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Volumn 4, Issue 4, 2009, Pages

Histoplasma capsulatum Encodes a Dipeptidyl Peptidase Active against the Mammalian Immunoregulatory Peptide, Substance P

Author keywords

[No Author keywords available]

Indexed keywords

DIPEPTIDYL PEPTIDASE IV; PRIMER DNA; RECOMBINANT PROTEIN; SUBSTANCE P;

EID: 67649230240     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0005281     Document Type: Article
Times cited : (9)

References (34)
  • 1
    • 0034953642 scopus 로고    scopus 로고
    • The epidemiology of histoplasmosis: a review
    • Cano MV, Hajjeh RA, (2001) The epidemiology of histoplasmosis: a review. Semin Respir Infect 16: 109-118.
    • (2001) Semin Respir Infect , vol.16 , pp. 109-118
    • Cano, M.V.1    Hajjeh, R.A.2
  • 2
    • 0035723325 scopus 로고    scopus 로고
    • CD26: a multifunctional integral membrane and secreted protein of activated lymphocytes
    • Gorrell MD, Gysbers V, McCaughan GW, (2001) CD26: a multifunctional integral membrane and secreted protein of activated lymphocytes. Scand J Immunol 54: 249-264.
    • (2001) Scand J Immunol , vol.54 , pp. 249-264
    • Gorrell, M.D.1    Gysbers, V.2    McCaughan, G.W.3
  • 3
    • 0036634815 scopus 로고    scopus 로고
    • Loss of dipeptidylpeptidase IV activity in chronic rhinosinusitis contributes to the neurogenic inflammation induced by substance P in the nasal mucosa
    • 10.1096/fj.01-0939fje
    • Grouzmann E, Monod M, Landis B, Wilk S, Brakch N, et al.(2002) Loss of dipeptidylpeptidase IV activity in chronic rhinosinusitis contributes to the neurogenic inflammation induced by substance P in the nasal mucosa. FASEB J 10.1096/fj.01-0939fje.
    • (2002) FASEB J
    • Grouzmann, E.1    Monod, M.2    Landis, B.3    Wilk, S.4    Brakch, N.5
  • 4
    • 0037213660 scopus 로고    scopus 로고
    • Granulomas in schistosome and mycobacterial infections: a model of local immune responses
    • Sandor M, Weinstock JV, Wynn TA, (2003) Granulomas in schistosome and mycobacterial infections: a model of local immune responses. Trends Immunol 24: 44-52.
    • (2003) Trends Immunol , vol.24 , pp. 44-52
    • Sandor, M.1    Weinstock, J.V.2    Wynn, T.A.3
  • 5
    • 2442703201 scopus 로고    scopus 로고
    • The role of substance P, hemokinin and their receptor in governing mucosal inflammation and granulomatous responses
    • Weinstock JV, (2004) The role of substance P, hemokinin and their receptor in governing mucosal inflammation and granulomatous responses. Frontiers Bioscience 9: 1936-1943.
    • (2004) Frontiers Bioscience , vol.9 , pp. 1936-1943
    • Weinstock, J.V.1
  • 6
    • 0038191082 scopus 로고    scopus 로고
    • Impaired growth rates in milk of Lactobacillus helveticus peptidase mutants can be overcome by use of amino acid supplements
    • Christensen JE, Steele JL, (2003) Impaired growth rates in milk of Lactobacillus helveticus peptidase mutants can be overcome by use of amino acid supplements. J Bacteriol 185: 3297-3306.
    • (2003) J Bacteriol , vol.185 , pp. 3297-3306
    • Christensen, J.E.1    Steele, J.L.2
  • 7
    • 0034778624 scopus 로고    scopus 로고
    • Histopathological studies on virulence of dipeptidyl aminopeptidase IV (DPPIV) of Porphyromonas gingivalis in a mouse abscess model: use of a DPPIV-deficient mutant
    • Yagishita H, Kumagai Y, Konishi K, Takahashi Y, Aoba T, et al.(2001) Histopathological studies on virulence of dipeptidyl aminopeptidase IV (DPPIV) of Porphyromonas gingivalis in a mouse abscess model: use of a DPPIV-deficient mutant. Infect Immun 69: 7159-7161.
