메뉴 건너뛰기




Volumn 43, Issue 12, 2008, Pages 1330-1337

Interaction of human protein disulfide isomerase and human P5 with drug compounds: Analysis using biosensor technology

Author keywords

Biosensor analysis; Inhibitor; Molecular chaperone; P5; Protein disulfide isomerase; Vincristine

Indexed keywords

AMINES; ANTIBIOTICS; BIOSENSORS; DRUG INTERACTIONS; FLOW INTERACTIONS; PROTEINS; SIGNAL TRANSDUCTION; SUGAR (SUCROSE); SUGARS;

EID: 54949122104     PISSN: 13595113     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.procbio.2008.07.018     Document Type: Article
Times cited : (10)

References (47)
  • 1
    • 0027959156 scopus 로고
    • Protein disulphide isomerase: building bridges in protein folding
    • Freedman R.B., Hirst T.R., and Tuite M.F. Protein disulphide isomerase: building bridges in protein folding. Trends Biochem Sci 19 (1994) 331-336
    • (1994) Trends Biochem Sci , vol.19 , pp. 331-336
    • Freedman, R.B.1    Hirst, T.R.2    Tuite, M.F.3
  • 2
    • 0022387362 scopus 로고
    • Sequence of protein disulphide isomerase and implications of its relationship to thioredoxin
    • Edman J.C., Ellis L., Blacher R.W., Roth R.A., and Rutter W.J. Sequence of protein disulphide isomerase and implications of its relationship to thioredoxin. Nature 317 (1985) 267-270
    • (1985) Nature , vol.317 , pp. 267-270
    • Edman, J.C.1    Ellis, L.2    Blacher, R.W.3    Roth, R.A.4    Rutter, W.J.5
  • 3
  • 4
    • 0029074071 scopus 로고
    • A possible role ER-60 protease in the degradation of misfolded proteins in the endoplasimic reticulum
    • Otsu M., Urade R., Kito M., Omura F., and Kikuchi M. A possible role ER-60 protease in the degradation of misfolded proteins in the endoplasimic reticulum. J Biol Chem 270 (1995) 14958-14961
    • (1995) J Biol Chem , vol.270 , pp. 14958-14961
    • Otsu, M.1    Urade, R.2    Kito, M.3    Omura, F.4    Kikuchi, M.5
  • 5
    • 0025831094 scopus 로고
    • Protein disulfide isomerase is essential for viability in Saccharomyces cerevisiae
    • Farquhar R., Honey N., Murant S.J., Bossier P., Schultz L., Montgomery D., et al. Protein disulfide isomerase is essential for viability in Saccharomyces cerevisiae. Gene 108 (1991) 81-89
    • (1991) Gene , vol.108 , pp. 81-89
    • Farquhar, R.1    Honey, N.2    Murant, S.J.3    Bossier, P.4    Schultz, L.5    Montgomery, D.6
  • 6
    • 0026334073 scopus 로고
    • The Saccharomyces cerevisiae TRG1 gene is essential for growth and encodes a lumenal endoplasmic reticulum glycoprotein involved in the maturation of vacuolar carboxypeptidase
    • Gunther R., Brauer C., Janetzky B., Forster H.H., Ehbrecht E.M., Lehle L., et al. The Saccharomyces cerevisiae TRG1 gene is essential for growth and encodes a lumenal endoplasmic reticulum glycoprotein involved in the maturation of vacuolar carboxypeptidase. J Biol Chem 266 (1991) 24536-24557
    • (1991) J Biol Chem , vol.266 , pp. 24536-24557
    • Gunther, R.1    Brauer, C.2    Janetzky, B.3    Forster, H.H.4    Ehbrecht, E.M.5    Lehle, L.6
  • 7
    • 0025855390 scopus 로고
    • Glycosylation site binding protein and protein disulfide isomerase are identical and essential for cell viability in yeast
    • LaMantia M.L., Miura T., Tachikawa H., Kaplan H.A., Lennarz W.J., and Mizunaga T. Glycosylation site binding protein and protein disulfide isomerase are identical and essential for cell viability in yeast. Proc Natl Acad Sci USA 88 (1991) 4453-4457
