메뉴 건너뛰기




Volumn 139, Issue 3, 2006, Pages 181-187

Glycosylation of recombinant proforms of major house dust mite allergens Der p 1 and Der f 1 decelerates the speed of maturation

Author keywords

Cysteine protease; Maturation speed; N glycosylation; Prosequence; Recombinant major house dust mite group 1 allergen

Indexed keywords

HOUSE DUST ALLERGEN; RECOMBINANT ANTIGEN;

EID: 33344463357     PISSN: 10182438     EISSN: None     Source Type: Journal    
DOI: 10.1159/000091163     Document Type: Article
Times cited : (25)

References (32)
  • 1
    • 0023571579 scopus 로고
    • Dust mites: Immunology, allergic disease, and environmental control
    • Platts-Mills TA, Chapman MD: Dust mites: immunology, allergic disease, and environmental control. J Allergy Clin Immunol 1987;80:755-775.
    • (1987) J Allergy Clin Immunol , vol.80 , pp. 755-775
    • Platts-Mills, T.A.1    Chapman, M.D.2
  • 3
    • 0032127867 scopus 로고    scopus 로고
    • A mite subversive: Cleavage of CD23 and CD25 by der p 1 enhances allergenicity
    • Shakib F, Schulz O, Sewell H: A mite subversive: cleavage of CD23 and CD25 by Der p 1 enhances allergenicity. Immunol Today 1998;19:313-316.
    • (1998) Immunol Today , vol.19 , pp. 313-316
    • Shakib, F.1    Schulz, O.2    Sewell, H.3
  • 4
    • 0033388991 scopus 로고    scopus 로고
    • The cysteine protease activity of the major dust mite allergen der p 1 selectively enhances the immunoglobulin e antibody response
    • Gough L, Schulz O, Sewell HF, Shakib F: The cysteine protease activity of the major dust mite allergen Der p 1 selectively enhances the immunoglobulin E antibody response. J Exp Med 1999;190:1897-1902.
    • (1999) J Exp Med , vol.190 , pp. 1897-1902
    • Gough, L.1    Schulz, O.2    Sewell, H.F.3    Shakib, F.4
  • 6
    • 0037108373 scopus 로고    scopus 로고
    • House dust mite allergens induce proinflammatory cytokines from respiratory epithelial cells: The cysteine protease allergen. der p 1, activates protease-activated receptor (PAR)-2 and inactivates PAR-1
    • Asokananthan N, Graham PT, Stewart DJ, Bakker AJ, Eidne KA, Thompson PJ, Stewart GA: House dust mite allergens induce proinflammatory cytokines from respiratory epithelial cells: the cysteine protease allergen. Der p 1, activates protease-activated receptor (PAR)-2 and inactivates PAR-1. J Immunol 2002;169:4572-4578.
    • (2002) J Immunol , vol.169 , pp. 4572-4578
    • Asokananthan, N.1    Graham, P.T.2    Stewart, D.J.3    Bakker, A.J.4    Eidne, K.A.5    Thompson, P.J.6    Stewart, G.A.7
  • 7
    • 0037391735 scopus 로고    scopus 로고
    • Human eosinophils are activated by cysteine proteases and release inflammatory mediators
    • Miike S, Kita H: Human eosinophils are activated by cysteine proteases and release inflammatory mediators. J Allergy Clin Immunol 2003;111:704-713.
    • (2003) J Allergy Clin Immunol , vol.111 , pp. 704-713
    • Miike, S.1    Kita, H.2
  • 8
    • 21344467711 scopus 로고    scopus 로고
    • Cystatin a inhibits IL-8 production by keratinocytes stimulated with der p 1 and der f 1: Biochemical skin barrier against mite cysteine proteases
    • Kato T, Takai T, Mitsuishi K, Okumura K, Ogawa H: Cystatin A inhibits IL-8 production by keratinocytes stimulated with Der p 1 and Der f 1: biochemical skin barrier against mite cysteine proteases. J Allergy Clin Immunol 2005;116:169-176.
    • (2005) J Allergy Clin Immunol , vol.116 , pp. 169-176
    • Kato, T.1    Takai, T.2    Mitsuishi, K.3    Okumura, K.4    Ogawa, H.5
  • 9
    • 21344459256 scopus 로고    scopus 로고
    • Proasthmatic effects and mechanisms of action of the dust mite allergen. der p 1, in airway smooth muscle
