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Volumn 94, Issue 4, 1999, Pages 1418-1428

A novel serpin expressed by blood-borne microfilariae of the parasitic nematode Brugia malayi inhibits human neutrophil serine proteinases

Author keywords

[No Author keywords available]

Indexed keywords

MICROORGANISM PROTEIN; SERINE PROTEINASE INHIBITOR;

EID: 0033567081     PISSN: 00064971     EISSN: None     Source Type: Journal    
DOI: 10.1182/blood.v94.4.1418     Document Type: Article
Times cited : (109)

References (57)
  • 1
    • 0028206262 scopus 로고
    • The serpin superfamily of proteinase inhibitors: Structure, function, and regulation
    • Potempa J, Korzus E, Travis J: The serpin superfamily of proteinase inhibitors: Structure, function, and regulation. J Biol Chem 269:15957, 1994
    • (1994) J Biol Chem , vol.269 , pp. 15957
    • Potempa, J.1    Korzus, E.2    Travis, J.3
  • 2
    • 0025936528 scopus 로고
    • Mobile reactive centre of serpins and the control of thrombosis
    • Carrell R, Evans DL, Stein PE: Mobile reactive centre of serpins and the control of thrombosis. Nature 353:576, 1991
    • (1991) Nature , vol.353 , pp. 576
    • Carrell, R.1    Evans, D.L.2    Stein, P.E.3
  • 3
    • 0026331304 scopus 로고
    • Basic and clinical aspects of fibrinolysis and thrombolysis
    • Collen D, Lijnen HR: Basic and clinical aspects of fibrinolysis and thrombolysis. Blood 78:3114, 1991
    • (1991) Blood , vol.78 , pp. 3114
    • Collen, D.1    Lijnen, H.R.2
  • 6
    • 0029745109 scopus 로고    scopus 로고
    • The serpin PAI-1 inhibits cell migration by blocking integrin alpha V beta 3 binding to vitronectin
    • Stefansson S, Lawrence DA: The serpin PAI-1 inhibits cell migration by blocking integrin alpha V beta 3 binding to vitronectin. Nature 383:441, 1996
    • (1996) Nature , vol.383 , pp. 441
    • Stefansson, S.1    Lawrence, D.A.2
  • 7
    • 0028874970 scopus 로고
    • Plasminogen activator inhibitor type 2 inhibits tumor necrosis factor α-induced apoptosis. Evidence for an alternate biological function
    • Dickinson JL, Bates EJ, Ferrante A, Antalis TM: Plasminogen activator inhibitor type 2 inhibits tumor necrosis factor α-induced apoptosis. Evidence for an alternate biological function. J Biol Chem 270:27894, 1995
    • (1995) J Biol Chem , vol.270 , pp. 27894
    • Dickinson, J.L.1    Bates, E.J.2    Ferrante, A.3    Antalis, T.M.4
  • 8
    • 0026726631 scopus 로고
    • Virus proteins that counteract host immune defenses
    • Gooding LR: Virus proteins that counteract host immune defenses. Cell 71:5, 1992
    • (1992) Cell , vol.71 , pp. 5
    • Gooding, L.R.1
  • 9
    • 0027438948 scopus 로고
    • Immunological modulation and evasion by helminth parasites in human populations
    • Maizels RM, Bundy DAP, Selkirk ME, Smith DF, Anderson RM: Immunological modulation and evasion by helminth parasites in human populations. Nature 365:797, 1993
    • (1993) Nature , vol.365 , pp. 797
    • Maizels, R.M.1    Bundy, D.A.P.2    Selkirk, M.E.3    Smith, D.F.4    Anderson, R.M.5
  • 11
    • 0029839388 scopus 로고    scopus 로고
    • Characterization of a myxoma virus-encoded serpin-like protein with activity against interleukin-1 β-converting enzyme
    • Petit F, Bertagnoli S, Gelfi J, Fassy F, Boucraut-Baralon C, Milon A: Characterization of a myxoma virus-encoded serpin-like protein with activity against interleukin-1 β-converting enzyme. J Virol 70: 5860, 1996
    • (1996) J Virol , vol.70 , pp. 5860
    • Petit, F.1    Bertagnoli, S.2    Gelfi, J.3    Fassy, F.4    Boucraut-Baralon, C.5    Milon, A.6
  • 12
    • 0031052956 scopus 로고    scopus 로고
    • Vaccinia virus serpin B13R (SPI-2) inhibits interleukin-1β-converting enzyme and protects virus-infected cells from TNF-and Fas-mediated apoptosis, but does not prevent IL-1β-induced fever
    • Kettle S, Alcami A, Khanna A, Ehret R, Jassoy C, Smith GL: Vaccinia virus serpin B13R (SPI-2) inhibits interleukin-1β-converting enzyme and protects virus-infected cells from TNF-and Fas-mediated apoptosis, but does not prevent IL-1β-induced fever. J Gen Virol 78:677, 1997