    • (2001) Infect Immun , vol.69 , pp. 7159-7161
    • Yagishita, H.1    Kumagai, Y.2    Konishi, K.3    Takahashi, Y.4    Aoba, T.5
  • 8
    • 0033972312 scopus 로고    scopus 로고
    • Enzymatic properties of dipeptidyl aminopeptidase IV produced by the periodontal pathogen Porphyromonas gingivalis and its participation in virulence
    • Kumagai Y, Konishi K, Gomi T, Yagishita H, Yajima A, et al.(2000) Enzymatic properties of dipeptidyl aminopeptidase IV produced by the periodontal pathogen Porphyromonas gingivalis and its participation in virulence. Infect Immun 68: 716-724.
    • (2000) Infect Immun , vol.68 , pp. 716-724
    • Kumagai, Y.1    Konishi, K.2    Gomi, T.3    Yagishita, H.4    Yajima, A.5
  • 9
    • 17644416120 scopus 로고    scopus 로고
    • Molecular mechanism for connective tissue destruction by dipeptidyl aminopeptidase IV produced by the periodontal pathogen Porphyromonas gingivalis
    • Kumagai Y, Yagishita H, Yajima A, Okamoto T, Konishi K, (2005) Molecular mechanism for connective tissue destruction by dipeptidyl aminopeptidase IV produced by the periodontal pathogen Porphyromonas gingivalis. Infect Immun 73: 2655-2664.
    • (2005) Infect Immun , vol.73 , pp. 2655-2664
    • Kumagai, Y.1    Yagishita, H.2    Yajima, A.3    Okamoto, T.4    Konishi, K.5
  • 10
    • 0033574747 scopus 로고    scopus 로고
    • Transcript splicing is essential for functional Histoplasma capsulatum URA5 expression
    • Retallack DM, Woods JP, (1999) Transcript splicing is essential for functional Histoplasma capsulatum URA5 expression. Gene 230: 181-185.
    • (1999) Gene , vol.230 , pp. 181-185
    • Retallack, D.M.1    Woods, J.P.2
  • 11
    • 0032038703 scopus 로고    scopus 로고
    • Electrotransformation and expression of bacterial genes encoding hygromycin phosphotransferase and beta-galactosidase in the pathogenic fungus Histoplasma capsulatum
    • Woods JP, Heinecke EL, Goldman WE, (1998) Electrotransformation and expression of bacterial genes encoding hygromycin phosphotransferase and beta-galactosidase in the pathogenic fungus Histoplasma capsulatum. Infect Immun 66: 1697-1707.
    • (1998) Infect Immun , vol.66 , pp. 1697-1707
    • Woods, J.P.1    Heinecke, E.L.2    Goldman, W.E.3
  • 12
    • 52649152402 scopus 로고    scopus 로고
    • Histoplasma capsulatum secreted gamma-glutamyltransferase reduces iron by generating an efficient ferric reductant
    • Zarnowski R, Cooper KG, Brunold LS, Calaycay J, Woods JP, (2008) Histoplasma capsulatum secreted gamma-glutamyltransferase reduces iron by generating an efficient ferric reductant. Mol Microbiol 70: 352-368.
    • (2008) Mol Microbiol , vol.70 , pp. 352-368
    • Zarnowski, R.1    Cooper, K.G.2    Brunold, L.S.3    Calaycay, J.4    Woods, J.P.5
  • 13
    • 33745045683 scopus 로고    scopus 로고
    • Identification of hydrophobic residues critical for DPP-IV dimerization
    • Chien CH, Tsai CH, Lin CH, Chou CY, Chen X, (2006) Identification of hydrophobic residues critical for DPP-IV dimerization. Biochemistry 45: 7006-7012.
