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Volumn 1800, Issue 9, 2010, Pages 937-945

Comparative study of mature and zymogen mite cysteine protease stability and pH unfolding

Author keywords

Allergen; Cysteine protease; Der p 1; Fluorescence quenching; Mechanism of activation; PH induced unfolding; Propeptide; Stability; Thermal denaturation; Zymogen

Indexed keywords

CYSTEINE PROTEINASE; DER P 1; ENZYME PRECURSOR; PAPAIN; TRYPTOPHAN; UNCLASSIFIED DRUG; ARTHROPOD PROTEIN; DERMATOPHAGOIDES PTERONYSSINUS ANTIGEN P 1; HOUSE DUST ALLERGEN;

EID: 77955282029     PISSN: 03044165     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbagen.2010.05.011     Document Type: Article
Times cited : (9)

References (49)
  • 5
    • 18944365919 scopus 로고    scopus 로고
    • The role of cathepsins in osteoporosis and arthritis: rationale for the design of new therapeutics
    • Yasuda Y., Kaleta J., Bromme D. The role of cathepsins in osteoporosis and arthritis: rationale for the design of new therapeutics. Adv. Drug Deliv. Rev. 2005, 57:973-993.
    • (2005) Adv. Drug Deliv. Rev. , vol.57 , pp. 973-993
    • Yasuda, Y.1    Kaleta, J.2    Bromme, D.3
  • 9
    • 2442610018 scopus 로고    scopus 로고
    • Structure-function relationships in class CA1 cysteine peptidase propeptides
    • Wiederanders B. Structure-function relationships in class CA1 cysteine peptidase propeptides. Acta Biochim. Pol. 2003, 50:691-713.
    • (2003) Acta Biochim. Pol. , vol.50 , pp. 691-713
    • Wiederanders, B.1
  • 10
    • 0027394245 scopus 로고
    • Two distinct gene subfamilies within the family of cysteine protease genes
    • Karrer K.M., Peiffer S.L., DiTomas M.E. Two distinct gene subfamilies within the family of cysteine protease genes. Proc. Natl. Acad. Sci. U.S.A. 1993, 90:3063-3067.
    • (1993) Proc. Natl. Acad. Sci. U.S.A. , vol.90 , pp. 3063-3067
    • Karrer, K.M.1    Peiffer, S.L.2    DiTomas, M.E.3
  • 11
    • 0030587773 scopus 로고    scopus 로고
    • The prosequence of procaricain forms an alpha-helical domain that prevents access to the substrate-binding cleft
    • Groves M.R., Taylor M.A., Scott M., Cummings N.J., Pickersgill R.W., Jenkins J.A. The prosequence of procaricain forms an alpha-helical domain that prevents access to the substrate-binding cleft. Structure 1996, 4:1193-1203.
    • (1996) Structure , vol.4 , pp. 1193-1203
    • Groves, M.R.1    Taylor, M.A.2    Scott, M.3    Cummings, N.J.4    Pickersgill, R.W.5    Jenkins, J.A.6
  • 13
    • 0031826072 scopus 로고    scopus 로고
    • Structural basis for specificity of papain-like cysteine protease proregions toward their cognate enzymes
    • Groves M.R., Coulombe R., Jenkins J., Cygler M. Structural basis for specificity of papain-like cysteine protease proregions toward their cognate enzymes. Proteins 1998, 32:504-514.
    • (1998) Proteins , vol.32 , pp. 504-514
    • Groves, M.R.1    Coulombe, R.2    Jenkins, J.3    Cygler, M.4
  • 14
    • 0028905069 scopus 로고
    • Processing of the papain precursor. The ionization state of a conserved amino acid motif within the Pro region participates in the regulation of intramolecular processing
    • Vernet T., Berti P.J., de Montigny C., Musil R., Tessier D.C., Menard R., Magny M.C., Storer A.C., Thomas D.Y. Processing of the papain precursor. The ionization state of a conserved amino acid motif within the Pro region participates in the regulation of intramolecular processing. J. Biol. Chem. 1995, 270:10838-10846.
