메뉴 건너뛰기




Volumn 118, Issue 4, 2006, Pages 878-884

Purification of a novel aminopeptidase from the pollen of Parietaria judaica that alters epithelial integrity and degrades neuropeptides

Author keywords

aminopeptidase; angiotensin I; E cadherin; occludin; Parietaria judaica; substance P; VIP

Indexed keywords

AMINOPEPTIDASE; METHYLENE BLUE; NEUROPEPTIDE; OCCLUDIN; POLLEN EXTRACT; UVOMORULIN;

EID: 33749349447     PISSN: 00916749     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jaci.2006.05.029     Document Type: Article
Times cited : (23)

References (26)
  • 1
    • 0031765220 scopus 로고    scopus 로고
    • Unique role of allergens and the epithelium in asthma
    • Thompson P.J. Unique role of allergens and the epithelium in asthma. Clin Exp Allergy 28 suppl 5 (1998) 110-116
    • (1998) Clin Exp Allergy , vol.28 , Issue.SUPPL. 5 , pp. 110-116
    • Thompson, P.J.1
  • 2
    • 0032695151 scopus 로고    scopus 로고
    • Der p 1 facilitates transepithelial allergen delivery by disruption of tight junctions
    • Wan H., Winton H.L., Soeller C., Tovey E.R., Gruenert D.C., Thompson P.J., et al. Der p 1 facilitates transepithelial allergen delivery by disruption of tight junctions. J Clin Invest 104 (1999) 123-133
    • (1999) J Clin Invest , vol.104 , pp. 123-133
    • Wan, H.1    Winton, H.L.2    Soeller, C.3    Tovey, E.R.4    Gruenert, D.C.5    Thompson, P.J.6
  • 3
    • 0035546146 scopus 로고    scopus 로고
    • Localization, release and bioavailability of pollen allergens: the influence of environmental factors
    • Behrendt H., and Becker W.M. Localization, release and bioavailability of pollen allergens: the influence of environmental factors. Curr Opin Immunol 13 (2001) 709-715
    • (2001) Curr Opin Immunol , vol.13 , pp. 709-715
    • Behrendt, H.1    Becker, W.M.2
  • 4
    • 0031840748 scopus 로고    scopus 로고
    • Injury to murine airway epithelial cells by pollen enzymes
    • Hassim Z., Maronese S.E., and Kumar R.K. Injury to murine airway epithelial cells by pollen enzymes. Thorax 53 (1998) 368-371
    • (1998) Thorax , vol.53 , pp. 368-371
    • Hassim, Z.1    Maronese, S.E.2    Kumar, R.K.3
  • 5
    • 0034098619 scopus 로고    scopus 로고
    • Substrate preference profiles of proteases released by allergenic pollens
    • Widmer F., Hayes P.J., Whittaker R.G., and Kumar R.K. Substrate preference profiles of proteases released by allergenic pollens. Clin Exp Allergy 30 (2000) 571-576
    • (2000) Clin Exp Allergy , vol.30 , pp. 571-576
    • Widmer, F.1    Hayes, P.J.2    Whittaker, R.G.3    Kumar, R.K.4
  • 6
    • 0032011401 scopus 로고    scopus 로고
    • Purification and characterization of an arginine-specific peptidase from ragweed (Ambrosia artemisiifolia) pollen
    • Bagarozzi Jr. D.A., Potempa J., and Travis J. Purification and characterization of an arginine-specific peptidase from ragweed (Ambrosia artemisiifolia) pollen. Am J Respir Cell Mol Biol 18 (1998) 363-369
    • (1998) Am J Respir Cell Mol Biol , vol.18 , pp. 363-369
    • Bagarozzi Jr., D.A.1    Potempa, J.2    Travis, J.3
  • 7
    • 10244251626 scopus 로고    scopus 로고
    • Purification and characterization of a novel endopeptidase in ragweed (Ambrosia artemisiifolia) pollen
    • Bagarozzi Jr. D.A., Pike R., Potempa J., and Travis J. Purification and characterization of a novel endopeptidase in ragweed (Ambrosia artemisiifolia) pollen. J Biol Chem 271 (1996) 26227-26232
    • (1996) J Biol Chem , vol.271 , pp. 26227-26232