    • Grunstein MM, Veler H, Shan X, Larson J, Grunstein JS, Chuang S: Proasthmatic effects and mechanisms of action of the dust mite allergen. Der p 1, in airway smooth muscle. J Allergy Clin Immunol 2005;116:94-101.
    • (2005) J Allergy Clin Immunol , vol.116 , pp. 94-101
    • Grunstein, M.M.1    Veler, H.2    Shan, X.3    Larson, J.4    Grunstein, J.S.5    Chuang, S.6
  • 12
    • 0023877882 scopus 로고
    • Sequence analysis of cDNA coding for a major house dust mite allergen, der p 1. Homology with cysteine proteases
    • Chua KY, Stewart GA, Thomas WR, Simpson RJ, Dilworth RJ, Plozza TM, Turner KJ: 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
  • 13
    • 0026065591 scopus 로고
    • Sequence analysis of cDNA coding for a major house dust mite allergen, der f I
    • Dilworth RJ, Chua KY, Thomas WR: Sequence analysis of cDNA coding for a major house dust mite allergen, Der f I. Clin Exp Allergy 1991;21:25-32.
    • (1991) Clin Exp Allergy , vol.21 , pp. 25-32
    • Dilworth, R.J.1    Chua, K.Y.2    Thomas, W.R.3
  • 14
    • 0018958832 scopus 로고
    • Purification and characterization of the major allergen from Dermatophagoides pteronyssinus-antigen P1
    • Chapman MD, Platts-Mills TA: Purification and characterization of the major allergen from Dermatophagoides pteronyssinus-antigen P1. J Immunol 1980;125:587-592.
    • (1980) J Immunol , vol.125 , pp. 587-592
    • Chapman, M.D.1    Platts-Mills, T.A.2
  • 15
    • 0034124315 scopus 로고    scopus 로고
    • Biochemical and immunological characterization of a recombinant precursor form of the house dust mite allergen der p 1 produced by Drosophila cells
    • Jacquet A, Haumont M, Massaer M, Daminet V, Garcia L, Mazzu P, Jacobs P, Bollen A: Biochemical and immunological characterization of a recombinant precursor form of the house dust mite allergen Der p 1 produced by Drosophila cells. Clin Exp Allergy 2000;30:677-684.
    • (2000) Clin Exp Allergy , vol.30 , pp. 677-684
    • Jacquet, A.1    Haumont, M.2    Massaer, M.3    Daminet, V.4    Garcia, L.5    Mazzu, P.6    Jacobs, P.7    Bollen, A.8
  • 16
    • 0036159407 scopus 로고    scopus 로고
    • Maturation of Pichia pastoris-derived recombinant pro-Der p 1 induced by deglycosylation and by the natural cysteine protease der p 1 from house dust mite
    • van Oort E, de Heer PG, van Leeuwen WA, Derksen NI, Muller M, Huveneers S, Aalberse RC, van Ree R: Maturation of Pichia pastoris-derived recombinant pro-Der p 1 induced by deglycosylation and by the natural cysteine protease Der p 1 from house dust mite. Eur J Biochem 2002;269:671-679.
    • (2002) Eur J Biochem , vol.269 , pp. 671-679
    • Van Oort, E.1    De Heer, P.G.2    Van Leeuwen, W.A.3    Derksen, N.I.4    Muller, M.5    Huveneers, S.6    Aalberse, R.C.7    Van Ree, R.8
  • 18
    • 14844331520 scopus 로고    scopus 로고
    • Analysis of the structure and allergenicitiy 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 allergenicitiy 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
  • 19
    • 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
  • 20
    • 0035138773 scopus 로고    scopus 로고
    • Biologically active recombinant forms of a major house dust mite group 1 allergen der f 1 with full activities of both cysteine protease and IgE binding
    • Yasuhara T, Takai T, Yuuki T, Okudaira H, Okumura Y: Biologically active recombinant forms of a major house dust mite group 1 allergen Der f 1 with full activities of both cysteine protease and IgE binding. Clin Exp Allergy 2001;31:116-124.
    • (2001) Clin Exp Allergy , vol.31 , pp. 116-124
    • Yasuhara, T.1    Takai, T.2    Yuuki, T.3    Okudaira, H.4    Okumura, Y.5
  • 21
    • 0031826072 scopus 로고    scopus 로고
