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Volumn 114, Issue 1, 2001, Pages 111-117

In vitro cytocidal effects on Trypanosoma brucei and inhibition of Leishmania major GP63 by peptidomimetic metalloprotease inhibitors

Author keywords

GP63; Leishmania; Metalloprotease; Peptidomimetic; Trypanosomes

Indexed keywords

BB 3103; BRL 29808; BRL 48226; BRL 49244; BRL 54525; BRL 57240; CAPTOPRIL; CERANAPRIL; ENALAPRILAT; FOSINOPRILAT; GLYCOPROTEIN; LEISHMANOLYSIN; MEMBRANE PROTEIN; METALLOPROTEINASE; METALLOPROTEINASE INHIBITOR; PENTOPRILAT; PHOSPHORAMIDON; RENTIAPRIL; SB 201140; SB 202968Z; SB 227961; SB 227962; THIORPHAN; UNCLASSIFIED DRUG; VARIANT SURFACE GLYCOPROTEIN; ZINCOV;

EID: 0035946347     PISSN: 01666851     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0166-6851(01)00244-4     Document Type: Article
Times cited : (41)

References (33)
  • 3
    • 0005146309 scopus 로고    scopus 로고
    • Overview of the biological roles of metalloproteinases in health and disease
    • K.M.K. Bottomley, D. Bradshaw, & J.S. Nixon. Basel: Birkhauser Verlag
    • Hooper N.M. Overview of the biological roles of metalloproteinases in health and disease. Bottomley K.M.K., Bradshaw D., Nixon J.S. Metalloproteinases as targets for anti-inflammatory drugs. 1999;145-161 Birkhauser Verlag, Basel.
    • (1999) Metalloproteinases As Targets for Anti-inflammatory Drugs , pp. 145-161
    • Hooper, N.M.1
  • 5
    • 0027466501 scopus 로고
    • Evolution and Expression of the Leishmania surface proteinase (gp63) gene locus
    • Medina-Acosta E., Beverley S.M., Russell D.G. Evolution and Expression of the Leishmania surface proteinase (gp63) gene locus. Infect. Agents. and. Dis. 2:1993;25-34.
    • (1993) Infect. Agents. And. Dis. , vol.2 , pp. 25-34
    • Medina-Acosta, E.1    Beverley, S.M.2    Russell, D.G.3
  • 6
    • 0029038660 scopus 로고
    • Leishmanolysin: Surface metalloproteinase of Leishmania
    • Bouvier J., Schneider P., Etges R. Leishmanolysin: surface metalloproteinase of Leishmania. Methods Enzymol. 248:1995;614-633.
    • (1995) Methods Enzymol. , vol.248 , pp. 614-633
    • Bouvier, J.1    Schneider, P.2    Etges, R.3
  • 7
    • 0032529002 scopus 로고    scopus 로고
    • The crystal structure of the Leishmania major surface proteinase leishmanolysin (gp63)
    • Schlagenhauf E., Etges R., Metcalf P. The crystal structure of the Leishmania major surface proteinase leishmanolysin (gp63). Structure. 6:1998;1035-1046.
    • (1998) Structure , vol.6 , pp. 1035-1046
    • Schlagenhauf, E.1    Etges, R.2    Metcalf, P.3
  • 8
    • 0024268165 scopus 로고
    • Genes encoding the major surface glycoprotein in Leishmania are tandemly linked at a single chromosomal locus and are constitutively expressed
    • Button L.L., Russel D.G., Klein H.L., Medina-Acosta E., Karess R.E., McMaster W.R. Genes encoding the major surface glycoprotein in Leishmania are tandemly linked at a single chromosomal locus and are constitutively expressed. Mol. Biochem. Parasitol. 32:1989;271-284.
    • (1989) Mol. Biochem. Parasitol. , vol.32 , pp. 271-284
    • Button, L.L.1    Russel, D.G.2    Klein, H.L.3    Medina-Acosta, E.4    Karess, R.E.5    McMaster, W.R.6
  • 9
    • 0027472098 scopus 로고
    • Structurally distinct genes for the surface protease of Leishmania mexicana are developmentally regulated
    • Medina-Acosta E., Karess R.E., Russell D.G. Structurally distinct genes for the surface protease of Leishmania mexicana are developmentally regulated. Mol. Biochem. Parasitol. 57:1993;31-46.
    • (1993) Mol. Biochem. Parasitol. , vol.57 , pp. 31-46
    • Medina-Acosta, E.1    Karess, R.E.2    Russell, D.G.3
  • 11
    • 0026598731 scopus 로고
    • Three distinct RNAs for the surface protease gp63 are differentially expressed during development of Leishmania donovani chagasi promastigotes to an infectious form
    • Ramamoorthy R., Donelson J.E., Paetz K.E., Maybodi M., Roberts S.C., Wilson M.E. Three distinct RNAs for the surface protease gp63 are differentially expressed during development of Leishmania donovani chagasi promastigotes to an infectious form. J. Biol. Chem. 267:1992;1888-1895.
    • (1992) J. Biol. Chem. , vol.267 , pp. 1888-1895
