메뉴 건너뛰기




Volumn 136, Issue 2, 2004, Pages 173-180

Dependence of Giardia lamblia encystation on novel transglutaminase activity

Author keywords

CWP; cyst wall protein; ECM; electron microscopy; EM; encystation secretory vesicle; ER; ESV; extracellular matrix; giardial protein disulfide isomerase; gPDI; high performance liquid chromatography; HPLC; PDI; protein disulfide isomerase; TGase; transglutaminase

Indexed keywords

CYSTAMINE; PEPTIDE DERIVATIVE; PROTEIN DISULFIDE ISOMERASE; PROTEIN GLUTAMINE GAMMA GLUTAMYLTRANSFERASE;

EID: 2942536417     PISSN: 01666851     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molbiopara.2004.03.011     Document Type: Article
Times cited : (32)

References (38)
  • 1
    • 0033984156 scopus 로고    scopus 로고
    • Transglutaminase-catalyzed reactions in the growth, maturation and development of parasitic nematodes
    • Chandrashekar R., Mehta K. Transglutaminase-catalyzed reactions in the growth, maturation and development of parasitic nematodes. Parasitol. Today. 16:2000;11-17
    • (2000) Parasitol. Today , vol.16 , pp. 11-17
    • Chandrashekar, R.1    Mehta, K.2
  • 2
    • 0032866851 scopus 로고    scopus 로고
    • Tissue transglutaminase: An enzyme with a split personality
    • Chen J.S., Mehta K. Tissue transglutaminase: an enzyme with a split personality. Int. J. Biochem. Cell Biol. 31:1999;817-836
    • (1999) Int. J. Biochem. Cell Biol. , vol.31 , pp. 817-836
    • Chen, J.S.1    Mehta, K.2
  • 3
    • 0037317032 scopus 로고    scopus 로고
    • Transglutaminases: Crosslinking enzymes with pleiotropic functions
    • Lorand L., Graham R.M. Transglutaminases: crosslinking enzymes with pleiotropic functions. Nat. Rev. Mol. Cell Biol. 4:2003;140-156
    • (2003) Nat. Rev. Mol. Cell Biol. , vol.4 , pp. 140-156
    • Lorand, L.1    Graham, R.M.2
  • 4
    • 0033230231 scopus 로고    scopus 로고
    • A transglutaminase immunologically related to tissue transglutaminase catalyzes cross-linking of cell wall proteins in Chlamydomonas reinhardtii
    • Waffenschmidt S., Kusch T., Woessner J.P. A transglutaminase immunologically related to tissue transglutaminase catalyzes cross-linking of cell wall proteins in Chlamydomonas reinhardtii. Plant Physiol. 121:1999;1003-1015
    • (1999) Plant Physiol. , vol.121 , pp. 1003-1015
    • Waffenschmidt, S.1    Kusch, T.2    Woessner, J.P.3
  • 5
    • 0034093354 scopus 로고    scopus 로고
    • Protein crosslinking in assembly and remodelling of extracellular matrices: The role of transglutaminases
    • Aeschlimann D., Thomazy V. Protein crosslinking in assembly and remodelling of extracellular matrices: the role of transglutaminases. Connect. Tissue Res. 41:2000;1-27
    • (2000) Connect. Tissue Res. , vol.41 , pp. 1-27
    • Aeschlimann, D.1    Thomazy, V.2
  • 6
    • 0034933985 scopus 로고    scopus 로고
    • Biology of Giardia lamblia
    • Adam R.D. Biology of Giardia lamblia. Clin. Microbiol. Rev. 14:2001;447-475
    • (2001) Clin. Microbiol. Rev. , vol.14 , pp. 447-475
    • Adam, R.D.1
  • 7
    • 0029929221 scopus 로고    scopus 로고
    • Inhibition of Giardia lamblia excystation by antibodies against cyst walls and by wheat germ agglutinin
    • Meng T.C., Hetsko M.L., Gillin F.D. Inhibition of Giardia lamblia excystation by antibodies against cyst walls and by wheat germ agglutinin. Infect. Immun. 64:1996;2151-2157
