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Volumn 109, Issue 10, 2012, Pages 3850-3855

Erratum: Protein disulfide isomerase homolog PDILT is required for quality control of sperm membrane protein ADAM3 and male infertility (Proceedings of the National Academy of Sciences of the United States of America (2012) 109, 10 (3850-3855) DOI: 10.1073/pnas.1117963109);Protein disulfide isomerase homolog PDILT is required for quality control of sperm membrane protein ADAM3 and male infertility

Author keywords

Calmegin; Cyritestin; Disease; Gamete; Uterotubal

Indexed keywords

ADAM3 PROTEIN; CALRETICULIN; CALSPERIN; MEMBRANE PROTEIN; PROTEIN DISULFIDE ISOMERASE; TESTIS SPECIFIC PROTEIN DISULFIDE ISOMERASE HOMOLOG; UNCLASSIFIED DRUG;

EID: 84857969832     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1204275109     Document Type: Erratum
Times cited : (122)

References (52)
  • 1
    • 34548253523 scopus 로고
    • Fertilization of rabbit ova in vitro
    • Chang MC (1959) Fertilization of rabbit ova in vitro. Nature 184(Suppl 7):466-467.
    • (1959) Nature , vol.184 , Issue.SUPPL. 7 , pp. 466-467
    • Chang, M.C.1
  • 2
    • 0003178422 scopus 로고
    • The capacitation of the mammalian sperm
    • Austin CR (1952) The capacitation of the mammalian sperm. Nature 170:326.
    • (1952) Nature , vol.170 , pp. 326
    • Austin, C.R.1
  • 3
    • 77951148607 scopus 로고    scopus 로고
    • Fertilization: A sperm's journey to and interaction with the oocyte
    • Ikawa M, Inoue N, Benham AM, Okabe M (2010) Fertilization: A sperm's journey to and interaction with the oocyte. J Clin Invest 120:984-994.
    • (2010) J Clin Invest , vol.120 , pp. 984-994
    • Ikawa, M.1    Inoue, N.2    Benham, A.M.3    Okabe, M.4
  • 4
    • 0030951614 scopus 로고    scopus 로고
    • A role for the disintegrin domain of cyritestin, a sperm surface protein belonging to the ADAM family, in mouse sperm-egg plasma membrane adhesion and fusion
    • DOI 10.1083/jcb.137.1.105
    • Yuan R, Primakoff P, Myles DG (1997) A role for the disintegrin domain of cyritestin, a sperm surface protein belonging to the ADAM family, in mouse sperm-egg plasma membrane adhesion and fusion. J Cell Biol 137:105-112. (Pubitemid 27167299)
    • (1997) Journal of Cell Biology , vol.137 , Issue.1 , pp. 105-112
    • Yuan, R.1    Primakoff, P.2    Myles, D.G.3
  • 5
    • 0032710099 scopus 로고    scopus 로고
    • Male mice deficient for germ-cell cyritestin are infertile
    • Shamsadin R, et al. (1999) Male mice deficient for germ-cell cyritestin are infertile. Biol Reprod 61:1445-1451.
    • (1999) Biol Reprod , vol.61 , pp. 1445-1451
    • Shamsadin, R.1
  • 6
    • 33750845874 scopus 로고    scopus 로고
    • Aberrant distribution of ADAM3 in sperm from both angiotensin-converting enzyme (Ace)- and calmegin (Clgn)-deficient mice
    • DOI 10.1095/biolreprod.106.052977
    • Yamaguchi R, Yamagata K, Ikawa M, Moss SB, Okabe M (2006) Aberrant distribution of ADAM3 in sperm from both angiotensin-converting enzyme (Ace)- and calmegin (Clgn)-deficient mice. Biol Reprod 75:760-766. (Pubitemid 44720396)
    • (2006) Biology of Reproduction , vol.75 , Issue.5 , pp. 760-766
    • Yamaguchi, R.1    Yamagata, K.2    Ikawa, M.3    Moss, S.B.4    Okabe, M.5
  • 9
    • 4544250782 scopus 로고    scopus 로고
    • Possible function of the ADAM1a/ADAM2 fertilin complex in the appearance of ADAM3 on the sperm surface
    • DOI 10.1074/jbc.M314249200
    • Nishimura H, Kim E, Nakanishi T, Baba T (2004) Possible function of the ADAM1a/ ADAM2 Fertilin complex in the appearance of ADAM3 on the sperm surface. J Biol Chem 279:34957-34962. (Pubitemid 39318132)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.33 , pp. 34957-34962
    • Nishimura, H.1    Kim, E.2    Nakanishi, T.3    Baba, T.4
  • 11
    • 79953135154 scopus 로고    scopus 로고
    • Calsperin is a testis-specific chaperone required for sperm fertility