    • (1997) J Gen Virol , vol.78 , pp. 677
    • Kettle, S.1    Alcami, A.2    Khanna, A.3    Ehret, R.4    Jassoy, C.5    Smith, G.L.6
  • 13
    • 0028955325 scopus 로고
    • Granzyme B is inhibited by the cowpox virus serpin cytokine response modifier A
    • Quan LT, Caputo A, Bleackley RC, Pickup DJ, Salvesen GS: Granzyme B is inhibited by the cowpox virus serpin cytokine response modifier A. J Biol Chem 270:10377, 1995
    • (1995) J Biol Chem , vol.270 , pp. 10377
    • Quan, L.T.1    Caputo, A.2    Bleackley, R.C.3    Pickup, D.J.4    Salvesen, G.S.5
  • 14
    • 0029834497 scopus 로고    scopus 로고
    • CrmA expression in T lymphocytes of transgenic mice inhibits CD95 (Fas/APO-1)-transduced apoptosis, but does not cause lymphadenopathy or autoimmune disease
    • Smith KG, Strasser A, Vaux DL: CrmA expression in T lymphocytes of transgenic mice inhibits CD95 (Fas/APO-1)-transduced apoptosis, but does not cause lymphadenopathy or autoimmune disease. EMBO J 15:5167, 1996
    • (1996) EMBO J , vol.15 , pp. 5167
    • Smith, K.G.1    Strasser, A.2    Vaux, D.L.3
  • 15
    • 0022978276 scopus 로고
    • Interleukin inhibition by a parasite proteinase inhibitor, taeniaestatin
    • Leid RW, Suquet CM, Bouwer HGA, Hinrichs DJ: Interleukin inhibition by a parasite proteinase inhibitor, taeniaestatin. J Immunol 137:2700, 1986
    • (1986) J Immunol , vol.137 , pp. 2700
    • Leid, R.W.1    Suquet, C.M.2    Bouwer, H.G.A.3    Hinrichs, D.J.4
  • 16
    • 0029014045 scopus 로고
    • Ancylostoma caninum anticoagulant peptide: A hookworm-derived inhibitor of human coagulation factor Xa
    • Cappello M, Vlasuk GP, Bergum P, Hunag S, Hotez PJ: Ancylostoma caninum anticoagulant peptide: A hookworm-derived inhibitor of human coagulation factor Xa. Proc Natl Acad Sci USA 92:6152, 1995
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 6152
    • Cappello, M.1    Vlasuk, G.P.2    Bergum, P.3    Hunag, S.4    Hotez, P.J.5
  • 17
    • 0030249127 scopus 로고    scopus 로고
    • Ancylostoma caninum anticoagulant peptide: Cloning by PCR and expression of soluble, active protein in E. Coli
    • Cappello M, Hawdon JM, Jones BF, Kennedy WP, Hotez PJ: Ancylostoma caninum anticoagulant peptide: Cloning by PCR and expression of soluble, active protein in E. coli. Mol Biochem Parasitol 80:113, 1996
    • (1996) Mol Biochem Parasitol , vol.80 , pp. 113
    • Cappello, M.1    Hawdon, J.M.2    Jones, B.F.3    Kennedy, W.P.4    Hotez, P.J.5
  • 19
    • 0026587182 scopus 로고
    • Antigen processing for presentation by class II major histocompatibility complex requires cleavage by cathepsin E
    • Bennett K, Levine T, Ellis JS, Peanasky RJ, Samlogg IM, Kay J, Chain BM: Antigen processing for presentation by class II major histocompatibility complex requires cleavage by cathepsin E. Eur J Immunol 22:1519, 1992
    • (1992) Eur J Immunol , vol.22 , pp. 1519
    • Bennett, K.1    Levine, T.2    Ellis, J.S.3    Peanasky, R.J.4    Samlogg, I.M.5    Kay, J.6    Chain, B.M.7
  • 21
    • 0029962945 scopus 로고    scopus 로고
    • Re-assessing the global prevalence and distribution of lymphatic filariasis
    • Michael E, Bundy DAP, Grenfell BT: Re-assessing the global prevalence and distribution of lymphatic filariasis. Parasitology 112: 409, 1996
    • (1996) Parasitology , vol.112 , pp. 409
    • Michael, E.1    Bundy, D.A.P.2    Grenfell, B.T.3
  • 22
    • 0028089035 scopus 로고
    • Characterization of a native and recombinant schistosoma haematobium serine protease inhibitor gene product
    • Blanton RE, Licate LS, Aman RA: Characterization of a native and recombinant Schistosoma haematobium serine protease inhibitor gene product. Mol Biochem Parasitol 63:1, 1994
    • (1994) Mol Biochem Parasitol , vol.63 , pp. 1
    • Blanton, R.E.1    Licate, L.S.2    Aman, R.A.3
  • 23
    • 0028948124 scopus 로고