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 4453-4457
    • LaMantia, M.L.1    Miura, T.2    Tachikawa, H.3    Kaplan, H.A.4    Lennarz, W.J.5    Mizunaga, T.6
  • 8
    • 0023303619 scopus 로고
    • Molecular cloning of the β-subunit of human prolyl 4-hydroxylase: this subunit and protein disulphide isomerase are products of the same gene
    • Pihlajaniemi T., Helaakoski T., Tasanen K., Myllylä R., Huhtala M.L., Koivu J., et al. Molecular cloning of the β-subunit of human prolyl 4-hydroxylase: this subunit and protein disulphide isomerase are products of the same gene. EMBO J 6 (1987) 643-649
    • (1987) EMBO J , vol.6 , pp. 643-649
    • Pihlajaniemi, T.1    Helaakoski, T.2    Tasanen, K.3    Myllylä, R.4    Huhtala, M.L.5    Koivu, J.6
  • 9
    • 0025329901 scopus 로고
    • Protein disulfide isomerase is a component of the microsomal triglyceride-transfer protein complex
    • Wetterau J.R., Combs K.A., Spinner S.N., and Joiner B.J. Protein disulfide isomerase is a component of the microsomal triglyceride-transfer protein complex. J Biol Chem 265 (1990) 9800-9807
    • (1990) J Biol Chem , vol.265 , pp. 9800-9807
    • Wetterau, J.R.1    Combs, K.A.2    Spinner, S.N.3    Joiner, B.J.4
  • 10
    • 0023865390 scopus 로고
    • Thyroid hormone down-regulates p55, a thyroid hormone-binding protein that is homologous to protein disulfide isomerase and the beta-subunit of prolyl-4-hydroxylase
    • Obata T., Kitagawa S., Gong Q.H., Pastan I., and Cheng S.Y. Thyroid hormone down-regulates p55, a thyroid hormone-binding protein that is homologous to protein disulfide isomerase and the beta-subunit of prolyl-4-hydroxylase. J Biol Chem 263 (1988) 782-785
    • (1988) J Biol Chem , vol.263 , pp. 782-785
    • Obata, T.1    Kitagawa, S.2    Gong, Q.H.3    Pastan, I.4    Cheng, S.Y.5
  • 11
    • 0029808166 scopus 로고    scopus 로고
    • Reexamination of hormone-binding properties of protein disulfide-isomerase
    • Guthapfel R., Gueguen P., and Quemeneur E. Reexamination of hormone-binding properties of protein disulfide-isomerase. Eur J Biochem 242 (1996) 315-319
    • (1996) Eur J Biochem , vol.242 , pp. 315-319
    • Guthapfel, R.1    Gueguen, P.2    Quemeneur, E.3
  • 12
    • 0035808319 scopus 로고    scopus 로고
    • Hormone binding by protein disulfide isomerase, a high capacity hormone reservoir of the endoplasmic reticulum
    • Primm T.P., and Gilbert H.F. Hormone binding by protein disulfide isomerase, a high capacity hormone reservoir of the endoplasmic reticulum. J Biol Chem 276 (2001) 281-286
    • (2001) J Biol Chem , vol.276 , pp. 281-286
    • Primm, T.P.1    Gilbert, H.F.2
  • 13
    • 33646342053 scopus 로고    scopus 로고
    • Inhibitory effects of environmental chemicals on protein disulfide isomerase in vitro
    • Okada K., Hiroi T., Imaoka S., and Funae Y. Inhibitory effects of environmental chemicals on protein disulfide isomerase in vitro. Osaka City Med J 51 (2005) 51-63
    • (2005) Osaka City Med J , vol.51 , pp. 51-63
    • Okada, K.1    Hiroi, T.2    Imaoka, S.3    Funae, Y.4
  • 14
    • 33646798398 scopus 로고    scopus 로고
    • A binds to protein disulfide isomerase and inhibits its enzymatic and hormone-binding activities