    • (1996) Infect. Immun. , vol.64 , pp. 2151-2157
    • Meng, T.C.1    Hetsko, M.L.2    Gillin, F.D.3
  • 8
    • 0032032031 scopus 로고    scopus 로고
    • Cellular and transcriptional changes during excystation of Giardia lamblia in vitro
    • Hetsko M.L., McCaffery J.M., Svard S.G., et al. Cellular and transcriptional changes during excystation of Giardia lamblia in vitro. Exp. Parasitol. 88:1998;172-183
    • (1998) Exp. Parasitol. , vol.88 , pp. 172-183
    • Hetsko, M.L.1    McCaffery, J.M.2    Svard, S.G.3
  • 9
    • 0024578388 scopus 로고
    • Identification and localization of cyst-specific antigens of Giardia lamblia
    • Reiner D.S., Douglas H., Gillin F.D. Identification and localization of cyst-specific antigens of Giardia lamblia. Infect. Immun. 57:1989;963-968
    • (1989) Infect. Immun. , vol.57 , pp. 963-968
    • Reiner, D.S.1    Douglas, H.2    Gillin, F.D.3
  • 10
    • 0025010850 scopus 로고
    • Sorting of cyst wall proteins to a regulated secretory pathway during differentiation of the primitive eukaryote, Giardia lamblia
    • Reiner D.S., McCaffery M., Gillin F.D. Sorting of cyst wall proteins to a regulated secretory pathway during differentiation of the primitive eukaryote, Giardia lamblia. Eur. J. Cell Biol. 53:1990;142-153
    • (1990) Eur. J. Cell Biol. , vol.53 , pp. 142-153
    • Reiner, D.S.1    McCaffery, M.2    Gillin, F.D.3
  • 11
    • 0034938382 scopus 로고    scopus 로고
    • Reversible interruption of Giardia lamblia cyst wall protein transport in a novel regulated secretory pathway
    • Reiner D.S., McCaffery J.M., Gillin F.D. Reversible interruption of Giardia lamblia cyst wall protein transport in a novel regulated secretory pathway. Cell Microbiol. 3:2001;459-472
    • (2001) Cell Microbiol. , vol.3 , pp. 459-472
    • Reiner, D.S.1    McCaffery, J.M.2    Gillin, F.D.3
  • 12
    • 0031905860 scopus 로고    scopus 로고
    • An ERp60-like protein from the filarial parasite Dirofilaria immitis has both transglutaminase and protein disulfide isomerase activity
    • Chandrashekar R., Tsuji N., Morales T., et al. An ERp60-like protein from the filarial parasite Dirofilaria immitis has both transglutaminase and protein disulfide isomerase activity. Proc. Natl. Acad. Sci. U.S.A. 95:1998;531-536
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 531-536
    • Chandrashekar, R.1    Tsuji, N.2    Morales, T.3
  • 13
    • 0035663887 scopus 로고    scopus 로고
    • Molecular cloning and expression of Caenorhabditis elegans ERp57-homologue with transglutaminase activity
    • Natsuka S., Takubo R., Seki R., Ikura K. Molecular cloning and expression of Caenorhabditis elegans ERp57-homologue with transglutaminase activity. J. Biochem. (Tokyo). 130:2001;731-735
    • (2001) J. Biochem. (Tokyo) , vol.130 , pp. 731-735
    • Natsuka, S.1    Takubo, R.2    Seki, R.3    Ikura, K.4
  • 14
    • 0033569720 scopus 로고    scopus 로고
    • Novel protein-disulfide isomerases from the early-diverging protist Giardia lamblia
    • Knodler L.A., Noiva R., Mehta K., et al. Novel protein-disulfide isomerases from the early-diverging protist Giardia lamblia. J. Biol. Chem. 274:1999;29805-29811
    • (1999) J. Biol. Chem. , vol.274 , pp. 29805-29811
    • Knodler, L.A.1    Noiva, R.2    Mehta, K.3
  • 15
    • 0034906253 scopus 로고    scopus 로고