    • Molecular cloning of a serine proteinase inhibitor from Brugia malayi
    • Yenbutr P, Scott AL: Molecular cloning of a serine proteinase inhibitor from Brugia malayi. Infect Immunity 63:1745, 1995
    • (1995) Infect Immunity , vol.63 , pp. 1745
    • Yenbutr, P.1    Scott, A.L.2
  • 25
    • 0030050801 scopus 로고    scopus 로고
    • APC from mice harbouring the filarial nematode, Brugia malayi, prevent cellular proliferation but not cytokine production
    • Allen JE, Lawrence RA, Maizels RM: APC from mice harbouring the filarial nematode, Brugia malayi, prevent cellular proliferation but not cytokine production. Int Immunol 8:143, 1996
    • (1996) Int Immunol , vol.8 , pp. 143
    • Allen, J.E.1    Lawrence, R.A.2    Maizels, R.M.3
  • 26
    • 0028844443 scopus 로고
    • The filarial genome network
    • Blaxter ML: The filarial genome network. Parasitol Today 11:441, 1995
    • (1995) Parasitol Today , vol.11 , pp. 441
    • Blaxter, M.L.1
  • 28
    • 0030741671 scopus 로고    scopus 로고
    • Differentially expressed, abundant trans-spliced cDNAs from larval Brugia malayi
    • Gregory WF, Blaxter ML, Maizels RM: Differentially expressed, abundant trans-spliced cDNAs from larval Brugia malayi. Mol Biochem Parasitol 87:85, 1997
    • (1997) Mol Biochem Parasitol , vol.87 , pp. 85
    • Gregory, W.F.1    Blaxter, M.L.2    Maizels, R.M.3
  • 29
    • 0027399530 scopus 로고
    • Identification of protein coding regions by database similarity search
    • Gish W, States DJ: Identification of protein coding regions by database similarity search. Nat Genet 3:266, 1993
    • (1993) Nat Genet , vol.3 , pp. 266
    • Gish, W.1    States, D.J.2
  • 31
    • 0031012783 scopus 로고    scopus 로고
    • Characterization and functional analysis of 12 naturally occurring reactive site variants of serpin-1 from Manduca sexta
    • Jiang H, Kanost MR: Characterization and functional analysis of 12 naturally occurring reactive site variants of serpin-1 from Manduca sexta. J Biol Chem 272:1082, 1997
    • (1997) J Biol Chem , vol.272 , pp. 1082
    • Jiang, H.1    Kanost, M.R.2
  • 32
    • 0032488988 scopus 로고    scopus 로고
    • Different endosomal proteolysis requirements for antigen processing of two T-cell epitopes of the M5 protein from viable streptococcus pyogenes
    • Delvig AA, Robinson JH: Different endosomal proteolysis requirements for antigen processing of two T-cell epitopes of the M5 protein from viable Streptococcus pyogenes. J Biol Chem 273:3291, 1998
    • (1998) J Biol Chem , vol.273 , pp. 3291
    • Delvig, A.A.1    Robinson, J.H.2
  • 33
    • 0000461349 scopus 로고    scopus 로고
    • RNA processing and gene structure
    • Riddle DL, Blumenthal T, Meyer BJ, Priess JR (eds): Cold Spring Harbor, NY, Cold Spring Harbor Laboratory
    • Blumenthal T, Steward K: RNA processing and gene structure, in Riddle DL, Blumenthal T, Meyer BJ, Priess JR (eds): C.elegans II. Cold Spring Harbor, NY, Cold Spring Harbor Laboratory, 1997, p 117
    • (1997) C.Elegans II , pp. 117
    • Blumenthal, T.1    Steward, K.2
  • 34
    • 0025102251 scopus 로고
    • Nuclear pre-mRNA introns: Analysis and comparison of intron sequences from Tetrahymena thermophila and other eukaryotes
    • Csank C, Taylor FM, Matindale DW: Nuclear pre-mRNA introns: Analysis and comparison of intron sequences from Tetrahymena thermophila and other eukaryotes. Nucleic Acids Res 18:5133, 1990
    • (1990) Nucleic Acids Res , vol.18 , pp. 5133
    • Csank, C.1    Taylor, F.M.2    Matindale, D.W.3
  • 35
    • 0024423930 scopus 로고
    • Implications of the three-dimensional structure of α-1-antitrypsin for structure and function of serpins
    • Huber R, Carrell RW: Implications of the three-dimensional structure of α-1-antitrypsin for structure and function of serpins. Biochemistry 28:8952, 1989
    • (1989) Biochemistry , vol.28 , pp. 8952
    • Huber, R.1    Carrell, R.W.2
  • 37
    • 0020489960 scopus 로고
    • The ovalbumin gene family: Complete sequence and structure of the Y gene