    • Ikawa M, et al. (2011) Calsperin is a testis-specific chaperone required for sperm fertility. J Biol Chem 286:5639-5646.
    • (2011) J Biol Chem , vol.286 , pp. 5639-5646
    • Ikawa, M.1
  • 12
    • 0031011488 scopus 로고    scopus 로고
    • The putative chaperone calmegin is required for sperm fertility
    • Ikawa M, et al. (1997) The putative chaperone calmegin is required for sperm fertility. Nature 387:607-611.
    • (1997) Nature , vol.387 , pp. 607-611
    • Ikawa, M.1
  • 13
    • 79953901981 scopus 로고    scopus 로고
    • Lack of tyrosylprotein sulfotransferase- 2 activity results in altered sperm-egg interactions and loss of ADAM3 and ADAM6 in epididymal sperm
    • Marcello MR, Jia W, Leary JA, Moore KL, Evans JP (2011) Lack of tyrosylprotein sulfotransferase- 2 activity results in altered sperm-egg interactions and loss of ADAM3 and ADAM6 in epididymal sperm. J Biol Chem 286:13060-13070.
    • (2011) J Biol Chem , vol.286 , pp. 13060-13070
    • Marcello, M.R.1    Jia, W.2    Leary, J.A.3    Moore, K.L.4    Evans, J.P.5
  • 14
  • 15
    • 0028278179 scopus 로고
    • Molecular cloning of a novel Ca(2+)-binding protein (calmegin) specifically expressed during male meiotic germ cell development
    • Watanabe D, et al. (1994) Molecular cloning of a novel Ca(2+)-binding protein (calmegin) specifically expressed during male meiotic germ cell development. J Biol Chem 269:7744-7749.
    • (1994) J Biol Chem , vol.269 , pp. 7744-7749
    • Watanabe, D.1
  • 16
    • 0037019814 scopus 로고    scopus 로고
    • Identification of a novel calreticulin isoform (Crt2) in human and mouse
    • DOI 10.1016/S0378-1119(02)00880-6, PII S0378111902008806
    • Persson S, Rosenquist M, Sommarin M (2002) Identification of a novel calreticulin isoform (Crt2) in human and mouse. Gene 297:151-158. (Pubitemid 35217790)
    • (2002) Gene , vol.297 , Issue.1-2 , pp. 151-158
    • Persson, S.1    Rosenquist, M.2    Sommarin, M.3
  • 18
    • 14044271131 scopus 로고    scopus 로고
    • The human protein disulphide isomerase family: Substrate interactions and functional properties
    • DOI 10.1038/sj.embor.7400311
    • Ellgaard L, Ruddock LW (2005) The human protein disulphide isomerase family: Substrate interactions and functional properties. EMBO Rep 6:28-32. (Pubitemid 41710070)
    • (2005) EMBO Reports , vol.6 , Issue.1 , pp. 28-32
    • Ellgaard, L.1    Ruddock, L.W.2
  • 19
    • 23744499653 scopus 로고    scopus 로고
    • Diversity of the protein disulfide isomerase family: Identification of breast tumor induced Hag2 and Hag3 as novel members of the protein family
    • DOI 10.1016/j.ympev.2005.04.002, PII S1055790305001132
    • Persson S, et al. (2005) Diversity of the protein disulfide isomerase family: Identification of breast tumor induced Hag2 and Hag3 as novel members of the protein family. Mol Phylogenet Evol 36:734-740. (Pubitemid 41138906)
    • (2005) Molecular Phylogenetics and Evolution , vol.36 , Issue.3 , pp. 734-740
    • Persson, S.1    Rosenquist, M.2    Knoblach, B.3    Khosravi-Far, R.4    Sommarin, M.5    Michalak, M.6
  • 20
    • 0037013950 scopus 로고    scopus 로고
    • The oxidoreductase ERp57 efficiently reduces partially folded in preference to fully folded MHC class I molecules
    • DOI 10.1093/emboj/21.11.2655
    • Antoniou AN, et al. (2002) The oxidoreductase ERp57 efficiently reduces partially folded in preference to fully folded MHC class I molecules. EMBO J 21:2655-2663. (Pubitemid 34619381)
    • (2002) EMBO Journal , vol.21 , Issue.11 , pp. 2655-2663
    • Antoniou, A.N.1    Ford, S.2    Alphey, M.3    Osborne, A.4    Elliott, T.5    Powis, S.J.6
  • 21
    • 2442534124 scopus 로고    scopus 로고
    • ERp57 is a multifunctional thiol-disulfide oxidoreductase
    • Frickel EM, et al. (2004) ERp57 is a multifunctional thiol-disulfide oxidoreductase. J Biol Chem 279:18277-18287.