    • Ramamoorthy, R.1    Donelson, J.E.2    Paetz, K.E.3    Maybodi, M.4    Roberts, S.C.5    Wilson, M.E.6
  • 12
    • 0032523872 scopus 로고    scopus 로고
    • Differentially expressed Leishmania major gp63 genes encode cell surface leishmanolysin with distinct signals for glycosyphosphatidylinositol attachment
    • Voth B.V., Kelly B.L., Joshi P.B., Ivens A.C., McMaster W.R. Differentially expressed Leishmania major gp63 genes encode cell surface leishmanolysin with distinct signals for glycosyphosphatidylinositol attachment. Mole. Biochem. Parasitol. 93:1998;31-41.
    • (1998) Mole. Biochem. Parasitol. , vol.93 , pp. 31-41
    • Voth, B.V.1    Kelly, B.L.2    Joshi, P.B.3    Ivens, A.C.4    McMaster, W.R.5
  • 13
    • 0024439986 scopus 로고
    • The promastigote surface protease (gp63) of Leishmania is expressed but differentially processed and localized in the amastigote stage
    • Medina-Acosta E., Karess R.E., Schwarz H., Russell D.G. The promastigote surface protease (gp63) of Leishmania is expressed but differentially processed and localized in the amastigote stage. Mole. Biochem. Parasitol. 37:1989;263-273.
    • (1989) Mole. Biochem. Parasitol. , vol.37 , pp. 263-273
    • Medina-Acosta, E.1    Karess, R.E.2    Schwarz, H.3    Russell, D.G.4
  • 14
  • 15
    • 0028142227 scopus 로고
    • Genetic rescue of surface metalloproteinase (GP63)-deficiency in Leishmania amazonensis variants increases their infection of macrophages in the early phase
    • McGuire B., Chang K.-P. Genetic rescue of surface metalloproteinase (GP63)-deficiency in Leishmania amazonensis variants increases their infection of macrophages in the early phase. Mole. Biochem. Parasitol. 66:1994;345-347.
    • (1994) Mole. Biochem. Parasitol. , vol.66 , pp. 345-347
    • McGuire, B.1    Chang, K.-P.2
  • 16
    • 0023726598 scopus 로고
    • Complement receptor type 3 (CR3) binds to an Arg-Gly-Asp-containing region on the major surface glycoprotein, gp63, of leishmania promastigotes
    • Russell D.G., Wright S.D. Complement receptor type 3 (CR3) binds to an Arg-Gly-Asp-containing region on the major surface glycoprotein, gp63, of leishmania promastigotes. J. Exp. Med. 168:1988;279-292.
    • (1988) J. Exp. Med. , vol.168 , pp. 279-292
    • Russell, D.G.1    Wright, S.D.2
  • 17
    • 0029046678 scopus 로고
    • Role of Leishmania surface protease GP63 in complement fixation, cell adhesion, and resistance to complement-mediated lysis
    • Brittingham A., Morrison C.J., McMaster W.R., McGuire B.S., Chang K.-P., Mosser D.M. Role of Leishmania surface protease GP63 in complement fixation, cell adhesion, and resistance to complement-mediated lysis. J. Immunol. 155:1995;3102-3111.
    • (1995) J. Immunol. , vol.155 , pp. 3102-3111
    • Brittingham, A.1    Morrison, C.J.2    McMaster, W.R.3    McGuire, B.S.4    Chang, K.-P.5    Mosser, D.M.6
  • 19
    • 0031984118 scopus 로고    scopus 로고
    • Targeted gene deletion of Leishmania major genes encoding developmental stage-specific leishmanolysin (GP63)
    • Joshi P.B., Sacks D.L., Modi G., McMaster W.R. Targeted gene deletion of Leishmania major genes encoding developmental stage-specific leishmanolysin (GP63). Mol. Microbiol. 27:1998;519-530.
    • (1998) Mol. Microbiol. , vol.27 , pp. 519-530
    • Joshi, P.B.1    Sacks, D.L.2    Modi, G.3    McMaster, W.R.4
  • 20
    • 0033966027 scopus 로고    scopus 로고
    • Episomal expression of specific sense and antisense mRNAs in Leishmania amazonensis: Modulation of gp63 level in promastigotes and their infection of macrophages in vitro
    • Chen D.-Q., Kolli B.K., Yadava N., Lu H.G., Gilman-Sacks A., Peterson D.A., Chang K.-P. Episomal expression of specific sense and antisense mRNAs in Leishmania amazonensis: modulation of gp63 level in promastigotes and their infection of macrophages in vitro. Infect. Immun. 68:2000;80-86.
    • (2000) Infect. Immun. , vol.68 , pp. 80-86
    • Chen, D.-Q.1    Kolli, B.K.2    Yadava, N.3    Lu, H.G.4    Gilman-Sacks, A.5    Peterson, D.A.6    Chang, K.-P.7
  • 21
    • 0030791382 scopus 로고    scopus 로고
    • Expression of bloodstream variant surface glycoproteins in procyclic stage Trypanosoma brucei: Role of GPI anchors in secretion
