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Volumn 8, Issue , 2010, Pages

Endoplasmic reticulum protein 29 (ERp29), a protein related to sperm maturation is involved in sperm-oocyte fusion in mouse

Author keywords

[No Author keywords available]

Indexed keywords

ENDOPLASMIC RETICULUM PROTEIN 29; IMMUNOGLOBULIN G ANTIBODY; MEMBRANE PROTEIN; UNCLASSIFIED DRUG; ANTIBODY; ERP29 PROTEIN, MOUSE; HEAT SHOCK PROTEIN; RECOMBINANT PROTEIN;

EID: 77950103889     PISSN: None     EISSN: 14777827     Source Type: Journal    
DOI: 10.1186/1477-7827-8-10     Document Type: Article
Times cited : (21)

References (32)
  • 1
    • 1842843786 scopus 로고    scopus 로고
    • The mechanism of sperm-oocyte fusion in mammals
    • 10.1530/rep.1.00163, 15047933
    • Kaji K, Kudo A. The mechanism of sperm-oocyte fusion in mammals. Reproduction 2004, 127(4):423-429. 10.1530/rep.1.00163, 15047933.
    • (2004) Reproduction , vol.127 , Issue.4 , pp. 423-429
    • Kaji, K.1    Kudo, A.2
  • 2
    • 0032544623 scopus 로고    scopus 로고
    • Fertilization defects in sperm from mice lacking fertilin beta
    • 10.1126/science.281.5384.1857, 9743500
    • Cho C, Bunch DO, Faure JE, Goulding EH, Eddy EM, Primakoff P, Myles DG. Fertilization defects in sperm from mice lacking fertilin beta. Science 1998, 281:1857-1859. 10.1126/science.281.5384.1857, 9743500.
    • (1998) Science , vol.281 , pp. 1857-1859
    • Cho, C.1    Bunch, D.O.2    Faure, J.E.3    Goulding, E.H.4    Eddy, E.M.5    Primakoff, P.6    Myles, D.G.7
  • 3
    • 0035337709 scopus 로고    scopus 로고
    • Analysis of loss of adhesive function in sperm lacking cyritestin or fertilin beta
    • 10.1006/dbio.2001.0166, 11319869
    • Nishimura H, Cho C, Branciforte DR, Myles DG, Primakoff P. Analysis of loss of adhesive function in sperm lacking cyritestin or fertilin beta. Dev Biol 2001, 233:204-213. 10.1006/dbio.2001.0166, 11319869.
    • (2001) Dev Biol , vol.233 , pp. 204-213
    • Nishimura, H.1    Cho, C.2    Branciforte, D.R.3    Myles, D.G.4    Primakoff, P.5
  • 4
    • 0032710099 scopus 로고    scopus 로고
    • Male mice deficient for germ-cell cyritestin are infertile
    • 10.1095/biolreprod61.6.1445, 10569988
    • Shamsadin R, Adham IM, Nayernia K, Heinlein UA, Oberwinkler H, Engel W. Male mice deficient for germ-cell cyritestin are infertile. Biol Reprod 1999, 61:1445-1451. 10.1095/biolreprod61.6.1445, 10569988.
    • (1999) Biol Reprod , vol.61 , pp. 1445-1451
    • Shamsadin, R.1    Adham, I.M.2    Nayernia, K.3    Heinlein, U.A.4    Oberwinkler, H.5    Engel, W.6
  • 5
    • 33947494440 scopus 로고    scopus 로고
    • Evidence for the involvement of testicular protein CRISP2 in mouse sperm-egg fusion
    • 10.1095/biolreprod.106.056770, 17202389
    • Busso D, Goldweic NM, Hayashi M, Kasahara M, Cuasnicú PS. Evidence for the involvement of testicular protein CRISP2 in mouse sperm-egg fusion. Biol Reprod 2007, 76:701-708. 10.1095/biolreprod.106.056770, 17202389.
    • (2007) Biol Reprod , vol.76 , pp. 701-708
    • Busso, D.1    Goldweic, N.M.2    Hayashi, M.3    Kasahara, M.4    Cuasnicú, P.S.5
  • 6
    • 0036785275 scopus 로고    scopus 로고
    • Expression and structure-function analysis of de, a sperm cysteine-rich secretory protein that mediates gamete fusion
    • 10.1095/biolreprod67.4.1225, 12297540
    • Ellerman DA, Da Ros VG, Cohen DJ, Busso D, Morgenfeld MM, Cuasnicú PS. Expression and structure-function analysis of de, a sperm cysteine-rich secretory protein that mediates gamete fusion. Biol Reprod 2002, 67:1225-1231. 10.1095/biolreprod67.4.1225, 12297540.