    • (2006) Biochemistry , vol.45 , pp. 7006-7012
    • Chien, C.H.1    Tsai, C.H.2    Lin, C.H.3    Chou, C.Y.4    Chen, X.5
  • 14
    • 0347994115 scopus 로고    scopus 로고
    • N-linked glycosylation of dipeptidyl peptidase IV (CD26): effects on enzyme activity, homodimer formation, and adenosine deaminase binding
    • Aertgeerts K, Ye S, Shi L, Prasad SG, Witmer D, et al.(2004) N-linked glycosylation of dipeptidyl peptidase IV (CD26): effects on enzyme activity, homodimer formation, and adenosine deaminase binding. Protein Sci 13: 145-154.
    • (2004) Protein Sci , vol.13 , pp. 145-154
    • Aertgeerts, K.1    Ye, S.2    Shi, L.3    Prasad, S.G.4    Witmer, D.5
  • 15
    • 0026326713 scopus 로고
    • Differential processing of substance P and neurokinin A by plasma dipeptidyl(amino)peptidase IV, aminopeptidase M and angiotensin converting enzyme
    • Wang LH, Ahmad S, Benter IF, Chow A, Mizutani S, et al.(1991) Differential processing of substance P and neurokinin A by plasma dipeptidyl(amino)peptidase IV, aminopeptidase M and angiotensin converting enzyme. Peptides 12: 1357-1364.
    • (1991) Peptides , vol.12 , pp. 1357-1364
    • Wang, L.H.1    Ahmad, S.2    Benter, I.F.3    Chow, A.4    Mizutani, S.5
  • 16
    • 0026755628 scopus 로고
    • Dipeptidyl(amino)peptidase IV and aminopeptidase M metabolize circulating substance P in vivo
    • Ahmad S, Wang L, Ward PE, (1992) Dipeptidyl(amino)peptidase IV and aminopeptidase M metabolize circulating substance P in vivo. J Pharmacol Exp Ther 260: 1257-1261.
    • (1992) J Pharmacol Exp Ther , vol.260 , pp. 1257-1261
    • Ahmad, S.1    Wang, L.2    Ward, P.E.3
  • 17
    • 34249909212 scopus 로고    scopus 로고
    • RNA interference-mediated silencing of the YPS3 gene of Histoplasma capsulatum reveals virulence defects
    • Bohse ML, Woods JP, (2007) RNA interference-mediated silencing of the YPS3 gene of Histoplasma capsulatum reveals virulence defects. Infect Immun 75: 2811-2817.
    • (2007) Infect Immun , vol.75 , pp. 2811-2817
    • Bohse, M.L.1    Woods, J.P.2
  • 19
    • 0030858804 scopus 로고    scopus 로고
    • Dipeptidyl-peptidase IV secreted by Aspergillus fumigatus, a fungus pathogenic to humans
    • Beauvais A, Monod M, Wyniger J, Debeaupuis JP, Grouzmann E, et al.(1997) Dipeptidyl-peptidase IV secreted by Aspergillus fumigatus, a fungus pathogenic to humans. Infect Immun 65: 3042-3047.
    • (1997) Infect Immun , vol.65 , pp. 3042-3047
    • Beauvais, A.1    Monod, M.2    Wyniger, J.3    Debeaupuis, J.P.4    Grouzmann, E.5
  • 20
    • 38049059907 scopus 로고    scopus 로고
    • Implication of dipeptidylpeptidase IV activity in human bronchial inflammation and in bronchoconstriction evaluated in anesthetized rabbits
    • Landis BN, Grouzmann E, Monod M, Busso N, Petak F, et al.(2008) Implication of dipeptidylpeptidase IV activity in human bronchial inflammation and in bronchoconstriction evaluated in anesthetized rabbits. Respiration 75: 89-97.