    • The evolutionary origins of eukaryotic protein disulfide isomerase domains: New evidence from the amitochondriate protist Giardia lamblia
    • McArthur A.G., Knodler L.A., Silberman J.D., et al. The evolutionary origins of eukaryotic protein disulfide isomerase domains: new evidence from the amitochondriate protist Giardia lamblia. Mol. Biol. Evol. 18:2001;1455-1463
    • (2001) Mol. Biol. Evol. , vol.18 , pp. 1455-1463
    • McArthur, A.G.1    Knodler, L.A.2    Silberman, J.D.3
  • 16
    • 0345505270 scopus 로고    scopus 로고
    • Thioredoxin motif of Caenorhabditis elegans PDI-3 provides Cys and His catalytic residues for transglutaminase activity
    • Blasko B., Madi A., Fesus L. Thioredoxin motif of Caenorhabditis elegans PDI-3 provides Cys and His catalytic residues for transglutaminase activity. Biochem. Biophys. Res. Commun. 303:2003;1142-1147
    • (2003) Biochem. Biophys. Res. Commun. , vol.303 , pp. 1142-1147
    • Blasko, B.1    Madi, A.2    Fesus, L.3
  • 18
    • 0029862978 scopus 로고    scopus 로고
    • Transglutaminase-catalyzed incorporation of host proteins in Brugia malayi microfilariae
    • Mehta K., Chandrashekar R., Rao U.R. Transglutaminase-catalyzed incorporation of host proteins in Brugia malayi microfilariae. Mol. Biochem. Parasitol. 76:1996;105-114
    • (1996) Mol. Biochem. Parasitol. , vol.76 , pp. 105-114
    • Mehta, K.1    Chandrashekar, R.2    Rao, U.R.3
  • 19
    • 0034788583 scopus 로고    scopus 로고
    • Transglutaminase in Plasmodium parasites: Activity and putative role in oocysts and blood stages
    • Adini A., Krugliak M., Ginsburg H., et al. Transglutaminase in Plasmodium parasites: activity and putative role in oocysts and blood stages. Mol. Biochem. Parasitol. 117:2001;161-168
    • (2001) Mol. Biochem. Parasitol. , vol.117 , pp. 161-168
    • Adini, A.1    Krugliak, M.2    Ginsburg, H.3
  • 20
    • 0028954114 scopus 로고
    • Developmentally regulated expression of a Giardia lamblia cyst wall protein gene
    • Mowatt M.R., Lujan H.D., Cotten D.B., et al. Developmentally regulated expression of a Giardia lamblia cyst wall protein gene. Mol. Microbiol. 15:1995;955-963
    • (1995) Mol. Microbiol. , vol.15 , pp. 955-963
    • Mowatt, M.R.1    Lujan, H.D.2    Cotten, D.B.3
  • 21
    • 0028882358 scopus 로고
    • Identification of a novel Giardia lamblia cyst wall protein with leucine-rich repeats. Implications for secretory granule formation and protein assembly into the cyst wall
    • Lujan H.D., Mowatt M.R., Conrad J.T., et al. Identification of a novel Giardia lamblia cyst wall protein with leucine-rich repeats. Implications for secretory granule formation and protein assembly into the cyst wall. J. Biol. Chem. 270:1995;29307-29313
    • (1995) J. Biol. Chem. , vol.270 , pp. 29307-29313
    • Lujan, H.D.1    Mowatt, M.R.2    Conrad, J.T.3
  • 22
    • 0037484284 scopus 로고    scopus 로고
    • Mining the Giardia lamblia genome for new cyst wall proteins
    • Sun C.H., McCaffery J.M., Reiner D.S., Gillin F.D. Mining the Giardia lamblia genome for new cyst wall proteins. J. Biol. Chem. 278:2003;21701-21708
    • (2003) J. Biol. Chem. , vol.278 , pp. 21701-21708
    • Sun, C.H.1    McCaffery, J.M.2    Reiner, D.S.3    Gillin, F.D.4
  • 23
    • 0036434922 scopus 로고    scopus 로고
    • A novel Myb-related protein involved in transcriptional activation of encystation genes in Giardia lamblia