    • Hiroi T., Okada K., Imaoka S., Osada M., Funae Y., and Bisphenol. A binds to protein disulfide isomerase and inhibits its enzymatic and hormone-binding activities. Endocrinology 147 (2006) 2773-2780
    • (2006) Endocrinology , vol.147 , pp. 2773-2780
    • Hiroi, T.1    Okada, K.2    Imaoka, S.3    Osada, M.4    Funae, Y.5    Bisphenol6
  • 15
    • 0019833479 scopus 로고
    • The accumulation of three specific proteins related to glucose-regulated proteins in a temperature-sensitive hamster mutant cell line K12
    • Lee A.S. The accumulation of three specific proteins related to glucose-regulated proteins in a temperature-sensitive hamster mutant cell line K12. J Cell Physiol 106 (1981) 119-125
    • (1981) J Cell Physiol , vol.106 , pp. 119-125
    • Lee, A.S.1
  • 16
    • 0023687758 scopus 로고
    • Molecular cloning and complete amino-acid sequence of form-I phosphoinositide-specific phospholipase C
    • Bennett C.F., Balcarek J.M., Varrichio A., and Crooke S.T. Molecular cloning and complete amino-acid sequence of form-I phosphoinositide-specific phospholipase C. Nature 334 (1988) 268-270
    • (1988) Nature , vol.334 , pp. 268-270
    • Bennett, C.F.1    Balcarek, J.M.2    Varrichio, A.3    Crooke, S.T.4
  • 17
    • 0025233474 scopus 로고
    • HIP-70: a protein induced by estrogen in the brain and LH-RH in the pituitary
    • Mobbs C.V., Fink G., and Pfaff D.W. HIP-70: a protein induced by estrogen in the brain and LH-RH in the pituitary. Science 247 (1990) 1477-1479
    • (1990) Science , vol.247 , pp. 1477-1479
    • Mobbs, C.V.1    Fink, G.2    Pfaff, D.W.3
  • 18
    • 0026651766 scopus 로고
    • Protein degradation by the phosphoinositide-specific phospholipase C-alpha family from rat liver endoplasmic reticulum
    • Urade R., Nasu M., Moriyama T., Wada K., and Kito M. Protein degradation by the phosphoinositide-specific phospholipase C-alpha family from rat liver endoplasmic reticulum. J Biol Chem 267 (1992) 15152-15159
    • (1992) J Biol Chem , vol.267 , pp. 15152-15159
    • Urade, R.1    Nasu, M.2    Moriyama, T.3    Wada, K.4    Kito, M.5
  • 19
    • 0028846534 scopus 로고
    • Cloning and sequencing of the cDNA encoding human P5
    • Hayano T., and Kikuchi M. Cloning and sequencing of the cDNA encoding human P5. Gene 164 (1995) 377-378
    • (1995) Gene , vol.164 , pp. 377-378
    • Hayano, T.1    Kikuchi, M.2
  • 20
    • 0029121158 scopus 로고
    • Molecular cloning of the cDNA encoding a novel protein disulfide isomerase-related protein (PDIR)
    • Hayano T., and Kikuchi M. Molecular cloning of the cDNA encoding a novel protein disulfide isomerase-related protein (PDIR). FEBS Lett 372 (1995) 210-214
    • (1995) FEBS Lett , vol.372 , pp. 210-214
    • Hayano, T.1    Kikuchi, M.2
  • 21
    • 0025070112 scopus 로고
    • ERp72, an abundant luminal endoplasmic reticulum protein, contains three copies of the active site sequences of protein disulfide isomerase
    • Mazzarella R.A., Srinivasan M., Haugejorden S.M., and Green M. ERp72, an abundant luminal endoplasmic reticulum protein, contains three copies of the active site sequences of protein disulfide isomerase. J Biol Chem 265 (1990) 1094-1101
    • (1990) J Biol Chem , vol.265 , pp. 1094-1101
    • Mazzarella, R.A.1    Srinivasan, M.2    Haugejorden, S.M.3    Green, M.4
  • 22
    • 0034737776 scopus 로고    scopus 로고