    • (2002) Biol Reprod , vol.67 , pp. 1225-1231
    • Ellerman, D.A.1    Da Ros, V.G.2    Cohen, D.J.3    Busso, D.4    Morgenfeld, M.M.5    Cuasnicú, P.S.6
  • 7
    • 15044362481 scopus 로고    scopus 로고
    • The immunoglobulin superfamily protein Izumo is required for sperm to fuse with eggs
    • 10.1038/nature03362, 15758983
    • Inoue N, Ikawa M, Isotani A, Okabe M. The immunoglobulin superfamily protein Izumo is required for sperm to fuse with eggs. Nature 2005, 434(7030):152-153. 10.1038/nature03362, 15758983.
    • (2005) Nature , vol.434 , Issue.7030 , pp. 152-153
    • Inoue, N.1    Ikawa, M.2    Isotani, A.3    Okabe, M.4
  • 8
    • 0346096508 scopus 로고    scopus 로고
    • Quality control in the endoplasmic reticulum protein factory
    • 10.1038/nature02262, 14685249
    • Sitia R, Braakman I. Quality control in the endoplasmic reticulum protein factory. Nature 2003, 426:891-894. 10.1038/nature02262, 14685249.
    • (2003) Nature , vol.426 , pp. 891-894
    • Sitia, R.1    Braakman, I.2
  • 9
    • 33646882179 scopus 로고    scopus 로고
    • A role for sperm surface protein disulfide isomerase activity in gamete fusion: evidence for the participation of ERp57
    • 10.1016/j.devcel.2006.03.011, 16740484
    • Ellerman DA, Myles DG, Primakoff P. A role for sperm surface protein disulfide isomerase activity in gamete fusion: evidence for the participation of ERp57. Dev Cell 2006, 10:831-837. 10.1016/j.devcel.2006.03.011, 16740484.
    • (2006) Dev Cell , vol.10 , pp. 831-837
    • Ellerman, D.A.1    Myles, D.G.2    Primakoff, P.3
  • 10
    • 34548413603 scopus 로고    scopus 로고
    • ERp57 is a potential biomarker for human fertilization capability
    • 10.1093/molehr/gam049, 17704119
    • Zhang J, Wu J, Huo R, Mao Y, Lu Y, Guo X, Liu J, Zhou Z, Huang X, Sha J. ERp57 is a potential biomarker for human fertilization capability. Mol Hum Reprod 2007, 13:633-639. 10.1093/molehr/gam049, 17704119.
    • (2007) Mol Hum Reprod , vol.13 , pp. 633-639
    • Zhang, J.1    Wu, J.2    Huo, R.3    Mao, Y.4    Lu, Y.5    Guo, X.6    Liu, J.7    Zhou, Z.8    Huang, X.9    Sha, J.10
  • 11
    • 34247588123 scopus 로고    scopus 로고
    • Identification and characterization of ERp29 in rat spermatozoa during epididymal transit
    • 10.1530/REP-06-0301, 17379652
    • Guo W, Qu F, Xia L, Guo Q, Ying X, Ding Z. Identification and characterization of ERp29 in rat spermatozoa during epididymal transit. Reproduction 2007, 133:575-584. 10.1530/REP-06-0301, 17379652.
    • (2007) Reproduction , vol.133 , pp. 575-584
    • Guo, W.1    Qu, F.2    Xia, L.3    Guo, Q.4    Ying, X.5    Ding, Z.6
  • 12
    • 26944450514 scopus 로고    scopus 로고
    • ERp29 triggers a conformational change in polyomavirus to stimulate membrane binding
    • 10.1016/j.molcel.2005.08.034, 16246730
    • Magnuson B, Rainey EK, Benjamin T, Baryshev M, Mkrtchian S, Tsai B. ERp29 triggers a conformational change in polyomavirus to stimulate membrane binding. Mol Cell 2005, 20:289-300. 10.1016/j.molcel.2005.08.034, 16246730.