    • Heilig R, Muraskowsky R, Kloepfer C, Mandel JL: The ovalbumin gene family: Complete sequence and structure of the Y gene. Nucleic Acids Res 10:4363, 1982
    • (1982) Nucleic Acids Res , vol.10 , pp. 4363
    • Heilig, R.1    Muraskowsky, R.2    Kloepfer, C.3    Mandel, J.L.4
  • 38
    • 0029029157 scopus 로고
    • Gene structure, chromosomal localization, and expression of the murine homologue of human proteinase inhibitor 6 (PI-6) suggests divergence of PI-6 from the ovalbumin serpins
    • Sun J, Rose JB, Bird P: Gene structure, chromosomal localization, and expression of the murine homologue of human proteinase inhibitor 6 (PI-6) suggests divergence of PI-6 from the ovalbumin serpins. J Biol Chem 270:16089, 1995
    • (1995) J Biol Chem , vol.270 , pp. 16089
    • Sun, J.1    Rose, J.B.2    Bird, P.3
  • 39
    • 0031008162 scopus 로고    scopus 로고
    • A new family of 10 murine ovalbumin serpins includes two homologs of proteinase inhibitor 8 and two homologs of the granzyme B inhibitor (proteinase inhibitor 9)
    • Sun J, Ooms L, Bird CH, Sutton VR, Trapani JA, Bird PI: A new family of 10 murine ovalbumin serpins includes two homologs of proteinase inhibitor 8 and two homologs of the granzyme B inhibitor (proteinase inhibitor 9). J Biol Chem 272:15434, 1997
    • (1997) J Biol Chem , vol.272 , pp. 15434
    • Sun, J.1    Ooms, L.2    Bird, C.H.3    Sutton, V.R.4    Trapani, J.A.5    Bird, P.I.6
  • 40
    • 0021747157 scopus 로고
    • Human α1-proteinase inhibitor. Crystal structure analysis of two crystal modifications, molecular model and preliminary analysis of the implications for function
    • Loebermann H, Tokuoka R, Diesenhofer J, Huber R: Human α1-proteinase inhibitor. Crystal structure analysis of two crystal modifications, molecular model and preliminary analysis of the implications for function. J Mol Biol 177:531, 1984
    • (1984) J Mol Biol , vol.177 , pp. 531
    • Loebermann, H.1    Tokuoka, R.2    Diesenhofer, J.3    Huber, R.4
  • 42
    • 0028773279 scopus 로고
    • Biological implications of a 3 A structure of dimeric antithrombin
    • Carrell R, Stein PE, Fermi G, Wardell MR: Biological implications of a 3 A structure of dimeric antithrombin. Structure 2:257, 1994
    • (1994) Structure , vol.2 , pp. 257
    • Carrell, R.1    Stein, P.E.2    Fermi, G.3    Wardell, M.R.4
  • 43
    • 0024967250 scopus 로고
    • The AU-rich sequences present in the introns of plant nuclear pre-mRNAs are required for splicing
    • Goodall GJ, Filipowicz W: The AU-rich sequences present in the introns of plant nuclear pre-mRNAs are required for splicing. Cell 58:473, 1989
    • (1989) Cell , vol.58 , pp. 473
    • Goodall, G.J.1    Filipowicz, W.2
  • 44
    • 0030425648 scopus 로고    scopus 로고
    • Molecular evidence for deep precambrian divergences amony metazoan phyla
    • Wray GA, Levinton JS, Shapiro LH: Molecular evidence for deep precambrian divergences amony metazoan phyla. Science 274: 568, 1996
    • (1996) Science , vol.274 , pp. 568
    • Wray, G.A.1    Levinton, J.S.2    Shapiro, L.H.3
  • 45
    • 0023812882 scopus 로고
    • The organization of the human-plasminogen-activator-inhibitor-1 gene. Implications on the evolution of the serine-protease inhibitor family
    • Strandberg L, Lawrence D, Ny T: The organization of the human-plasminogen-activator-inhibitor-1 gene. Implications on the evolution of the serine-protease inhibitor family. Eur J Biochem 176:609, 1988
    • (1988) Eur J Biochem , vol.176 , pp. 609
    • Strandberg, L.1    Lawrence, D.2    Ny, T.3
  • 48
    • 0027925921 scopus 로고
    • Evolutionary relationships among the serpins
    • Marshall CJ: Evolutionary relationships among the serpins. Phil Trans R Soc Lond Series B 342:101, 1993
    • (1993) Phil Trans R Soc Lond Series B , vol.342 , pp. 101
    • Marshall, C.J.1
  • 50
    • 0029589824 scopus 로고
    • What do dysfunctional serpins tell us about molecular mobility and disease?
