메뉴 건너뛰기




Volumn 68, Issue 4, 2000, Pages 389-395

Glutathione excretion in response to heterologous protein secretion Saccharomyces cerevisiae

Author keywords

Glutathione excretion; Heterologous protein secretion; Oxidative stress; Yeast

Indexed keywords

BIOSYNTHESIS; ENZYME INHIBITION; OLIGOMERS; OXIDATION; POLYPEPTIDES; PROTEINS; SULFUR COMPOUNDS; YEAST;

EID: 0034690581     PISSN: 00063592     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0290(20000520)68:4<389::AID-BIT4>3.0.CO;2-N     Document Type: Article
Times cited : (15)

References (34)
  • 1
    • 0030765707 scopus 로고    scopus 로고
    • Cysteine and glutathione secretion in response to protein disulfide bond formation in the ER
    • Carelli S, Ceriotti A, Cabibbo A, Fassina G, Ruvo M, Sitia R. 1997. Cysteine and glutathione secretion in response to protein disulfide bond formation in the ER. Science 277:1681-1684.
    • (1997) Science , vol.277 , pp. 1681-1684
    • Carelli, S.1    Ceriotti, A.2    Cabibbo, A.3    Fassina, G.4    Ruvo, M.5    Sitia, R.6
  • 3
    • 0343046899 scopus 로고
    • Role of glutathione in the regulation of protein synthesis and degradation in eukaryotes
    • Vina J, editor. Boca Raton: CRC Press
    • Estrela JM, Pollard FV. 1990. Role of glutathione in the regulation of protein synthesis and degradation in eukaryotes. In: Vina J, editor. Glutathione: Metabolism and physiological functions. Boca Raton: CRC Press. p 177-185.
    • (1990) Glutathione: Metabolism and Physiological Functions , pp. 177-185
    • Estrela, J.M.1    Pollard, F.V.2
  • 5
    • 0031609760 scopus 로고    scopus 로고
    • The ERO1 gene of yeast is required for oxidation of protein dithiols in the endoplasmic reticulum
    • Frand AR, Kaiser CA. 1998. The ERO1 gene of yeast is required for oxidation of protein dithiols in the endoplasmic reticulum. Mol Cell 1:161-170.
    • (1998) Mol Cell , vol.1 , pp. 161-170
    • Frand, A.R.1    Kaiser, C.A.2
  • 6
    • 0025823035 scopus 로고
    • Compartmental organization of Golgi-specific protein modification and vacuolar protein sorting events defined in a yeast sec18 (NSF) mutant
    • Graham TR, Emr SD. 1991. Compartmental organization of Golgi-specific protein modification and vacuolar protein sorting events defined in a yeast sec18 (NSF) mutant. J Cell Biol 114:207-218.
    • (1991) J Cell Biol , vol.114 , pp. 207-218
    • Graham, T.R.1    Emr, S.D.2
  • 7
    • 0030016469 scopus 로고    scopus 로고
    • Yeast glutathione reductase is required for protection against oxidative stress and is a target gene for yAP-1 transcriptional regulation
    • Grant CM, Collinson LP, Roe JH, Dawes IW. 1996. Yeast glutathione reductase is required for protection against oxidative stress and is a target gene for yAP-1 transcriptional regulation. Mol Microbiol 21: 171-179.
    • (1996) Mol Microbiol , vol.21 , pp. 171-179
    • Grant, C.M.1    Collinson, L.P.2    Roe, J.H.3    Dawes, I.W.4
  • 8
    • 0032583570 scopus 로고    scopus 로고
    • Glutathione and catalase provide overlapping defenses for protection against hydrogen peroxide in the yeast Saccharomyces cerevisiae
    • Grant CM, Perrone G, Dawes IW. 1998. Glutathione and catalase provide overlapping defenses for protection against hydrogen peroxide in the yeast Saccharomyces cerevisiae. Biochem Biophys Res Commun 253: 893-898.
    • (1998) Biochem Biophys Res Commun , vol.253 , pp. 893-898
    • Grant, C.M.1    Perrone, G.2    Dawes, I.W.3
  • 9
    • 4244087065 scopus 로고
    • Reactive oxygen species in living systems: Source, biochemistry, and role in human disease