    • (1995) J. Biol. Chem. , vol.270 , pp. 10838-10846
    • Vernet, T.1    Berti, P.J.2    de Montigny, C.3    Musil, R.4    Tessier, D.C.5    Menard, R.6    Magny, M.C.7    Storer, A.C.8    Thomas, D.Y.9
  • 15
    • 0029007093 scopus 로고
    • Pericellular mobilization of the tissue-destructive cysteine proteinases, cathepsins B, L, and S, by human monocyte-derived macrophages
    • Reddy V.Y., Zhang Q.Y., Weiss S.J. Pericellular mobilization of the tissue-destructive cysteine proteinases, cathepsins B, L, and S, by human monocyte-derived macrophages. Proc. Natl. Acad. Sci. U.S.A. 1995, 92:3849-3853.
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 3849-3853
    • Reddy, V.Y.1    Zhang, Q.Y.2    Weiss, S.J.3
  • 16
    • 0034941496 scopus 로고    scopus 로고
    • Folding incompetence of cathepsin L-like cysteine proteases may be compensated by the highly conserved, domain-building N-terminal extension of the proregion
    • Schilling K., Pietschmann S., Fehn M., Wenz I., Wiederanders B. Folding incompetence of cathepsin L-like cysteine proteases may be compensated by the highly conserved, domain-building N-terminal extension of the proregion. Biol. Chem. 2001, 382:859-865.
    • (2001) Biol. Chem. , vol.382 , pp. 859-865
    • Schilling, K.1    Pietschmann, S.2    Fehn, M.3    Wenz, I.4    Wiederanders, B.5
  • 17
    • 0036753993 scopus 로고    scopus 로고
    • Foldase function of the cathepsin S proregion is strictly based upon its domain structure
    • Pietschmann S., Fehn M., Kaulmann G., Wenz I., Wiederanders B., Schilling K. Foldase function of the cathepsin S proregion is strictly based upon its domain structure. Biol. Chem. 2002, 383:1453-1458.
    • (2002) Biol. Chem. , vol.383 , pp. 1453-1458
    • Pietschmann, S.1    Fehn, M.2    Kaulmann, G.3    Wenz, I.4    Wiederanders, B.5    Schilling, K.6
  • 18
    • 0039702904 scopus 로고    scopus 로고
    • Protease trafficking in two primitive eukaryotes is mediated by a prodomain protein motif
    • Huete-Perez J.A., Engel J.C., Brinen L.S., Mottram J.C., McKerrow J.H. Protease trafficking in two primitive eukaryotes is mediated by a prodomain protein motif. J. Biol. Chem. 1999, 274:16249-16256.
    • (1999) J. Biol. Chem. , vol.274 , pp. 16249-16256
    • Huete-Perez, J.A.1    Engel, J.C.2    Brinen, L.S.3    Mottram, J.C.4    McKerrow, J.H.5
  • 19
    • 0242452190 scopus 로고    scopus 로고
    • Autocatalytic processing of recombinant human procathepsin L. Contribution of both intermolecular and unimolecular events in the processing of procathepsin L in vitro
    • Menard R., Carmona E., Takebe S., Dufour E., Plouffe C., Mason P., Mort J.S. Autocatalytic processing of recombinant human procathepsin L. Contribution of both intermolecular and unimolecular events in the processing of procathepsin L in vitro. J. Biol. Chem. 1998, 273:4478-4484.
    • (1998) J. Biol. Chem. , vol.273 , pp. 4478-4484
    • Menard, R.1    Carmona, E.2    Takebe, S.3    Dufour, E.4    Plouffe, C.5    Mason, P.6    Mort, J.S.7
  • 24
    • 0032906630 scopus 로고    scopus 로고
    • Analysis of where and which types of proteinases participate in lysosomal proteinase processing using bafilomycin A1 and Helicobacter pylori Vac A toxin
    • Ishidoh K., Takeda-Ezaki M., Watanabe S., Sato N., Aihara M., Imagawa K., Kikuchi M., Kominami E. Analysis of where and which types of proteinases participate in lysosomal proteinase processing using bafilomycin A1 and Helicobacter pylori Vac A toxin. J. Biochem. 1999, 125:770-779.