    • Physical proximity and functional association of glycoprotein 1bα and protein disulfide isomerase on the platelet plasma membrane
    • Burgess J.K., Hotchkiss K.A., Suter C., Dudman N.P., Szöllösi J., Chesterman C.N., et al. Physical proximity and functional association of glycoprotein 1bα and protein disulfide isomerase on the platelet plasma membrane. J Biol Chem 275 (2000) 9758-9766
    • (2000) J Biol Chem , vol.275 , pp. 9758-9766
    • Burgess, J.K.1    Hotchkiss, K.A.2    Suter, C.3    Dudman, N.P.4    Szöllösi, J.5    Chesterman, C.N.6
  • 23
    • 0035918587 scopus 로고    scopus 로고
    • Protein disulfide isomerase and sulfhydryl-dependent pathways in platelet activation
    • Essex D.W., Li M., Miller A., and Feinman R.D. Protein disulfide isomerase and sulfhydryl-dependent pathways in platelet activation. Biochemistry 40 (2001) 6070-6075
    • (2001) Biochemistry , vol.40 , pp. 6070-6075
    • Essex, D.W.1    Li, M.2    Miller, A.3    Feinman, R.D.4
  • 24
    • 0036786353 scopus 로고    scopus 로고
    • Sustained integrin ligation involves extracellular free sulfhdryls and enzymatically catalyzed disulfide exchange
    • Lahav J., Jurk K., Hess O., Barnes M.J., Farndale R.W., Luboshitz J., et al. Sustained integrin ligation involves extracellular free sulfhdryls and enzymatically catalyzed disulfide exchange. Blood 100 (2002) 2472-2478
    • (2002) Blood , vol.100 , pp. 2472-2478
    • Lahav, J.1    Jurk, K.2    Hess, O.3    Barnes, M.J.4    Farndale, R.W.5    Luboshitz, J.6
  • 25
    • 0141567629 scopus 로고    scopus 로고
    • Enzymatically catalyzed disulfide exchange is required for platelet adhesion to collagen via integrin alpha2beta1
    • Lahav J., Wijnen E.M., Hess O., Hamaia S.W., Griffiths D., Makris M., et al. Enzymatically catalyzed disulfide exchange is required for platelet adhesion to collagen via integrin alpha2beta1. Blood 102 (2003) 2085-2092
    • (2003) Blood , vol.102 , pp. 2085-2092
    • Lahav, J.1    Wijnen, E.M.2    Hess, O.3    Hamaia, S.W.4    Griffiths, D.5    Makris, M.6
  • 26
    • 0032939206 scopus 로고    scopus 로고
    • Cell-surface protein disulfide isomerase catalyzes transnitrosation and regulates intracellular transfer of nitric oxide
    • Zai A., Rudd A., Scribner A.W., and Loscalzo J. Cell-surface protein disulfide isomerase catalyzes transnitrosation and regulates intracellular transfer of nitric oxide. J Clin Invest 103 (1999) 393-399
    • (1999) J Clin Invest , vol.103 , pp. 393-399
    • Zai, A.1    Rudd, A.2    Scribner, A.W.3    Loscalzo, J.4
  • 28
    • 0036737949 scopus 로고    scopus 로고
    • Functional analysis of human P5, a protein disulfide isomerase homologue
    • Kikuchi M., Doi E., Tsujimoto I., Horibe T., and Tsujimoto Y. Functional analysis of human P5, a protein disulfide isomerase homologue. J Biochem 132 (2002) 451-455
    • (2002) J Biochem , vol.132 , pp. 451-455
    • Kikuchi, M.1    Doi, E.2    Tsujimoto, I.3    Horibe, T.4    Tsujimoto, Y.5
  • 29
    • 1042266634 scopus 로고    scopus 로고
    • Different contributions of the three CXXC motifs of human protein-disulfide isomerase-related protein to isomerase activity and oxidative refolding
    • Horibe T., Gomi M., Iguchi D., Ito H., Kitamura Y., Masuoka T., et al. Different contributions of the three CXXC motifs of human protein-disulfide isomerase-related protein to isomerase activity and oxidative refolding. J Biol Chem 279 (2004) 4604-4611