    • Halliwell B. 1991. Reactive oxygen species in living systems: Source, biochemistry, and role in human disease. Am J Med 91:14S-22S.
    • (1991) Am J Med , vol.91
    • Halliwell, B.1
  • 10
    • 0026698060 scopus 로고
    • Oxidized redox state of glutathione in the endoplasmic reticulum
    • Hwang C, Sinskey AJ, Lodish HF. 1992. Oxidized redox state of glutathione in the endoplasmic reticulum. Science 257:1496-1502.
    • (1992) Science , vol.257 , pp. 1496-1502
    • Hwang, C.1    Sinskey, A.J.2    Lodish, H.F.3
  • 11
    • 0028260121 scopus 로고
    • Selective retention of secretory proteins in the yeast endoplasmic reticulum by treatment of cells with a reducing agent
    • Jämsä, E, Simonen M, Makarow M. 1994. Selective retention of secretory proteins in the yeast endoplasmic reticulum by treatment of cells with a reducing agent. Yeast 10:355-370.
    • (1994) Yeast , vol.10 , pp. 355-370
    • Jämsä, E.1    Simonen, M.2    Makarow, M.3
  • 12
    • 0025277750 scopus 로고
    • Distinct sets of SEC genes govern transport vesicle formation and fusion early in the secretory pathway
    • Kaiser CA, Schekman R. 1990. Distinct sets of SEC genes govern transport vesicle formation and fusion early in the secretory pathway. Cell 61: 723-733.
    • (1990) Cell , vol.61 , pp. 723-733
    • Kaiser, C.A.1    Schekman, R.2
  • 13
    • 0027526906 scopus 로고
    • The effect of folding catalysts on the in vivo folding process of different antibody fragments expressed in Escherichia coli
    • Knappik A, Krebber C, Plückthun A. 1993. The effect of folding catalysts on the in vivo folding process of different antibody fragments expressed in Escherichia coli. Biotechnol (NY) 11:77-83.
    • (1993) Biotechnol (Ny) , vol.11 , pp. 77-83
    • Knappik, A.1    Krebber, C.2    Plückthun, A.3
  • 14
    • 0029912351 scopus 로고    scopus 로고
    • ATP-dependent glutathione disulphide transport mediated by the MRP gene-encoded conjugate export pump
    • Leier I, Jedlitschky G, Buchholz U, Center M, Cole SP, Deeley RG, Keppler D. 1996. ATP-dependent glutathione disulphide transport mediated by the MRP gene-encoded conjugate export pump. Biochem J 314:433-437.
    • (1996) Biochem J , vol.314 , pp. 433-437
    • Leier, I.1    Jedlitschky, G.2    Buchholz, U.3    Center, M.4    Cole, S.P.5    Deeley, R.G.6    Keppler, D.7
  • 15
    • 0029983266 scopus 로고    scopus 로고
    • The yeast Cadmium Factor Protein (YCF1) is a vacuolar glutathione 5-conjugate pump
    • Li Z-S, Lu Y-P, Zhe R-G, Szczypka M, Thiele DJ, Rea PA. 1996. The Yeast Cadmium Factor Protein (YCF1) is a vacuolar glutathione 5-conjugate pump. J Biol Chem 271:6509-6517.
    • (1996) J Biol Chem , vol.271 , pp. 6509-6517
    • Li, Z.-S.1    Lu, Y.-P.2    Zhe, R.-G.3    Szczypka, M.4    Thiele, D.J.5    Rea, P.A.6
  • 16
    • 0032919167 scopus 로고    scopus 로고
    • When less is more: Enhanced baculovirus production of recombinant proteins at very low multiplicities of infection
    • Liebman JM, LaSala D, Wang W, Steed PM. 1999. When less is more: Enhanced baculovirus production of recombinant proteins at very low multiplicities of infection. Biotechniques 26:36-38, 40, 42.
    • (1999) Biotechniques , vol.26 , pp. 36-38
    • Liebman, J.M.1    LaSala, D.2    Wang, W.3    Steed, P.M.4
  • 18
    • 0030041567 scopus 로고    scopus 로고
    • The molecular defences against reactive oxygen species in yeast
    • Moradas-Ferreira P, Costa V, Piper P, Mager W. 1996. The molecular defences against reactive oxygen species in yeast. Mol Microbiol 19:651-658.
    • (1996) Mol Microbiol , vol.19 , pp. 651-658
    • Moradas-Ferreira, P.1    Costa, V.2    Piper, P.3    Mager, W.4
  • 19
    • 85009638304 scopus 로고