    • (2004) J Biol Chem , vol.279 , pp. 18277-18287
    • Frickel, E.M.1
  • 22
    • 12544251988 scopus 로고    scopus 로고
    • PDILT, a divergent testis-specific protein disulfide isomerase with a non-classical SXXC motif that engages in disulfidedependent interactions in the endoplasmic reticulum
    • van Lith M, Hartigan N, Hatch J, Benham AM (2005) PDILT, a divergent testis-specific protein disulfide isomerase with a non-classical SXXC motif that engages in disulfidedependent interactions in the endoplasmic reticulum. J Biol Chem 280:1376-1383.
    • (2005) J Biol Chem , vol.280 , pp. 1376-1383
    • Van Lith, M.1    Hartigan, N.2    Hatch, J.3    Benham, A.M.4
  • 23
    • 34547735918 scopus 로고    scopus 로고
    • A developmentally regulated chaperone complex for the endoplasmic reticulum of male haploid germ cells
    • van Lith M, et al. (2007) A developmentally regulated chaperone complex for the endoplasmic reticulum of male haploid germ cells. Mol Biol Cell 18:2795-2804.
    • (2007) Mol Biol Cell , vol.18 , pp. 2795-2804
    • Van Lith, M.1
  • 24
    • 33646882179 scopus 로고    scopus 로고
    • A Role for Sperm Surface Protein Disulfide Isomerase Activity in Gamete Fusion: Evidence for the Participation of ERp57
    • DOI 10.1016/j.devcel.2006.03.011, PII S1534580706001572
    • Ellerman DA, Myles DG, Primakoff P (2006) A role for sperm surface protein disulfide isomerase activity in gamete fusion: Evidence for the participation of ERp57. Dev Cell 10:831-837. (Pubitemid 43779114)
    • (2006) Developmental Cell , vol.10 , Issue.6 , pp. 831-837
    • Ellerman, D.A.1    Myles, D.G.2    Primakoff, P.3
  • 25
    • 0033523910 scopus 로고    scopus 로고
    • Glycoproteins form mixed disulphides with oxidoreductases during folding in living cells
    • Molinari M, Helenius A (1999) Glycoproteins form mixed disulphides with oxidoreductases during folding in living cells. Nature 402:90-93.
    • (1999) Nature , vol.402 , pp. 90-93
    • Molinari, M.1    Helenius, A.2
  • 26
    • 0037414440 scopus 로고    scopus 로고
    • Differential localization of ADAM1a and ADAM1b in the endoplasmic reticulum of testicular germ cells and on the surface of epididymal sperm
    • DOI 10.1016/S0006-291X(03)00588-6
    • Kim E, Nishimura H, Baba T (2003) Differential localization of ADAM1a and ADAM1b in the endoplasmic reticulum of testicular germ cells and on the surface of epididymal sperm. Biochem Biophys Res Commun 304:313-319. (Pubitemid 36444571)
    • (2003) Biochemical and Biophysical Research Communications , vol.304 , Issue.2 , pp. 313-319
    • Kim, E.1    Nishimura, H.2    Baba, T.3
  • 28
    • 0035890470 scopus 로고    scopus 로고
    • Hormone-triggered conformational changes within the insulinreceptor ectodomain: Requirement for transmembrane anchors
    • Flörke RR, et al. (2001) Hormone-triggered conformational changes within the insulinreceptor ectodomain: Requirement for transmembrane anchors. Biochem J 360:189-198.
    • (2001) Biochem J , vol.360 , pp. 189-198
    • Flörke, R.R.1
  • 29
    • 77950675728 scopus 로고    scopus 로고
    • Transgenic mouse sperm that have green acrosome and red mitochondria allow visualization of sperm and their acrosome reaction in vivo
    • Hasuwa H, et al. (2010) Transgenic mouse sperm that have green acrosome and red mitochondria allow visualization of sperm and their acrosome reaction in vivo. Exp Anim 59:105-107.
    • (2010) Exp Anim , vol.59 , pp. 105-107
    • Hasuwa, H.1
  • 31
    • 0034646876 scopus 로고    scopus 로고
    • Chaperone selection during glycoprotein translocation into the endoplasmic reticulum
    • DOI 10.1126/science.288.5464.331
    • Molinari M, Helenius A (2000) Chaperone selection during glycoprotein translocation into the endoplasmic reticulum. Science 288:331-333. (Pubitemid 30226193)
    • (2000) Science , vol.288 , Issue.5464 , pp. 331-333