    • (2005) Mol Cell , vol.20 , pp. 289-300
    • Magnuson, B.1    Rainey, E.K.2    Benjamin, T.3    Baryshev, M.4    Mkrtchian, S.5    Tsai, B.6
  • 13
    • 35048837995 scopus 로고    scopus 로고
    • The role of Zn-alpha2 glycoprotein in sperm motility is mediated by changes in cyclic AMP
    • 10.1530/REP-07-0145, 17890292
    • Qu F, Ying X, Guo W, Guo Q, Chen G, Liu Y, Ding Z. The role of Zn-alpha2 glycoprotein in sperm motility is mediated by changes in cyclic AMP. Reproduction 2007, 134:569-576. 10.1530/REP-07-0145, 17890292.
    • (2007) Reproduction , vol.134 , pp. 569-576
    • Qu, F.1    Ying, X.2    Guo, W.3    Guo, Q.4    Chen, G.5    Liu, Y.6    Ding, Z.7
  • 14
    • 0033061672 scopus 로고    scopus 로고
    • Simple histochemical stain for acrosomes on sperm from several species
    • 10.1002/(SICI)1098-2795(199904)52:4<445::AID-MRD14>3.0.CO;2-6, 10092125
    • Larson JL, Miller DJ. Simple histochemical stain for acrosomes on sperm from several species. Mol Reprod Dev 1999, 52:445-449. 10.1002/(SICI)1098-2795(199904)52:4<445::AID-MRD14>3.0.CO;2-6, 10092125.
    • (1999) Mol Reprod Dev , vol.52 , pp. 445-449
    • Larson, J.L.1    Miller, D.J.2
  • 15
    • 0031054441 scopus 로고    scopus 로고
    • Molecular cloning of ERp29, a novel and widely expressed resident of the endoplasmic reticulum
    • 10.1016/S0014-5793(96)01513-X, 9037184
    • Demmer J, Zhou C, Hubbard MJ. Molecular cloning of ERp29, a novel and widely expressed resident of the endoplasmic reticulum. FEBS Lett 1997, 402:145-150. 10.1016/S0014-5793(96)01513-X, 9037184.
    • (1997) FEBS Lett , vol.402 , pp. 145-150
    • Demmer, J.1    Zhou, C.2    Hubbard, M.J.3
  • 16
    • 0032518585 scopus 로고    scopus 로고
    • A stress-inducible rat liver endoplasmic reticulum protein, ERp29
    • 10.1046/j.1432-1327.1998.2510304.x, 9492298
    • Mkrtchian S, Fang C, Hellman U, Ingelman-Sundberg M. A stress-inducible rat liver endoplasmic reticulum protein, ERp29. Eur J Biochem 1998, 251:304-313. 10.1046/j.1432-1327.1998.2510304.x, 9492298.
    • (1998) Eur J Biochem , vol.251 , pp. 304-313
    • Mkrtchian, S.1    Fang, C.2    Hellman, U.3    Ingelman-Sundberg, M.4
  • 17
    • 0033662286 scopus 로고    scopus 로고
    • Human ERp29: isolation, primary structural characterisation and two-dimensional gel mapping
    • 10.1002/1522-2683(200011)21:17<3785::AID-ELPS3785>3.0.CO;2-2, 11271497
    • Hubbard MJ, McHugh NJ. Human ERp29: isolation, primary structural characterisation and two-dimensional gel mapping. Electrophoresis 2000, 21:3785-3796. 10.1002/1522-2683(200011)21:17<3785::AID-ELPS3785>3.0.CO;2-2, 11271497.
    • (2000) Electrophoresis , vol.21 , pp. 3785-3796
    • Hubbard, M.J.1    McHugh, N.J.2
  • 18
    • 18444402788 scopus 로고    scopus 로고
    • Overexpression of ERp29 in the thyrocytes of FRTL-5 cells
    • 10.1007/s11033-004-3069-3, 15865205
    • Kwon OY. Overexpression of ERp29 in the thyrocytes of FRTL-5 cells. Mol Biol Rep 2005, 32:7-13. 10.1007/s11033-004-3069-3, 15865205.
    • (2005) Mol Biol Rep , vol.32 , pp. 7-13
    • Kwon, O.Y.1
  • 19
    • 0036200181 scopus 로고    scopus 로고
    • ERp29 is a ubiquitous resident of the endoplasmic reticulum with a distinct role in secretory protein production
    • Shnyder SD, Hubbard MJ. ERp29 is a ubiquitous resident of the endoplasmic reticulum with a distinct role in secretory protein production. J Histochem Cytochem 2002, 50:557-566.