    • Effect of L-Buthionine-[S,R]-sulfoximine on the cellular glutathione level and growth of Saccharomyces cerevisiae
    • Murata K, Kimura A. 1987. Effect of L-Buthionine-[S,R]-sulfoximine on the cellular glutathione level and growth of Saccharomyces cerevisiae. Agri Biol Chem 51:2827-2829.
    • (1987) Agri Biol Chem , vol.51 , pp. 2827-2829
    • Murata, K.1    Kimura, A.2
  • 20
    • 0024321694 scopus 로고
    • Cassette mutagenic analysis of the yeast invertase signal peptide: Effects on protein translocation
    • Ngsee JK, Hansen W, Walter P, Smith M. 1989. Cassette mutagenic analysis of the yeast invertase signal peptide: Effects on protein translocation. Mol Cell Biol 9:3400-3410.
    • (1989) Mol Cell Biol , vol.9 , pp. 3400-3410
    • Ngsee, J.K.1    Hansen, W.2    Walter, P.3    Smith, M.4
  • 21
    • 0029347117 scopus 로고
    • Multicopy overexpression of bovine pancreatic trypsin inhibitor saturates the protein folding and secretory capacity of Saccharomyces cerevisiae
    • Parekh RN, Forrester KJ, Wittrup KD. 1995. Multicopy overexpression of bovine pancreatic trypsin inhibitor saturates the protein folding and secretory capacity of Saccharomyces cerevisiae. Protein Expr Purif 6:537-545.
    • (1995) Protein Expr Purif , vol.6 , pp. 537-545
    • Parekh, R.N.1    Forrester, K.J.2    Wittrup, K.D.3
  • 22
    • 0030019291 scopus 로고    scopus 로고
    • An integrating vector for tunable, high copy, stable integration into the dispersed Ty delta sites of Saccharomyces cerevisiae
    • Parekh RN, Shaw MR, Wittrup KD. 1996. An integrating vector for tunable, high copy, stable integration into the dispersed Ty delta sites of Saccharomyces cerevisiae. Biotechnol Prog 12:16-21.
    • (1996) Biotechnol Prog , vol.12 , pp. 16-21
    • Parekh, R.N.1    Shaw, M.R.2    Wittrup, K.D.3
  • 23
    • 0031104672 scopus 로고    scopus 로고
    • Expression level tuning for optimal heterologous protein secretion in Saccharomyces cerivisiae
    • Parekh RN, Wittrup KD. 1997. Expression level tuning for optimal heterologous protein secretion in Saccharomyces cerivisiae. Biotechnol Prog 13:117-122.
    • (1997) Biotechnol Prog , vol.13 , pp. 117-122
    • Parekh, R.N.1    Wittrup, K.D.2
  • 24
    • 0027112480 scopus 로고
    • Effect of cloned gene dosage on cell growth and hepatitis B surface antigen synthesis and secretion in recombinant CHO cells
    • Pendse GJ, Karkare S, Bailey JE. 1992. Effect of cloned gene dosage on cell growth and hepatitis B surface antigen synthesis and secretion in recombinant CHO cells. Biotechnol Bioeng 40:119-129.
    • (1992) Biotechnol Bioeng , vol.40 , pp. 119-129
    • Pendse, G.J.1    Karkare, S.2    Bailey, J.E.3
  • 25
    • 0031610364 scopus 로고    scopus 로고
    • Ero1p: A novel and ubiquitous protein with an essential role in oxidative protein folding in the endoplasmic reticulum
    • Pollard MG, Travers KJ, Weissman JS. 1998. Ero1p: A novel and ubiquitous protein with an essential role in oxidative protein folding in the endoplasmic reticulum. Mol Cell 1:1711-82.
    • (1998) Mol Cell , vol.1 , pp. 1711-1782
    • Pollard, M.G.1    Travers, K.J.2    Weissman, J.S.3
  • 26
    • 0032509502 scopus 로고    scopus 로고
    • ATP-dependent transport of reduced glutathione on YCF1, the yeast orthologue of mammalian multidrug resistance associated proteins
    • Rebbeor JF, Connolly GC, Dumont ME, Ballatori N. 1998. ATP-dependent transport of reduced glutathione on YCF1, the yeast orthologue of mammalian multidrug resistance associated proteins. J Biol Chem 273:33449-33454.
    • (1998) J Biol Chem , vol.273 , pp. 33449-33454
    • Rebbeor, J.F.1    Connolly, G.C.2    Dumont, M.E.3    Ballatori, N.4