    • (2004) J Biol Chem , vol.279 , pp. 4604-4611
    • Horibe, T.1    Gomi, M.2    Iguchi, D.3    Ito, H.4    Kitamura, Y.5    Masuoka, T.6
  • 30
    • 34249295619 scopus 로고    scopus 로고
    • Disulphide-isomerase-enabled shedding of tumour-associated NKG2D ligands
    • Kaiser B.K., Yim D., Chow I.T., Gonzalez S., Dai Z., Mann H.H., et al. Disulphide-isomerase-enabled shedding of tumour-associated NKG2D ligands. Nature 447 (2007) 482-486
    • (2007) Nature , vol.447 , pp. 482-486
    • Kaiser, B.K.1    Yim, D.2    Chow, I.T.3    Gonzalez, S.4    Dai, Z.5    Mann, H.H.6
  • 32
    • 0036790739 scopus 로고    scopus 로고
    • A protein disulfide isomerase expressed in the embryonic midline is required for left/right asymmetries
    • Hoshijima K., Metherall J.E., and Grunwald D.J. A protein disulfide isomerase expressed in the embryonic midline is required for left/right asymmetries. Genes Dev 16 (2002) 2518-2529
    • (2002) Genes Dev , vol.16 , pp. 2518-2529
    • Hoshijima, K.1    Metherall, J.E.2    Grunwald, D.J.3
  • 34
    • 0036304251 scopus 로고    scopus 로고
    • Aminoglycoside antibiotics bind to protein disulfide isomerase and inhibit its chaperone activity
    • Horibe T., Nagai H., Matsui H., Hagiwara Y., and Kikuchi M. Aminoglycoside antibiotics bind to protein disulfide isomerase and inhibit its chaperone activity. J Antibiot 55 (2002) 528-530
    • (2002) J Antibiot , vol.55 , pp. 528-530
    • Horibe, T.1    Nagai, H.2    Matsui, H.3    Hagiwara, Y.4    Kikuchi, M.5
  • 36
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970) 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 37
    • 2442477583 scopus 로고    scopus 로고
    • Replacement of domain b of human protein disulfide isomerase-related protein with domain b′ of human protein disulfide isomerase dramatically increases its chaperone activity
    • Horibe T., Iguchi D., Masuoka T., Gomi M., Kimura T., and Kikuchi M. Replacement of domain b of human protein disulfide isomerase-related protein with domain b′ of human protein disulfide isomerase dramatically increases its chaperone activity. FEBS Lett 566 (2004) 311-315
    • (2004) FEBS Lett , vol.566 , pp. 311-315
    • Horibe, T.1    Iguchi, D.2    Masuoka, T.3    Gomi, M.4    Kimura, T.5    Kikuchi, M.6
  • 38
    • 0034087890 scopus 로고    scopus 로고
    • Biosensor analysis of the interaction between immobilized human serum albumin and drug compounds for prediction of human serum albumin binding levels
    • Frostell-Karlsson A., Remaeus A., Roos H., Andersson K., Borg P., Hämäläinen M., et al. Biosensor analysis of the interaction between immobilized human serum albumin and drug compounds for prediction of human serum albumin binding levels. J Med Chem 43 (2000) 1986-1992
    • (2000) J Med Chem , vol.43 , pp. 1986-1992
    • Frostell-Karlsson, A.1    Remaeus, A.2    Roos, H.3    Andersson, K.4    Borg, P.5    Hämäläinen, M.6
  • 39
    • 0017144476 scopus 로고
    • Thiol-protein disulphide oxidoreductases. Assay of microsomal membrane-bound glutathione-insulin transhydrogenase and comparison with protein disulphide-isomerase
    • Ibbetson A.L., and Freedman R.B. Thiol-protein disulphide oxidoreductases. Assay of microsomal membrane-bound glutathione-insulin transhydrogenase and comparison with protein disulphide-isomerase. Biochem J 159 (1976) 377-384