    • (1999) J. Biochem. , vol.125 , pp. 770-779
    • Ishidoh, K.1    Takeda-Ezaki, M.2    Watanabe, S.3    Sato, N.4    Aihara, M.5    Imagawa, K.6    Kikuchi, M.7    Kominami, E.8
  • 25
    • 0036925233 scopus 로고    scopus 로고
    • Chondroitin sulfate proteoglycan is a potent enhancer in the processing of procathepsin L
    • Kihara M., Kakegawa H., Matano Y., Murata E., Tsuge H., Kido H., Katunuma N. Chondroitin sulfate proteoglycan is a potent enhancer in the processing of procathepsin L. Biol. Chem. 2002, 383:1925-1929.
    • (2002) Biol. Chem. , vol.383 , pp. 1925-1929
    • Kihara, M.1    Kakegawa, H.2    Matano, Y.3    Murata, E.4    Tsuge, H.5    Kido, H.6    Katunuma, N.7
  • 26
    • 38849159247 scopus 로고    scopus 로고
    • Biochemical properties and regulation of cathepsin K activity
    • Lecaille F., Bromme D., Lalmanach G. Biochemical properties and regulation of cathepsin K activity. Biochimie 2008, 90:208-226.
    • (2008) Biochimie , vol.90 , pp. 208-226
    • Lecaille, F.1    Bromme, D.2    Lalmanach, G.3
  • 27
    • 13844276525 scopus 로고    scopus 로고
    • Recombinant human procathepsin S is capable of autocatalytic processing at neutral pH in the presence of glycosaminoglycans
    • Vasiljeva O., Dolinar M., Pungercar J.R., Turk V., Turk B. Recombinant human procathepsin S is capable of autocatalytic processing at neutral pH in the presence of glycosaminoglycans. FEBS Lett. 2005, 579:1285-1290.
    • (2005) FEBS Lett. , vol.579 , pp. 1285-1290
    • Vasiljeva, O.1    Dolinar, M.2    Pungercar, J.R.3    Turk, V.4    Turk, B.5
  • 28
    • 36348941660 scopus 로고    scopus 로고
    • Glycosaminoglycans facilitate procathepsin B activation through disruption of propeptide-mature enzyme interactions
    • Caglic D., Pungercar J.R., Pejler G., Turk V., Turk B. Glycosaminoglycans facilitate procathepsin B activation through disruption of propeptide-mature enzyme interactions. J. Biol. Chem. 2007, 282:33076-33085.
    • (2007) J. Biol. Chem. , vol.282 , pp. 33076-33085
    • Caglic, D.1    Pungercar, J.R.2    Pejler, G.3    Turk, V.4    Turk, B.5
  • 29
    • 0032496158 scopus 로고    scopus 로고
    • PH-induced conformational transitions of the propeptide of human cathepsin L. A role for a molten globule state in zymogen activation
    • Jerala R., Zerovnik E., Kidric J., Turk V. pH-induced conformational transitions of the propeptide of human cathepsin L. A role for a molten globule state in zymogen activation. J. Biol. Chem. 1998, 273:11498-11504.
    • (1998) J. Biol. Chem. , vol.273 , pp. 11498-11504
    • Jerala, R.1    Zerovnik, E.2    Kidric, J.3    Turk, V.4
  • 31
    • 0042062304 scopus 로고    scopus 로고
    • Protein inhibitors form complexes with procathepsin L and augment cleavage of the propeptide
    • Majerle A., Jerala R. Protein inhibitors form complexes with procathepsin L and augment cleavage of the propeptide. Arch. Biochem. Biophys. 2003, 417:53-58.