    • Stein PE, Carrell RW: What do dysfunctional serpins tell us about molecular mobility and disease? Nat Struct Biol 2:96, 1995
    • (1995) Nat Struct Biol , vol.2 , pp. 96
    • Stein, P.E.1    Carrell, R.W.2
  • 52
    • 0031836105 scopus 로고    scopus 로고
    • Mice lacking neutrophil elastase reveal impaired host defense against gram negative bacterial sepsis
    • Belaaouaj A, McCarthy R, Baumann M, Gao Z, Ley TJ, Abraham SN, Shapiro SD: Mice lacking neutrophil elastase reveal impaired host defense against gram negative bacterial sepsis. Nat Med 4:615, 1998
    • (1998) Nat Med , vol.4 , pp. 615
    • Belaaouaj, A.1    McCarthy, R.2    Baumann, M.3    Gao, Z.4    Ley, T.J.5    Abraham, S.N.6    Shapiro, S.D.7
  • 53
    • 0028136620 scopus 로고
    • Interleukin-8 processing by neutrophil elastase, cathepsin G and proteinase-3
    • Padrines M, Wolf M, Walz A, Baggiolini M: Interleukin-8 processing by neutrophil elastase, cathepsin G and proteinase-3. FEBS Lett 352:231, 1994
    • (1994) FEBS Lett , vol.352 , pp. 231
    • Padrines, M.1    Wolf, M.2    Walz, A.3    Baggiolini, M.4
  • 54
    • 0031056611 scopus 로고    scopus 로고
    • Cathepsin G binds to human lymphocytes
    • Yamazaki T, Aoki Y: Cathepsin G binds to human lymphocytes. J Leukoc Biol 61:73, 1997
    • (1997) J Leukoc Biol , vol.61 , pp. 73
    • Yamazaki, T.1    Aoki, Y.2
  • 55
    • 0030866891 scopus 로고    scopus 로고
    • Identification of human neutrophil-derived cathepsin g and azurocidin/CAP37 as chemoattractants for mononuclear cells and neutrophils
    • Chertov O, Ueda H, Xu LL, Tani K, Murphy WJ, Wang JM, Howard OMZ, Sayers TJ, Oppenheim JJ: Identification of human neutrophil-derived cathepsin G and azurocidin/CAP37 as chemoattractants for mononuclear cells and neutrophils. J Exp Med 186:739, 1997
    • (1997) J Exp Med , vol.186 , pp. 739
    • Chertov, O.1    Ueda, H.2    Xu, L.L.3    Tani, K.4    Murphy, W.J.5    Wang, J.M.6    Howard, O.M.Z.7    Sayers, T.J.8    Oppenheim, J.J.9
  • 56
    • 0028961449 scopus 로고
    • Stimulation of human lymphocytes by cathepsin G
    • Hase-Yamazaki T, Aoki Y: Stimulation of human lymphocytes by cathepsin G. Cell Immunol 160:24, 1995
    • (1995) Cell Immunol , vol.160 , pp. 24
    • Hase-Yamazaki, T.1    Aoki, Y.2
  • 57
    • 0031032401 scopus 로고    scopus 로고
    • Squamous cell carcinoma antigen 2 is a novel serpin that inhibits the chymotrypsin-like proteinases cathepsin G and mast cell chymase
    • Schick C, Kamachi Y, Bartuski AJ, Cataltepe S, Schechter NM, Pemberton PA, Silverman GA: Squamous cell carcinoma antigen 2 is a novel serpin that inhibits the chymotrypsin-like proteinases cathepsin G and mast cell chymase. J Biol Chem 272:1849, 1997
    • (1997) J Biol Chem , vol.272 , pp. 1849
    • Schick, C.1    Kamachi, Y.2    Bartuski, A.J.3    Cataltepe, S.4    Schechter, N.M.5    Pemberton, P.A.6    Silverman, G.A.7


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