  • 27
    • 0029257263 scopus 로고
    • Constitutive overexpression of secreted heterologous proteins decreases extractable BiP and protein disulfide isomerase levels in Saccharomyces cerevisiae
    • Robinson AS, Wittrup KD. 1995. Constitutive overexpression of secreted heterologous proteins decreases extractable BiP and protein disulfide isomerase levels in Saccharomyces cerevisiae. Biotechnol Prog 11:171-177.
    • (1995) Biotechnol Prog , vol.11 , pp. 171-177
    • Robinson, A.S.1    Wittrup, K.D.2
  • 28
    • 0029944822 scopus 로고    scopus 로고
    • Reduction of BiP levels decreases heterologous protein secretion in Saccharomyces cerevisiae
    • Robinson AS, Bockhaus JA, Voegler AC, Wittrup KD. 1996. Reduction of BiP levels decreases heterologous protein secretion in Saccharomyces cerevisiae. J Biol Chem 271:10017-10022.
    • (1996) J Biol Chem , vol.271 , pp. 10017-10022
    • Robinson, A.S.1    Bockhaus, J.A.2    Voegler, A.C.3    Wittrup, K.D.4
  • 29
    • 0024799254 scopus 로고
    • High efficiency transformation of intact yeast cells using single stranded nucleic acids as a carrier
    • Schiestl RH, Gietz RD. 1989. High efficiency transformation of intact yeast cells using single stranded nucleic acids as a carrier. Curr Genet 16:339-346.
    • (1989) Curr Genet , vol.16 , pp. 339-346
    • Schiestl, R.H.1    Gietz, R.D.2
  • 30
    • 0031879861 scopus 로고    scopus 로고
    • Increasing the secretory capacity of Saccharomyces cerevisiae for production of single-chain antibody fragments
    • Shusta EV, Raines RT, Plückthun A, Wittrup KD. 1998. Increasing the secretory capacity of Saccharomyces cerevisiae for production of single-chain antibody fragments. Nat Biotechnol 16:773-777.
    • (1998) Nat Biotechnol , vol.16 , pp. 773-777
    • Shusta, E.V.1    Raines, R.T.2    Plückthun, A.3    Wittrup, K.D.4
  • 31
    • 0032570383 scopus 로고    scopus 로고
    • Secretion of thiols and disulfide bond formation: Retraction
    • Sitia R, Ceriotti A, Cabibo A, Fassina G, Ruvo M. 1998. Secretion of thiols and disulfide bond formation: Retraction. Science 279: 1283.
    • (1998) Science , vol.279 , pp. 1283
    • Sitia, R.1    Ceriotti, A.2    Cabibo, A.3    Fassina, G.4    Ruvo, M.5
  • 32
    • 0029013534 scopus 로고
    • The role of the YAP1 and YAP2 genes in the regulation of the adaptive oxidative stress responses of Saccharomyces cerevisiae
    • Stephen DW, Rivers SL, Jamieson DJ. 1995. The role of the YAP1 and YAP2 genes in the regulation of the adaptive oxidative stress responses of Saccharomyces cerevisiae. Mol Microbiol 16:415-423.
    • (1995) Mol Microbiol , vol.16 , pp. 415-423
    • Stephen, D.W.1    Rivers, S.L.2    Jamieson, D.J.3
  • 33
    • 0014481378 scopus 로고
    • Enzymic method for quantitative determination of nanogram amounts of total and oxidized glutathione: Applications to mammalian blood and other tissues
    • Tietze F. 1969. Enzymic method for quantitative determination of nanogram amounts of total and oxidized glutathione: Applications to mammalian blood and other tissues. Anal Biochem 27:502-522.
    • (1969) Anal Biochem , vol.27 , pp. 502-522
    • Tietze, F.1
  • 34
    • 0028718055 scopus 로고
    • Existence of an optimum expression level for secretion of foreign proteins in yeast
    • Wittrup KD, Robinson AS, Parekh RN, Forrester KJ. 1994. Existence of an optimum expression level for secretion of foreign proteins in yeast. Ann NY Acad Sci 745:321-330.
    • (1994) Ann NY Acad Sci , vol.745 , pp. 321-330
    • Wittrup, K.D.1    Robinson, A.S.2    Parekh, R.N.3    Forrester, K.J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.