    scopus 로고
    • Full-length cDNA of human cathepsin F predicts the presence of a cystatin domain at the N-terminus of the cysteine protease zymogen
    • Nägler, D.K., Sulea, T., and Ménard, R. (1999). Full-length cDNA of human cathepsin F predicts the presence of a cystatin domain at the N-terminus of the cysteine protease zymogen. Biochem. Biophys. Res. Commun. 257, 313-318.
    • (1999) Biochem. Biophys. Res. Commun. , vol.257 , pp. 313-318
    • Nägler, D.K.1    Sulea, T.2    Ménard, R.3
  • 19
    • 0029101752 scopus 로고
    • Characterisation by spectroscopic, kinetic and equilibrium methods of the interaction between recombinant human cystatin A (stefin A) and cysteine proteinases
    • Pol, E., Olsson, S.L., Estrada, S., Prasthofer, T.W., and Björk, I. (1995). Characterisation by spectroscopic, kinetic and equilibrium methods of the interaction between recombinant human cystatin A (stefin A) and cysteine proteinases. Biochem. J. 311, 275-282.
    • (1995) Biochem. J. , vol.311 , pp. 275-282
    • Pol, E.1    Olsson, S.L.2    Estrada, S.3    Prasthofer, T.W.4    Björk, I.5
  • 20
    • 2942718876 scopus 로고    scopus 로고
    • Comprehensive search for cysteine cathepsins in the human genome
    • Rossi, A., Deveraux, Q., Turk, B., and Sali, A. (2004). Comprehensive search for cysteine cathepsins in the human genome. Biol. Chem. 385, 363-372.
    • (2004) Biol. Chem. , vol.385 , pp. 363-372
    • Rossi, A.1    Deveraux, Q.2    Turk, B.3    Sali, A.4
  • 21
    • 0022555509 scopus 로고
    • Human low-Mr kininogen contains three copies of cystatin sequence that are divergent in structure and in inhibitory activity for cysteine proteinases
    • Salvesen, G., Parkes, C., Abrahamson, M., Grubb, A., and Barrett, A.J. (1986). Human low-Mr kininogen contains three copies of cystatin sequence that are divergent in structure and in inhibitory activity for cysteine proteinases. Biochem. J. 234, 429-434.
    • (1986) Biochem. J. , vol.234 , pp. 429-434
    • Salvesen, G.1    Parkes, C.2    Abrahamson, M.3    Grubb, A.4    Barrett, A.J.5
  • 22
    • 0033553419 scopus 로고    scopus 로고
    • Molecular cloning and structural and functional characterization of human cathepsin F, a new cysteine proteinase of the papain family with a long propeptide domain
    • Santamaria, I., Velasco, G., Pendas, A.M., Paz, A., and Lopez-Otin, C. (1999). Molecular cloning and structural and functional characterization of human cathepsin F, a new cysteine proteinase of the papain family with a long propeptide domain. J. Biol. Chem. 274, 13800-13809.
    • (1999) J. Biol. Chem. , vol.274 , pp. 13800-13809
    • Santamaria, I.1    Velasco, G.2    Pendas, A.M.3    Paz, A.4    Lopez-Otin, C.5
  • 23
    • 0034599498 scopus 로고    scopus 로고
    • Role for cathepsin F in invariant chain processing and major histocompatibility complex class II peptide loading by macrophages
    • Shi, G.P., Bryant, R.A.R., Riese, R., Verhelst, S., Driessen, C., Li, Z., Brömme, D., Ploegh, H.L., and Chapman, H.A. (2000). Role for cathepsin F in invariant chain processing and major histocompatibility complex class II peptide loading by macrophages. J. Exp. Med. 191, 1177-1185.
    • (2000) J. Exp. Med. , vol.191 , pp. 1177-1185
    • Shi, G.P.1    Bryant, R.A.R.2    Riese, R.3    Verhelst, S.4    Driessen, C.5    Li, Z.6    Brömme, D.7    Ploegh, H.L.8    Chapman, H.A.9
  • 24
    • 0036382928 scopus 로고    scopus 로고
    • The crystal structure of human cathepsin F and its implications for the development of novel immunomodulators
    • Somoza, J.R., Palmer, J.T., and Ho, J.D. (2002). The crystal structure of human cathepsin F and its implications for the development of novel immunomodulators. J. Mol. Biol. 322, 559-568.