    • Sun C.H., Palm D., McArthur A.G., et al. A novel Myb-related protein involved in transcriptional activation of encystation genes in Giardia lamblia. Mol. Microbiol. 46:2002;971-984
    • (2002) Mol. Microbiol. , vol.46 , pp. 971-984
    • Sun, C.H.1    Palm, D.2    McArthur, A.G.3
  • 24
    • 0025196159 scopus 로고
    • Determination of epsilon (gamma-glutamyl)lysine crosslink in proteins using phenylisothiocyanate derivatization and high-pressure liquid chromatographic separation
    • Tarcsa E., Fesus L. Determination of epsilon (gamma-glutamyl)lysine crosslink in proteins using phenylisothiocyanate derivatization and high-pressure liquid chromatographic separation. Anal. Biochem. 186:1990;135-140
    • (1990) Anal. Biochem. , vol.186 , pp. 135-140
    • Tarcsa, E.1    Fesus, L.2
  • 25
    • 0028322002 scopus 로고
    • Recognition of Giardia lamblia cyst-specific antigens by monoclonal antibodies
    • Campbell J.D., Faubert G.M. Recognition of Giardia lamblia cyst-specific antigens by monoclonal antibodies. Parasite Immunol. 16:1994;211-219
    • (1994) Parasite Immunol. , vol.16 , pp. 211-219
    • Campbell, J.D.1    Faubert, G.M.2
  • 26
    • 0026734392 scopus 로고
    • Identification of a novel transglutaminase from the filarial parasite Brugia malayi and its role in growth and development
    • Mehta K., Rao U.R., Vickery A.C., Fesus L. Identification of a novel transglutaminase from the filarial parasite Brugia malayi and its role in growth and development. Mol. Biochem. Parasitol. 53:1992;1-15
    • (1992) Mol. Biochem. Parasitol. , vol.53 , pp. 1-15
    • Mehta, K.1    Rao, U.R.2    Vickery, A.C.3    Fesus, L.4
  • 27
    • 0036668099 scopus 로고    scopus 로고
    • The Giardia intestinalis filamentous cyst wall contains a novel beta(1-3)-N-acetyl-D-galactosamine polymer: A structural and conformational study
    • Gerwig G.J., van Kuik J.A., Leeflang B.R., et al. The Giardia intestinalis filamentous cyst wall contains a novel beta(1-3)-N-acetyl-D- galactosamine polymer: a structural and conformational study. Glycobiology. 12:2002;499-505
    • (2002) Glycobiology , vol.12 , pp. 499-505
    • Gerwig, G.J.1    Van Kuik, J.A.2    Leeflang, B.R.3
  • 28
    • 0030611193 scopus 로고    scopus 로고
    • Hydrolysis of gamma:epsilon isopeptides by cytosolic transglutaminases and by coagulation factor XIIIa
    • Parameswaran K.N., Cheng X.F., Chen E.C., et al. Hydrolysis of gamma:epsilon isopeptides by cytosolic transglutaminases and by coagulation factor XIIIa. J. Biol. Chem. 272:1997;10311-10317
    • (1997) J. Biol. Chem. , vol.272 , pp. 10311-10317
    • Parameswaran, K.N.1    Cheng, X.F.2    Chen, E.C.3
  • 29
    • 0025540557 scopus 로고
    • Significance of transglutaminase-catalyzed reactions in growth and development of filarial parasite, Brugia malayi
    • Mehta K., Rao U.R., Vickery A.C., Birckbichler P.J. Significance of transglutaminase-catalyzed reactions in growth and development of filarial parasite, Brugia malayi. Biochem. Biophys. Res. Commun. 173:1990;1051-1057
    • (1990) Biochem. Biophys. Res. Commun. , vol.173 , pp. 1051-1057
    • Mehta, K.1    Rao, U.R.2    Vickery, A.C.3    Birckbichler, P.J.4
  • 30
    • 0026001944 scopus 로고
    • Brugia malayi and Acanthocheilonema viteae: Antifilarial activity of transglutaminase inhibitors in vitro