    • (2002) J Histochem Cytochem , vol.50 , pp. 557-566
    • Shnyder, S.D.1    Hubbard, M.J.2
  • 20
    • 3843070861 scopus 로고    scopus 로고
    • ERp29, a general endoplasmic reticulum marker, is highly expressed throughout the brain
    • 10.1002/cne.20222, 15281078
    • MacLeod JC, Sayer RJ, Lucocq JM, Hubbard MJ. ERp29, a general endoplasmic reticulum marker, is highly expressed throughout the brain. J Comp Neurol 2004, 477:29-42. 10.1002/cne.20222, 15281078.
    • (2004) J Comp Neurol , vol.477 , pp. 29-42
    • MacLeod, J.C.1    Sayer, R.J.2    Lucocq, J.M.3    Hubbard, M.J.4
  • 21
    • 17144367645 scopus 로고    scopus 로고
    • Biophysical characterization of ERp29. Evidence for a key structural role of cysteine 125
    • 10.1074/jbc.M410889200, 15572350
    • Hermann VM, Cutfield JF, Hubbard MJ. Biophysical characterization of ERp29. Evidence for a key structural role of cysteine 125. J Biol Chem 2005, 280(14):13529-13537. 10.1074/jbc.M410889200, 15572350.
    • (2005) J Biol Chem , vol.280 , Issue.14 , pp. 13529-13537
    • Hermann, V.M.1    Cutfield, J.F.2    Hubbard, M.J.3
  • 22
    • 36348964305 scopus 로고    scopus 로고
    • A chaperone-activated nonenveloped virus perforates the physiologically relevant endoplasmic reticulum membrane
    • 10.1128/JVI.01037-07, 2169125, 17881435
    • Rainey-Barger EK, Magnuson B, Tsai B. A chaperone-activated nonenveloped virus perforates the physiologically relevant endoplasmic reticulum membrane. J Virol 2007, 81:12996-13004. 10.1128/JVI.01037-07, 2169125, 17881435.
    • (2007) J Virol , vol.81 , pp. 12996-13004
    • Rainey-Barger, E.K.1    Magnuson, B.2    Tsai, B.3
  • 23
    • 77950159747 scopus 로고    scopus 로고
    • Bactericidal/Permeability-Increasing Protein (BPI) Is Associated with the Acrosome Region of Rodent Epididymal Spermatozoa
    • Yano R, Matsuyama T, Kaneko T, Kurio H, Murayama E, Toshimori K, Iida H. Bactericidal/Permeability-Increasing Protein (BPI) Is Associated with the Acrosome Region of Rodent Epididymal Spermatozoa. J Androl 2009,
    • (2009) J Androl
    • Yano, R.1    Matsuyama, T.2    Kaneko, T.3    Kurio, H.4    Murayama, E.5    Toshimori, K.6    Iida, H.7
  • 24
    • 0036836665 scopus 로고    scopus 로고
    • Proteins of the PDI family: unpredicted non-ER locations and functions
    • 10.1002/jcp.10172, 12384992
    • Turano C, Coppari S, Altieri F, Ferraro A. Proteins of the PDI family: unpredicted non-ER locations and functions. J Cell Physiol 2002, 193:154-163. 10.1002/jcp.10172, 12384992.
    • (2002) J Cell Physiol , vol.193 , pp. 154-163
    • Turano, C.1    Coppari, S.2    Altieri, F.3    Ferraro, A.4
  • 25
    • 0034108939 scopus 로고    scopus 로고
    • Isolation of ERp29, a novel endoplasmic reticulum protein, from rat enamel cells evidence for a unique role in secretory-protein synthesis
    • 10.1046/j.1432-1327.2000.01193.x, 10727933
    • Hubbard MJ, McHugh NJ, Carne DL. Isolation of ERp29, a novel endoplasmic reticulum protein, from rat enamel cells evidence for a unique role in secretory-protein synthesis. Eur J Biochem 2000, 267:1945-1957. 10.1046/j.1432-1327.2000.01193.x, 10727933.
    • (2000) Eur J Biochem , vol.267 , pp. 1945-1957
    • Hubbard, M.J.1    McHugh, N.J.2    Carne, D.L.3
  • 26
    • 0034989106 scopus 로고    scopus 로고
    • Thioredoxin fold as homodimerization module in the putative chaperone ERp29: NMR structures of the domains and experimental model of the 51 kDa dimer
    • 10.1016/S0969-2126(01)00607-4, 11435111
    • Liepinsh E, Baryshev M, Sharipo A, Ingelman-Sundberg M, Otting G, Mkrtchian S. Thioredoxin fold as homodimerization module in the putative chaperone ERp29: NMR structures of the domains and experimental model of the 51 kDa dimer. Structure 2001, 9:457-471. 10.1016/S0969-2126(01)00607-4, 11435111.