    • (2008) Respiration , vol.75 , pp. 89-97
    • Landis, B.N.1    Grouzmann, E.2    Monod, M.3    Busso, N.4    Petak, F.5
  • 21
    • 34548563758 scopus 로고    scopus 로고
    • Production of extracellular proteolytic activity by Histoplasma capsulatum grown in Histoplasma-macrophage medium is limited to restriction fragment length polymorphism class 1 isolates
    • Zarnowski R, Connolly PA, Wheat LJ, Woods JP, (2007) Production of extracellular proteolytic activity by Histoplasma capsulatum grown in Histoplasma-macrophage medium is limited to restriction fragment length polymorphism class 1 isolates. Diagn Microbiol Infect Dis 59: 39-47.
    • (2007) Diagn Microbiol Infect Dis , vol.59 , pp. 39-47
    • Zarnowski, R.1    Connolly, P.A.2    Wheat, L.J.3    Woods, J.P.4
  • 22
    • 0027940569 scopus 로고
    • Expression of seven members of the gene family encoding secretory aspartyl proteinases in Candida albicans
    • Hube B, Monod M, Schofield DA, Brown AJ, Gow NA, (1994) Expression of seven members of the gene family encoding secretory aspartyl proteinases in Candida albicans. Mol Microbiol 14: 87-99.
    • (1994) Mol Microbiol , vol.14 , pp. 87-99
    • Hube, B.1    Monod, M.2    Schofield, D.A.3    Brown, A.J.4    Gow, N.A.5
  • 23
    • 4544365934 scopus 로고    scopus 로고
    • Candida albicans proteinases and host/pathogen interactions
    • Naglik J, Albrecht A, Bader O, Hube B, (2004) Candida albicans proteinases and host/pathogen interactions. Cell Microbiol 6: 915-926.
    • (2004) Cell Microbiol , vol.6 , pp. 915-926
    • Naglik, J.1    Albrecht, A.2    Bader, O.3    Hube, B.4
  • 24
    • 25444440084 scopus 로고    scopus 로고
    • Markers for host-induced gene expression in Trichophyton dermatophytosis
    • Kaufman G, Berdicevsky I, Woodfolk JA, Horwitz BA, (2005) Markers for host-induced gene expression in Trichophyton dermatophytosis. Infect Immun 73: 6584-6590.
    • (2005) Infect Immun , vol.73 , pp. 6584-6590
    • Kaufman, G.1    Berdicevsky, I.2    Woodfolk, J.A.3    Horwitz, B.A.4
  • 25
    • 4544344775 scopus 로고    scopus 로고
    • A pilot-scale expressed sequence tag analysis of Beauveria bassiana gene expression reveals a tripeptidyl peptidase that is differentially expressed in vivo
    • Tartar A, Boucias DG, (2004) A pilot-scale expressed sequence tag analysis of Beauveria bassiana gene expression reveals a tripeptidyl peptidase that is differentially expressed in vivo. Mycopathologia 158: 201-209.
    • (2004) Mycopathologia , vol.158 , pp. 201-209
    • Tartar, A.1    Boucias, D.G.2
  • 26
    • 0032078266 scopus 로고    scopus 로고
    • The substance P and somatostatin interferon-gamma immunoregulatory circuit
    • Weinstock JV, Elliott D, (1998) The substance P and somatostatin interferon-gamma immunoregulatory circuit. Ann N Y Acad Sci 840: 532-539.
    • (1998) Ann N Y Acad Sci , vol.840 , pp. 532-539
    • Weinstock, J.V.1    Elliott, D.2
  • 27
    • 0027104212 scopus 로고
    • Determination of the amino acid residues in substance P conferring selectivity and specificity for the rat neurokinin receptors
    • Cascieri MA, Huang RR, Fong TM, Cheung AH, Sadowski S, et al.(1992) Determination of the amino acid residues in substance P conferring selectivity and specificity for the rat neurokinin receptors. Mol Pharmacol 41: 1096-1099.