    • Bagarozzi Jr., D.A.1    Pike, R.2    Potempa, J.3    Travis, J.4
  • 8
    • 0032479174 scopus 로고    scopus 로고
    • Purification and characterization of a novel peptidase (IImes) from mesquite (Prosopis velutina) pollen
    • Matheson N.R., and Travis J. Purification and characterization of a novel peptidase (IImes) from mesquite (Prosopis velutina) pollen. J Biol Chem 273 (1998) 16771-16777
    • (1998) J Biol Chem , vol.273 , pp. 16771-16777
    • Matheson, N.R.1    Travis, J.2
  • 9
    • 0029282524 scopus 로고
    • Isolation and properties of an angiotensin II-cleaving peptidase from mesquite pollen
    • Matheson N., Schmidt J., and Travis J. Isolation and properties of an angiotensin II-cleaving peptidase from mesquite pollen. Am J Respir Cell Mol Biol 12 (1995) 441-448
    • (1995) Am J Respir Cell Mol Biol , vol.12 , pp. 441-448
    • Matheson, N.1    Schmidt, J.2    Travis, J.3
  • 12
    • 0033909638 scopus 로고    scopus 로고
    • Plant allergens and pathogenesis-related proteins: what do they have in common?
    • Hoffmann-Sommergruber K. Plant allergens and pathogenesis-related proteins: what do they have in common?. Int Arch Allergy Immunol 122 (2000) 155-166
    • (2000) Int Arch Allergy Immunol , vol.122 , pp. 155-166
    • Hoffmann-Sommergruber, K.1
  • 14
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during assembly of head of bacteriophage-T4
    • Laemmli U.K. Cleavage of structural proteins during assembly of head of bacteriophage-T4. Nature 227 (1970) 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 15
    • 0037458547 scopus 로고    scopus 로고
    • PepN, the major Suc-LLVY-AMC-hydrolyzing enzyme in Escherichia coli, displays functional similarity with downstream processing enzymes in Archaea and eukarya: implications in cytosolic protein degradation
    • Chandu D., Kumar A., and Nandi D. PepN, the major Suc-LLVY-AMC-hydrolyzing enzyme in Escherichia coli, displays functional similarity with downstream processing enzymes in Archaea and eukarya: implications in cytosolic protein degradation. J Biol Chem 278 (2003) 5548-5556
    • (2003) J Biol Chem , vol.278 , pp. 5548-5556
    • Chandu, D.1    Kumar, A.2    Nandi, D.3
  • 16
    • 0037385099 scopus 로고    scopus 로고
    • Purification and some properties of cathepsin H from rabbit skeletal muscle
    • Matsuishi M., Saito G., Okitani A., and Kato H. Purification and some properties of cathepsin H from rabbit skeletal muscle. Int J Biochem Cell Biol 35 (2003) 474-485
    • (2003) Int J Biochem Cell Biol , vol.35 , pp. 474-485
    • Matsuishi, M.1    Saito, G.2    Okitani, A.3    Kato, H.4
  • 17
    • 0020621648 scopus 로고
    • Action of human liver cathepsin B on the oxidized insulin B chain
    • McKay M.J., Offermann M.K., Barrett A.J., and Bond J.S. Action of human liver cathepsin B on the oxidized insulin B chain. Biochem J 213 (1983) 467-471
    • (1983) Biochem J , vol.213 , pp. 467-471
    • McKay, M.J.1    Offermann, M.K.2    Barrett, A.J.3    Bond, J.S.4
  • 18
    • 0035077983 scopus 로고    scopus 로고
    • Peptidase allergens, occludin and claudins: do their interactions facilitate the development of hypersensitivity reactions at mucosal surfaces?
    • Robinson C., Baker S.F., and Garrod D.R. Peptidase allergens, occludin and claudins: do their interactions facilitate the development of hypersensitivity reactions at mucosal surfaces?. Clin Exp Allergy 31 (2001) 186-192
    • (2001) Clin Exp Allergy , vol.31 , pp. 186-192