    • (2001) Structure , vol.9 , pp. 457-471
    • Liepinsh, E.1    Baryshev, M.2    Sharipo, A.3    Ingelman-Sundberg, M.4    Otting, G.5    Mkrtchian, S.6
  • 27
    • 0037138390 scopus 로고    scopus 로고
    • Genomic organization and promoter characterization of the gene encoding a putative endoplasmic reticulum chaperone, ERp29
    • 10.1016/S0378-1119(02)00417-1, 12039039
    • Sargsyan E, Baryshev M, Backlund M, Sharipo A, Mkrtchian S. Genomic organization and promoter characterization of the gene encoding a putative endoplasmic reticulum chaperone, ERp29. Gene 2002, 285:127-139. 10.1016/S0378-1119(02)00417-1, 12039039.
    • (2002) Gene , vol.285 , pp. 127-139
    • Sargsyan, E.1    Baryshev, M.2    Backlund, M.3    Sharipo, A.4    Mkrtchian, S.5
  • 28
    • 0037053397 scopus 로고    scopus 로고
    • Identification of ERp29, an endoplasmic reticulum lumenal protein, as a new member of the thyroglobulin folding complex
    • 10.1074/jbc.M200539200, 11884402
    • Sargsyan E, Baryshev M, Szekely L, Sharipo A, Mkrtchian S. Identification of ERp29, an endoplasmic reticulum lumenal protein, as a new member of the thyroglobulin folding complex. J Biol Chem 2002, 277:17009-17015. 10.1074/jbc.M200539200, 11884402.
    • (2002) J Biol Chem , vol.277 , pp. 17009-17015
    • Sargsyan, E.1    Baryshev, M.2    Szekely, L.3    Sharipo, A.4    Mkrtchian, S.5
  • 29
    • 33646687533 scopus 로고    scopus 로고
    • ERp29, an unusual redox-inactive member of the thioredoxin family
    • Mkrtchian S, Sandalova T. ERp29, an unusual redox-inactive member of the thioredoxin family. Antioxid Redox Sign 2006, 8:325-337.
    • (2006) Antioxid Redox Sign , vol.8 , pp. 325-337
    • Mkrtchian, S.1    Sandalova, T.2
  • 30
    • 33750310094 scopus 로고    scopus 로고
    • Downregulation of protein disulfide isomerase inhibits infection by the mouse polyomavirus
    • 10.1128/JVI.01117-06, 1641741, 16928750
    • Gilbert J, Ou W, Silver J, Benjamin T. Downregulation of protein disulfide isomerase inhibits infection by the mouse polyomavirus. J Virol 2006, 80(21):10868-10870. 10.1128/JVI.01117-06, 1641741, 16928750.
    • (2006) J Virol , vol.80 , Issue.21 , pp. 10868-10870
    • Gilbert, J.1    Ou, W.2    Silver, J.3    Benjamin, T.4
  • 31
    • 34247206573 scopus 로고    scopus 로고
    • Dimerization of ERp29, a PDI-like protein, is essential for its diverse functions
    • 10.1091/mbc.E06-11-1004, 1838973, 17267685
    • Rainey-Barger EK, Magnuson B, Tsai B. Dimerization of ERp29, a PDI-like protein, is essential for its diverse functions. Mol Biol Cell 2007, 18:1253-1260. 10.1091/mbc.E06-11-1004, 1838973, 17267685.
    • (2007) Mol Biol Cell , vol.18 , pp. 1253-1260
    • Rainey-Barger, E.K.1    Magnuson, B.2    Tsai, B.3
  • 32
    • 59749085866 scopus 로고    scopus 로고
    • The C-terminal domain of ERp29 mediates polyomavirus binding, unfolding and infection
    • 10.1128/JVI.02057-08, 2620899, 19019959
    • Rainey-Barger EK, Magnuson B, Tsai B. The C-terminal domain of ERp29 mediates polyomavirus binding, unfolding and infection. J Virol 2009, 83(3):1483-1491. 10.1128/JVI.02057-08, 2620899, 19019959.
    • (2009) J Virol , vol.83 , Issue.3 , pp. 1483-1491
    • Rainey-Barger, E.K.1    Magnuson, B.2    Tsai, B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.