    • Structural basis for specificity of papain-like cysteine protease proregions toward their cognate enzymes
    • Groves MR, 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
  • 22
    • 0035987313 scopus 로고    scopus 로고
    • High-level expression of recombinant house dust mite allergen der p 1 in Pichia pastoris
    • Jacquet A, Magi M, Petry H, Bollen A: High-level expression of recombinant house dust mite allergen Der p 1 in Pichia pastoris. Clin Exp Allergy 2002;32:1048-1053.
    • (2002) Clin Exp Allergy , vol.32 , pp. 1048-1053
    • Jacquet, A.1    Magi, M.2    Petry, H.3    Bollen, A.4
  • 23
    • 0030038759 scopus 로고    scopus 로고
    • Potency and selectivity of the cathepsin L propeptide as an inhibitor of cysteine proteases
    • Carmona E, Dufour E, Plouffe C, Takebe S, Mason P, Mort JS, Menard R: Potency and selectivity of the cathepsin L propeptide as an inhibitor of cysteine proteases. Biochemistry 1996;35:8149-8157.
    • (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
  • 24
    • 0028309017 scopus 로고
    • The proregion of cathepsin L is required for proper folding, stability, and ER exit
    • Tao K, Stearns NA, Dong J, Wu QL, Sahagian GG: The proregion of cathepsin L is required for proper folding, stability, and ER exit. Arch Biochem Biophys 1994;311:19-27.
    • (1994) Arch Biochem Biophys , vol.311 , pp. 19-27
    • Tao, K.1    Stearns, N.A.2    Dong, J.3    Wu, Q.L.4    Sahagian, G.G.5
  • 25
    • 0033226989 scopus 로고    scopus 로고
    • Proregion of Bombyx mori cysteine proteinase functions as an intramolecular chaperone to promote proper folding of the mature enzyme
    • Yamamoto Y, Watabe S, Kageyama T, Takahashi SY: Proregion of Bombyx mori cysteine proteinase functions as an intramolecular chaperone to promote proper folding of the mature enzyme. Arch Insect Biochem Physiol 1999;42:167-178.
    • (1999) Arch Insect Biochem Physiol , vol.42 , pp. 167-178
    • Yamamoto, Y.1    Watabe, S.2    Kageyama, T.3    Takahashi, S.Y.4
  • 26
    • 0034471704 scopus 로고    scopus 로고
    • The function of propeptide domains of cysteine proteinases
    • Wiederanders B: The function of propeptide domains of cysteine proteinases. Adv Exp Med Biol 2000;477:261-270.
    • (2000) Adv Exp Med Biol , vol.477 , pp. 261-270
    • Wiederanders, B.1
  • 27
    • 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
  • 29
    • 0036598404 scopus 로고    scopus 로고
    • The future of antigen-specific immunotherapy of allergy
    • Valenta R: The future of antigen-specific immunotherapy of allergy. Nat Rev Immunol 2002;2:446-453.
    • (2002) Nat Rev Immunol , vol.2 , pp. 446-453
    • Valenta, R.1
  • 30
    • 0027214181 scopus 로고
    • Sequence polymorphisms of cDNA clones encoding the mite allergen der p I
    • Chua KY, Kehal PK, Thomas WR: Sequence polymorphisms of cDNA clones encoding the mite allergen Der p I. Int Arch Allergy Immunol 1993;101:364-368.
    • (1993) Int Arch Allergy Immunol , vol.101 , pp. 364-368
    • Chua, K.Y.1    Kehal, P.K.2    Thomas, W.R.3
  • 31
    • 0035291498 scopus 로고    scopus 로고
    • Cloning and expression of cDNA encoding the complete prepro-form of an isoform of der f 1, the major group 1 allergen from house dust mite Dermatophagoides farinae
    • Yasuhara T, Takai T, Yuuki T, Okudaira H, Okumura Y: Cloning and expression of cDNA encoding the complete prepro-form of an isoform of Der f 1, the major group 1 allergen from house dust mite Dermatophagoides farinae. Biosci Biotechnol Biochem 2001;65:563-569.
    • (2001) Biosci Biotechnol Biochem , vol.65 , pp. 563-569
    • Yasuhara, T.1    Takai, T.2    Yuuki, T.3    Okudaira, H.4    Okumura, Y.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.