    • (1992) Mol Pharmacol , vol.41 , pp. 1096-1099
    • Cascieri, M.A.1    Huang, R.R.2    Fong, T.M.3    Cheung, A.H.4    Sadowski, S.5
  • 28
    • 0031899750 scopus 로고    scopus 로고
    • Neuropeptide regulation of proinflammatory cytokine responses
    • Dickerson C, Undem B, Bullock B, Winchurch RA, (1998) Neuropeptide regulation of proinflammatory cytokine responses. J Leukoc Biol 63: 602-605.
    • (1998) J Leukoc Biol , vol.63 , pp. 602-605
    • Dickerson, C.1    Undem, B.2    Bullock, B.3    Winchurch, R.A.4
  • 29
    • 0027313356 scopus 로고
    • Substance P modulates antigen-induced, IFN-gamma production in murine Schistosomiasis mansoni
    • Blum AM, Metwali A, Cook G, Mathew RC, Elliott D, et al.(1993) Substance P modulates antigen-induced, IFN-gamma production in murine Schistosomiasis mansoni. J Immunol 151: 225-233.
    • (1993) J Immunol , vol.151 , pp. 225-233
    • Blum, A.M.1    Metwali, A.2    Cook, G.3    Mathew, R.C.4    Elliott, D.5
  • 31
    • 0035798196 scopus 로고    scopus 로고
    • Kinetic study of the processing by dipeptidyl-peptidase IV/CD26 of neuropeptides involved in pancreatic insulin secretion
    • Lambeir AM, Durinx C, Proost P, Van Damme J, Scharpe S, et al.(2001) Kinetic study of the processing by dipeptidyl-peptidase IV/CD26 of neuropeptides involved in pancreatic insulin secretion. FEBS Lett 507: 327-330.
    • (2001) FEBS Lett , vol.507 , pp. 327-330
    • Lambeir, A.M.1    Durinx, C.2    Proost, P.3    Van Damme, J.4    Scharpe, S.5
  • 32
    • 33644690435 scopus 로고    scopus 로고
    • Breaking or making immunological privilege in the central nervous system: the regulation of immunity by neuropeptides
    • Reinke E, Fabry Z, (2006) Breaking or making immunological privilege in the central nervous system: the regulation of immunity by neuropeptides. Immunol Lett 104: 102-109.
    • (2006) Immunol Lett , vol.104 , pp. 102-109
    • Reinke, E.1    Fabry, Z.2
  • 33
    • 0030819309 scopus 로고    scopus 로고
    • Regulation of the receptor specificity and function of the chemokine RANTES (regulated on activation, normal T cell expressed and secreted) by dipeptidyl peptidase IV (CD26)-mediated cleavage
    • Oravecz T, Pall M, Roderiquez G, Gorrell MD, Ditto M, et al.(1997) Regulation of the receptor specificity and function of the chemokine RANTES (regulated on activation, normal T cell expressed and secreted) by dipeptidyl peptidase IV (CD26)-mediated cleavage. J Exp Med 186: 1865-1872.
    • (1997) J Exp Med , vol.186 , pp. 1865-1872
    • Oravecz, T.1    Pall, M.2    Roderiquez, G.3    Gorrell, M.D.4    Ditto, M.5
  • 34
    • 0033561659 scopus 로고    scopus 로고
    • CD26/dipeptidyl-peptidase IV down-regulates the eosinophil chemotactic potency, but not the anti-HIV activity of human eotaxin by affecting its interaction with CC chemokine receptor 3
    • Struyf S, Proost P, Schols D, De Clercq E, Opdenakker G, et al.(1999) CD26/dipeptidyl-peptidase IV down-regulates the eosinophil chemotactic potency, but not the anti-HIV activity of human eotaxin by affecting its interaction with CC chemokine receptor 3. J Immunol 162: 4903-4909.
    • (1999) J Immunol , vol.162 , pp. 4903-4909
    • Struyf, S.1    Proost, P.2    Schols, D.3    De Clercq, E.4    Opdenakker, G.5


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