    • Rao U.R., Mehta K., Subrahmanyam D., Vickery A.C. Brugia malayi and Acanthocheilonema viteae: antifilarial activity of transglutaminase inhibitors in vitro. Antimicrob. Agents Chemother. 35:1991;2219-2224
    • (1991) Antimicrob. Agents Chemother. , vol.35 , pp. 2219-2224
    • Rao, U.R.1    Mehta, K.2    Subrahmanyam, D.3    Vickery, A.C.4
  • 31
    • 0020651210 scopus 로고
    • Axenic culture of Giardia lamblia in TYI-S-33 medium supplemented with bile
    • Keister D.B. Axenic culture of Giardia lamblia in TYI-S-33 medium supplemented with bile. Trans. R. Soc. Trop. Med. Hyg. 77:1983;487-488
    • (1983) Trans. R. Soc. Trop. Med. Hyg. , vol.77 , pp. 487-488
    • Keister, D.B.1
  • 32
    • 0017846267 scopus 로고
    • A new medium for the axenic cultivation of Entamoeba histolytica and other Entamoeba
    • Diamond L.S., Harlow D., Cunnick C.C. A new medium for the axenic cultivation of Entamoeba histolytica and other Entamoeba. Trans. R. Soc. Trop. Med. Hyg. 77:1978;431-432
    • (1978) Trans. R. Soc. Trop. Med. Hyg. , vol.77 , pp. 431-432
    • Diamond, L.S.1    Harlow, D.2    Cunnick, C.C.3
  • 33
    • 0037040969 scopus 로고    scopus 로고
    • The activity of a developmentally regulated cysteine proteinase is required for cyst wall formation in the primitive eukaryote Giardia lamblia
    • Touz M.C., Nores M.J., Slavin I., et al. The activity of a developmentally regulated cysteine proteinase is required for cyst wall formation in the primitive eukaryote Giardia lamblia. J. Biol. Chem. 277:2002;8474-8481
    • (2002) J. Biol. Chem. , vol.277 , pp. 8474-8481
    • Touz, M.C.1    Nores, M.J.2    Slavin, I.3
  • 34
    • 0033593450 scopus 로고    scopus 로고
    • Redox control of exofacial protein thiols/disulfides by protein disulfide isomerase
    • Jiang X.M., Fitzgerald M., Grant C.M., Hogg P.J. Redox control of exofacial protein thiols/disulfides by protein disulfide isomerase. J. Biol. Chem. 274:1999;2416-2423
    • (1999) J. Biol. Chem. , vol.274 , pp. 2416-2423
    • Jiang, X.M.1    Fitzgerald, M.2    Grant, C.M.3    Hogg, P.J.4
  • 36
    • 0033945433 scopus 로고    scopus 로고
    • The most abundant glycoprotein of amebic cyst walls (Jacob) is a lectin with five Cys-rich, chitin-binding domains
    • Frisardi M., Ghosh S.K., Field J., et al. The most abundant glycoprotein of amebic cyst walls (Jacob) is a lectin with five Cys-rich, chitin-binding domains. Infect. Immun. 68:2000;4217-4224
    • (2000) Infect. Immun. , vol.68 , pp. 4217-4224
    • Frisardi, M.1    Ghosh, S.K.2    Field, J.3
  • 37
    • 0034899139 scopus 로고    scopus 로고
    • Encystation in parasitic protozoa
    • Eichinger D. Encystation in parasitic protozoa. Curr. Opin. Microbiol. 4:2001;421-426
    • (2001) Curr. Opin. Microbiol. , vol.4 , pp. 421-426
    • Eichinger, D.1
  • 38
    • 0030054457 scopus 로고    scopus 로고
    • Increased expression of the molecular chaperone BiP/GRP78 during the differentiation of a primitive eukaryote
    • Lujan H.D., Mowatt M.R., Conrad J.T., Nash T.E. Increased expression of the molecular chaperone BiP/GRP78 during the differentiation of a primitive eukaryote. Biol. Cell. 86:1996;11-18
    • (1996) Biol. Cell , vol.86 , pp. 11-18
    • Lujan, H.D.1    Mowatt, M.R.2    Conrad, J.T.3    Nash, T.E.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.