    • (2002) J. Mol. Biol. , vol.322 , pp. 559-568
    • Somoza, J.R.1    Palmer, J.T.2    Ho, J.D.3
  • 25
    • 0345161636 scopus 로고    scopus 로고
    • Cathepsin S and cruzipain are inhibited by equistatin from Actinia equina
    • Stoka, V., Lenarčič, B., Cazzulo, J.J., and Turk, V. (1999). Cathepsin S and cruzipain are inhibited by equistatin from Actinia equina. Biol. Chem. 380, 589-592.
    • (1999) Biol. Chem. , vol.380 , pp. 589-592
    • Stoka, V.1    Lenarčič, B.2    Cazzulo, J.J.3    Turk, V.4
  • 27
    • 0028936570 scopus 로고
    • Identification of bovine stefin A, a novel protein inhibitor of cysteine proteinases
    • Turk, B., Ritonja, A., Björk, I., Stoka, V., Dolenc, I., and Turk, V. (1995). Identification of bovine stefin A, a novel protein inhibitor of cysteine proteinases. FEBS Lett. 360, 101-105.
    • (1995) FEBS Lett. , vol.360 , pp. 101-105
    • Turk, B.1    Ritonja, A.2    Björk, I.3    Stoka, V.4    Dolenc, I.5    Turk, V.6
  • 28
    • 0030918546 scopus 로고    scopus 로고
    • Structural and functional aspects of papain-like cysteine proteinases and their protein inhibitors
    • Turk, B., Turk, V., and Turk, D. (1997). Structural and functional aspects of papain-like cysteine proteinases and their protein inhibitors. Biol. Chem. 378, 141-150.
    • (1997) Biol. Chem. , vol.378 , pp. 141-150
    • Turk, B.1    Turk, V.2    Turk, D.3
  • 29
    • 0035986219 scopus 로고    scopus 로고
    • Regulating cysteine protease activity: Essential role of protease inhibitors as guardians and regulators
    • Turk, B., Turk, D., and Salvesen, G.S. (2002). Regulating cysteine protease activity: essential role of protease inhibitors as guardians and regulators. Curr. Pharm. Design 8, 1623-1637.
    • (2002) Curr. Pharm. Design , vol.8 , pp. 1623-1637
    • Turk, B.1    Turk, D.2    Salvesen, G.S.3
  • 30
    • 3242768155 scopus 로고    scopus 로고
    • Regulating cysteine protease activity: Essential role of protease inhibitors as guardians and regulators
    • Reviews On-line, in press
    • Turk, B., Turk, D., and Salvesen, G.S. (2004). Regulating cysteine protease activity: essential role of protease inhibitors as guardians and regulators. Med. Chem. Reviews On-line, in press.
    • (2004) Med. Chem.
    • Turk, B.1    Turk, D.2    Salvesen, G.S.3
  • 31
    • 0345254939 scopus 로고
    • Recombinant human cathepsin H lacking the minichain is an endopeptidases
    • Vasiljeva, O., Dolinar, M., Turk, V., and Turk, B. (1993). Recombinant human cathepsin H lacking the minichain is an endopeptidases. Biochemistry 42, 13522-13528.
    • (1993) Biochemistry , vol.42 , pp. 13522-13528
    • Vasiljeva, O.1    Dolinar, M.2    Turk, V.3    Turk, B.4
  • 33
    • 0030067774 scopus 로고    scopus 로고
    • A novel cysteine protease inhibitor of the egg of chum salmon, containing a cysteine rich thyroglobulin-like motif
    • Yamashita, M., and Konagaya, S. (1996). A novel cysteine protease inhibitor of the egg of chum salmon, containing a cysteine rich thyroglobulin-like motif. J. Biol. Chem. 271, 1282-1284.
    • (1996) J. Biol. Chem. , vol.271 , pp. 1282-1284
    • Yamashita, M.1    Konagaya, S.2


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