    • Bangs J.D., Ransom D.M., McDowell M.A., Brouch E.M. Expression of bloodstream variant surface glycoproteins in procyclic stage Trypanosoma brucei: role of GPI anchors in secretion. EMBO. J. 16:1997;4285-4294.
    • (1997) EMBO. J. , vol.16 , pp. 4285-4294
    • Bangs, J.D.1    Ransom, D.M.2    McDowell, M.A.3    Brouch, E.M.4
  • 22
    • 0016809286 scopus 로고
    • Identification, purification and properties of clone-specific glycoprotein antigens constituting the surface coat of Trypanosoma brucei
    • Cross G.A.M. Identification, purification and properties of clone-specific glycoprotein antigens constituting the surface coat of Trypanosoma brucei. Parasitol. 71:1975;393-417.
    • (1975) Parasitol , vol.71 , pp. 393-417
    • Cross, G.A.M.1
  • 23
    • 0027314162 scopus 로고
    • Proteolytic release of cell surface proteins during differentiation of Trypanosoma brucei
    • Ziegelbauer K., Stahl B., Karas M., Stierhof Y.-D., Overath P. Proteolytic release of cell surface proteins during differentiation of Trypanosoma brucei. Biochem. 32:1993;3737-3742.
    • (1993) Biochem , vol.32 , pp. 3737-3742
    • Ziegelbauer, K.1    Stahl, B.2    Karas, M.3    Stierhof, Y.-D.4    Overath, P.5
  • 24
    • 0030664774 scopus 로고    scopus 로고
    • African trypanosomes have differentially expressed genes encoding homologues of Leishmania GP63 surface protease
    • El-Sayed N.M.A., Donelson J.E. African trypanosomes have differentially expressed genes encoding homologues of Leishmania GP63 surface protease. J. Biol. Chem. 272:1997;26742-26748.
    • (1997) J. Biol. Chem. , vol.272 , pp. 26742-26748
    • El-Sayed, N.M.A.1    Donelson, J.E.2
  • 25
    • 0029764290 scopus 로고    scopus 로고
    • A soluble secretory reporter system in Trypanosoma brucei: Studies on endoplasmic reticulum targeting
    • Bangs J.D., Brouch E.M., Ransom D.M., Roggy J.L. A soluble secretory reporter system in Trypanosoma brucei: studies on endoplasmic reticulum targeting. J. Biol. Chem. 271:1996;18387-18393.
    • (1996) J. Biol. Chem. , vol.271 , pp. 18387-18393
    • Bangs, J.D.1    Brouch, E.M.2    Ransom, D.M.3    Roggy, J.L.4
  • 26
    • 0024948840 scopus 로고
    • Continuous cultivation of Trypanosoma brucei blood stream forms in a medium containing a low concentration of serum protein without feeder cell layers
    • Hirumi H., Hirumi K. Continuous cultivation of Trypanosoma brucei blood stream forms in a medium containing a low concentration of serum protein without feeder cell layers. J. Parasitol. 75:1989;985-989.
    • (1989) J. Parasitol. , vol.75 , pp. 985-989
    • Hirumi, H.1    Hirumi, K.2
  • 27
    • 0023025407 scopus 로고
    • The effect of citrate/cis-aconitate on oxidative metabolism during transformation of Trypanosoma brucei
    • Overath P., Czichos J., Hass C. The effect of citrate/cis-aconitate on oxidative metabolism during transformation of Trypanosoma brucei. Eur. J. Biochem. 160:1986;175-182.
    • (1986) Eur. J. Biochem. , vol.160 , pp. 175-182
    • Overath, P.1    Czichos, J.2    Hass, C.3
  • 28
    • 0027941838 scopus 로고
    • Families of zinc metalloproteases
    • Hooper N.M. Families of zinc metalloproteases. FEBS. Lett. 354:1994;1-6.
    • (1994) FEBS. Lett. , vol.354 , pp. 1-6
    • Hooper, N.M.1
  • 29
    • 0030659835 scopus 로고    scopus 로고
    • Angiotensin-converting enzyme secretase is inhibited by zinc metalloprotease inhibitors and requires its substrate to be inserted in lipid a bilayer
    • Parvathy S., Oppong A.Y., Karran E.H., Buckle D.R., Turner A.J., Hooper N.M. Angiotensin-converting enzyme secretase is inhibited by zinc metalloprotease inhibitors and requires its substrate to be inserted in lipid a bilayer. Biochem. J. 327:1997;37-43.
    • (1997) Biochem. J. , vol.327 , pp. 37-43
    • Parvathy, S.1    Oppong, A.Y.2    Karran, E.H.3    Buckle, D.R.4    Turner, A.J.5    Hooper, N.M.6
  • 30
    • 0026030341 scopus 로고
    • Angiotensin converting enzyme: Implications from molecular biology for its physiological function
    • Hooper N.M. Angiotensin converting enzyme: implications from molecular biology for its physiological function. Int. J. Biochem. 23:1991;641-647.
    • (1991) Int. J. Biochem. , vol.23 , pp. 641-647
    • Hooper, N.M.1
  • 31


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