    • Robinson, C.1    Baker, S.F.2    Garrod, D.R.3
  • 20
    • 0034780321 scopus 로고    scopus 로고
    • Vasoactive intestinal polypeptide as mediator of asthma
    • Groneberg D.A., Springer J., and Fischer A. Vasoactive intestinal polypeptide as mediator of asthma. Pulm Pharm Ther 14 (2001) 391-401
    • (2001) Pulm Pharm Ther , vol.14 , pp. 391-401
    • Groneberg, D.A.1    Springer, J.2    Fischer, A.3
  • 21
    • 0034112105 scopus 로고    scopus 로고
    • Quantitative structural and biochemical analyses of tight junction dynamics following exposure of epithelial cells to house dust mite allergen Der p 1
    • Wan H., Winton H.L., Soeller C., Gruenert D.C., Thompson P.J., Cannell M.B., et al. Quantitative structural and biochemical analyses of tight junction dynamics following exposure of epithelial cells to house dust mite allergen Der p 1. Clin Exp Allergy 30 (2000) 685-698
    • (2000) Clin Exp Allergy , vol.30 , pp. 685-698
    • Wan, H.1    Winton, H.L.2    Soeller, C.3    Gruenert, D.C.4    Thompson, P.J.5    Cannell, M.B.6
  • 22
    • 0037336565 scopus 로고    scopus 로고
    • Signalling to and from tight junctions
    • Matter K., and Balda M.S. Signalling to and from tight junctions. Nat Rev Molec Cell Biol 4 (2003) 225-236
    • (2003) Nat Rev Molec Cell Biol , vol.4 , pp. 225-236
    • Matter, K.1    Balda, M.S.2
  • 23
    • 0035086672 scopus 로고    scopus 로고
    • The transmembrane protein occludin of epithelial tight junctions is a functional target for serine peptidases from faecal pellets of Dermatophagoides pteronyssinus
    • Wan H., Winton H.L., Soeller C., Taylor G.W., Gruenert D.C., Thompson P.J., et al. The transmembrane protein occludin of epithelial tight junctions is a functional target for serine peptidases from faecal pellets of Dermatophagoides pteronyssinus. Clin Exp Allergy 31 (2001) 279-294
    • (2001) Clin Exp Allergy , vol.31 , pp. 279-294
    • Wan, H.1    Winton, H.L.2    Soeller, C.3    Taylor, G.W.4    Gruenert, D.C.5    Thompson, P.J.6
  • 24
    • 0043123373 scopus 로고    scopus 로고
    • Proteolytic activity of the house dust mite allergen Der p 1 enhances allergenicity in a mouse inhalation model
    • Gough L., Campbell E., Bayley D., Van Heeke G., and Shakib F. Proteolytic activity of the house dust mite allergen Der p 1 enhances allergenicity in a mouse inhalation model. Clin Exp Allergy 33 (2003) 1159-1163
    • (2003) Clin Exp Allergy , vol.33 , pp. 1159-1163
    • Gough, L.1    Campbell, E.2    Bayley, D.3    Van Heeke, G.4    Shakib, F.5
  • 25
    • 0034796380 scopus 로고    scopus 로고
    • The proteolytic activity of the major dust mite allergen Der p 1 enhances the IgE antibody response to a bystander antigen
    • Gough L., Sewell H.F., and Shakib F. The proteolytic activity of the major dust mite allergen Der p 1 enhances the IgE antibody response to a bystander antigen. Clin Exp Allergy 31 (2001) 1594-1598
    • (2001) Clin Exp Allergy , vol.31 , pp. 1594-1598
    • Gough, L.1    Sewell, H.F.2    Shakib, F.3
  • 26
    • 20044381704 scopus 로고    scopus 로고
    • Potential roles in rhinitis for protease and other enzymatic activities of allergens
    • Sehgal N., Custovic A., and Woodcock A. Potential roles in rhinitis for protease and other enzymatic activities of allergens. Curr Allergy Asth Rep 5 (2005) 221-226
    • (2005) Curr Allergy Asth Rep , vol.5 , pp. 221-226
    • Sehgal, N.1    Custovic, A.2    Woodcock, A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.