    • (2003) Arch. Biochem. Biophys. , vol.417 , pp. 53-58
    • Majerle, A.1    Jerala, R.2
  • 32
    • 33751103711 scopus 로고    scopus 로고
    • The crystal structure of a Cys25→Ala mutant of human procathepsin S elucidates enzyme-prosequence interactions
    • Kaulmann G., Palm G.J., Schilling K., Hilgenfeld R., Wiederanders B. The crystal structure of a Cys25→Ala mutant of human procathepsin S elucidates enzyme-prosequence interactions. Protein Sci. 2006, 15:2619-2629.
    • (2006) Protein Sci. , vol.15 , pp. 2619-2629
    • Kaulmann, G.1    Palm, G.J.2    Schilling, K.3    Hilgenfeld, R.4    Wiederanders, B.5
  • 33
    • 0030918546 scopus 로고    scopus 로고
    • Structural and functional aspects of papain-like cysteine proteinases and their protein inhibitors
    • Turk B., Turk V., Turk D. Structural and functional aspects of papain-like cysteine proteinases and their protein inhibitors. Biol. Chem. 1997, 378:141-150.
    • (1997) Biol. Chem. , vol.378 , pp. 141-150
    • Turk, B.1    Turk, V.2    Turk, D.3
  • 34
    • 0032573356 scopus 로고    scopus 로고
    • Sequential unfolding of papain in molten globule state
    • Edwin F., Jagannadham M.V. Sequential unfolding of papain in molten globule state. Biochem. Biophys. Res. Commun. 1998, 252:654-660.
    • (1998) Biochem. Biophys. Res. Commun. , vol.252 , pp. 654-660
    • Edwin, F.1    Jagannadham, M.V.2
  • 36
    • 0036153595 scopus 로고    scopus 로고
    • Characterization of a partially folded intermediate of stem bromelain at low pH
    • Haq S.K., Rasheedi S., Khan R.H. Characterization of a partially folded intermediate of stem bromelain at low pH. Eur. J. Biochem. 2002, 269:47-52.
    • (2002) Eur. J. Biochem. , vol.269 , pp. 47-52
    • Haq, S.K.1    Rasheedi, S.2    Khan, R.H.3
  • 37
    • 37549071494 scopus 로고    scopus 로고
    • A heparin binding motif on the pro-domain of human procathepsin L mediates zymogen destabilization and activation
    • Fairhead M., Kelly S.M., van der Walle C.F. A heparin binding motif on the pro-domain of human procathepsin L mediates zymogen destabilization and activation. Biochem. Biophys. Res. Commun. 2008, 366:862-867.
    • (2008) Biochem. Biophys. Res. Commun. , vol.366 , pp. 862-867
    • Fairhead, M.1    Kelly, S.M.2    van der Walle, C.F.3
  • 39
    • 0023877882 scopus 로고
    • Sequence analysis of cDNA coding for a major house dust mite allergen, Der p 1. Homology with cysteine proteases
    • Chua K.Y., Stewart G.A., Thomas W.R., Simpson R.J., Dilworth R.J., Plozza T.M., Turner K.J. Sequence analysis of cDNA coding for a major house dust mite allergen, Der p 1. Homology with cysteine proteases. J. Exp. Med. 1988, 167:175-182.
    • (1988) J. Exp. Med. , vol.167 , pp. 175-182
    • Chua, K.Y.1    Stewart, G.A.2    Thomas, W.R.3    Simpson, R.J.4    Dilworth, R.J.5    Plozza, T.M.6    Turner, K.J.7
  • 40
    • 35148824511 scopus 로고    scopus 로고
    • Interactions between mature Der p 1 and its free prodomain indicate membership of a new family of C1 peptidases
    • Zhang J., Hamilton J.M., Garrod D.R., Robinson C. Interactions between mature Der p 1 and its free prodomain indicate membership of a new family of C1 peptidases. Allergy 2007, 62:1302-1309.