    • (1976) Biochem J , vol.159 , pp. 377-384
    • Ibbetson, A.L.1    Freedman, R.B.2
  • 40
    • 0026416043 scopus 로고
    • Chaperonin-mediated protein folding at the surface of groEL through a 'moltenglobule'-like intermediate
    • Martin J., Langer T., Boteva R., Schramel A., Horwich A.L., and Hartl F.U. Chaperonin-mediated protein folding at the surface of groEL through a 'moltenglobule'-like intermediate. Nature 352 (1991) 36-42
    • (1991) Nature , vol.352 , pp. 36-42
    • Martin, J.1    Langer, T.2    Boteva, R.3    Schramel, A.4    Horwich, A.L.5    Hartl, F.U.6
  • 41
    • 1642461466 scopus 로고    scopus 로고
    • PDI-mediated ER retention and proteasomal degradation of procollagen I in corneal endothelial cells
    • Ko M.K., and Kay E.P. PDI-mediated ER retention and proteasomal degradation of procollagen I in corneal endothelial cells. Exp Cell Res 295 (2004) 25-35
    • (2004) Exp Cell Res , vol.295 , pp. 25-35
    • Ko, M.K.1    Kay, E.P.2
  • 42
    • 0027220866 scopus 로고
    • Peptide binding to protein disulfide isomerase occurs at a site distinct from the active sites
    • Noiva R., Freedman R.B., and Lennarz W. Peptide binding to protein disulfide isomerase occurs at a site distinct from the active sites. J Biol Chem 268 (1993) 19210-19217
    • (1993) J Biol Chem , vol.268 , pp. 19210-19217
    • Noiva, R.1    Freedman, R.B.2    Lennarz, W.3
  • 43
    • 0032481380 scopus 로고    scopus 로고
    • The b′ domain provides the principal peptide-binding site of protein disulfide isomerase but all domains contribute to binding of misfolded proteins
    • Klappa P., Ruddock L.W., Darby N.J., and Freedman R.B. The b′ domain provides the principal peptide-binding site of protein disulfide isomerase but all domains contribute to binding of misfolded proteins. EMBO J 17 (1998) 927-935
    • (1998) EMBO J , vol.17 , pp. 927-935
    • Klappa, P.1    Ruddock, L.W.2    Darby, N.J.3    Freedman, R.B.4
  • 44
    • 0028093077 scopus 로고
    • Calcium binding properties of rabbit liver protein disulfide isomerase
    • Lebeche D., Lucero H.A., and Kaminer B. Calcium binding properties of rabbit liver protein disulfide isomerase. Biochem Biophys Res Commun 202 (1994) 556-561
    • (1994) Biochem Biophys Res Commun , vol.202 , pp. 556-561
    • Lebeche, D.1    Lucero, H.A.2    Kaminer, B.3
  • 46
    • 0030792311 scopus 로고    scopus 로고
    • Bacterial resistance to aminoglycoside antibiotics
    • Davies J., and Wright G.D. Bacterial resistance to aminoglycoside antibiotics. Trends Microbiol 5 (1997) 234-240
    • (1997) Trends Microbiol , vol.5 , pp. 234-240
    • Davies, J.1    Wright, G.D.2
  • 47
    • 0035868331 scopus 로고    scopus 로고
    • The pancreas-specific protein disulphide-isomerase PDIp interacts with a hydroxyaryl group in ligands
    • Klappa P., Freedman R.B., Langenbuch M., Lan M.S., Robinson G.K., and Ruddock L.W. The pancreas-specific protein disulphide-isomerase PDIp interacts with a hydroxyaryl group in ligands. Biochem J 354 (2001) 553-559
    • (2001) Biochem J , vol.354 , pp. 553-559
    • Klappa, P.1    Freedman, R.B.2    Langenbuch, M.3    Lan, M.S.4    Robinson, G.K.5    Ruddock, L.W.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.