    • (2007) Allergy , vol.62 , pp. 1302-1309
    • Zhang, J.1    Hamilton, J.M.2    Garrod, D.R.3    Robinson, C.4
  • 41
    • 0037032461 scopus 로고    scopus 로고
    • Maturation of the activities of recombinant mite allergens Der p 1 and Der f 1, and its implication in the blockade of proteolytic activity
    • Takai T., Mineki R., Nakazawa T., Takaoka M., Yasueda H., Murayama K., Okumura K., Ogawa H. Maturation of the activities of recombinant mite allergens Der p 1 and Der f 1, and its implication in the blockade of proteolytic activity. FEBS Lett. 2002, 531:265-272.
    • (2002) FEBS Lett. , vol.531 , pp. 265-272
    • Takai, T.1    Mineki, R.2    Nakazawa, T.3    Takaoka, M.4    Yasueda, H.5    Murayama, K.6    Okumura, K.7    Ogawa, H.8
  • 43
    • 33344463357 scopus 로고    scopus 로고
    • Glycosylation of recombinant proforms of major house dust mite allergens Der p 1 and Der f 1 decelerates the speed of maturation
    • Takai T., Mizuuchi E., Kikuchi Y., Nagamune T., Okumura K., Ogawa H. Glycosylation of recombinant proforms of major house dust mite allergens Der p 1 and Der f 1 decelerates the speed of maturation. Int. Arch. Allergy Immunol. 2006, 139:181-187.
    • (2006) Int. Arch. Allergy Immunol. , vol.139 , pp. 181-187
    • Takai, T.1    Mizuuchi, E.2    Kikuchi, Y.3    Nagamune, T.4    Okumura, K.5    Ogawa, H.6
  • 45
    • 0030579558 scopus 로고    scopus 로고
    • Histidine-tryptophan interactions in T4 lysozyme: 'anomalous' pH dependence of fluorescence
    • Van Gilst M., Hudson B.S. Histidine-tryptophan interactions in T4 lysozyme: 'anomalous' pH dependence of fluorescence. Biophys. Chem. 1996, 63:17-25.
    • (1996) Biophys. Chem. , vol.63 , pp. 17-25
    • Van Gilst, M.1    Hudson, B.S.2
  • 46
    • 0025991056 scopus 로고
    • Ultrastructural localization of the allergen Der p I in the gut of the house dust mite Dermatophagoides pteronyssinus
    • Thomas B., Heap P., Carswell F. Ultrastructural localization of the allergen Der p I in the gut of the house dust mite Dermatophagoides pteronyssinus. Int. Arch. Allergy Appl. Immunol. 1991, 94:365-367.
    • (1991) Int. Arch. Allergy Appl. Immunol. , vol.94 , pp. 365-367
    • Thomas, B.1    Heap, P.2    Carswell, F.3
  • 48
    • 14844331520 scopus 로고    scopus 로고
    • Analysis of the structure and allergenicity of recombinant pro- and mature Der p 1 and Der f 1: major conformational IgE epitopes blocked by prodomains
    • Takai T., Kato T., Yasueda H., Okumura K., Ogawa H. Analysis of the structure and allergenicity of recombinant pro- and mature Der p 1 and Der f 1: major conformational IgE epitopes blocked by prodomains. J. Allergy Clin. Immunol. 2005, 115:555-563.
    • (2005) J. Allergy Clin. Immunol. , vol.115 , pp. 555-563
    • Takai, T.1    Kato, T.2    Yasueda, H.3    Okumura, K.4    Ogawa, H.5
  • 49
    • 76249111368 scopus 로고    scopus 로고
    • Modulation of allergenicity of major house dust mite allergens Der f 1 and Der p 1 by interaction with an endogenous ligand
    • Takai T., Kato T., Hatanaka H., Inui K., Nakazawa T., Ichikawa S., Mitsuishi K., Ogawa H., Okumura K. Modulation of allergenicity of major house dust mite allergens Der f 1 and Der p 1 by interaction with an endogenous ligand. J. Immunol. 2009, 183:7958-7965.
    • (2009) J. Immunol. , vol.183 , pp. 7958-7965
    • Takai, T.1    Kato, T.2    Hatanaka, H.3    Inui, K.4    Nakazawa, T.5    Ichikawa, S.6    Mitsuishi, K.7    Ogawa, H.8    Okumura, K.9


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