    • Molinari, M.1    Helenius, A.2
  • 32
    • 35548935984 scopus 로고    scopus 로고
    • Dipeptidase-inactivated tACE action in vivo: Selective inhibition of sperm-zona pellucida binding in the mouse
    • DOI 10.1095/biolreprod.107.060004
    • Deguchi E, Tani T, Watanabe H, Yamada S, Kondoh G (2007) Dipeptidase-inactivated tACE action in vivo: Selective inhibition of sperm-zona pellucida binding in the mouse. Biol Reprod 77:794-802. (Pubitemid 350014167)
    • (2007) Biology of Reproduction , vol.77 , Issue.5 , pp. 794-802
    • Deguchi, E.1    Tani, T.2    Watanabe, H.3    Yamada, S.4    Kondoh, G.5
  • 33
    • 77954152541 scopus 로고    scopus 로고
    • Multivariate analysis of male reproductive function in Inpp5b-/- Mice reveals heterogeneity in defects in fertility, sperm-egg membrane interaction and proteolytic cleavage of sperm ADAMs
    • Marcello MR, Evans JP (2010) Multivariate analysis of male reproductive function in Inpp5b-/- mice reveals heterogeneity in defects in fertility, sperm-egg membrane interaction and proteolytic cleavage of sperm ADAMs. Mol Hum Reprod 16:492-505.
    • (2010) Mol Hum Reprod , vol.16 , pp. 492-505
    • Marcello, M.R.1    Evans, J.P.2
  • 34
    • 33745847479 scopus 로고    scopus 로고
    • Diagnosis and treatment of Parkinson disease: Molecules to medicine
    • DOI 10.1172/JCI29178
    • Savitt JM, Dawson VL, Dawson TM (2006) Diagnosis and treatment of Parkinson disease: Molecules to medicine. J Clin Invest 116:1744-1754. (Pubitemid 44033293)
    • (2006) Journal of Clinical Investigation , vol.116 , Issue.7 , pp. 1744-1754
    • Savitt, J.M.1    Dawson, V.L.2    Dawson, T.M.3
  • 35
    • 7944233158 scopus 로고    scopus 로고
    • Cell biology of protein misfolding: The examples of Alzheimer's and Parkinson's diseases
    • Selkoe DJ (2004) Cell biology of protein misfolding: The examples of Alzheimer's and Parkinson's diseases. Nat Cell Biol 6:1054-1061.
    • (2004) Nat Cell Biol , vol.6 , pp. 1054-1061
    • Selkoe, D.J.1
  • 36
    • 3142587059 scopus 로고    scopus 로고
    • Protein folding and quality control in the endoplasmic reticulum
    • DOI 10.1016/j.ceb.2004.06.012, PII S095506740400081X
    • Kleizen B, Braakman I (2004) Protein folding and quality control in the endoplasmic reticulum. Curr Opin Cell Biol 16:343-349. (Pubitemid 38903139)
    • (2004) Current Opinion in Cell Biology , vol.16 , Issue.4 , pp. 343-349
    • Kleizen, B.1    Braakman, I.2
  • 37
    • 79953232734 scopus 로고    scopus 로고
    • Most fertilizing mouse spermatozoa begin their acrosome reaction before contact with the zona pellucida during in vitro fertilization
    • Jin M, et al. (2011) Most fertilizing mouse spermatozoa begin their acrosome reaction before contact with the zona pellucida during in vitro fertilization. Proc Natl Acad Sci USA 108:4892-4896.
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 4892-4896
    • Jin, M.1
  • 38
    • 84055200837 scopus 로고    scopus 로고
    • Acrosome-reacted mouse spermatozoa recovered from the perivitelline space can fertilize other eggs
    • Inoue N, Satouh Y, Ikawa M, Okabe M, Yanagimachi R (2011) Acrosome-reacted mouse spermatozoa recovered from the perivitelline space can fertilize other eggs. Proc Natl Acad Sci USA 108:20008-20011.
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 20008-20011
    • Inoue, N.1    Satouh, Y.2    Ikawa, M.3    Okabe, M.4    Yanagimachi, R.5
  • 39
    • 54249097511 scopus 로고    scopus 로고
    • The role of the acrosomal matrix in fertilization
    • Buffone MG, Foster JA, Gerton GL (2008) The role of the acrosomal matrix in fertilization. Int J Dev Biol 52:511-522.
    • (2008) Int J Dev Biol , vol.52 , pp. 511-522
    • Buffone, M.G.1    Foster, J.A.2    Gerton, G.L.3
  • 40
    • 0002302562 scopus 로고
    • Mammalian fertilization
    • eds Knobil E, Neil JD (Raven, New York), 2nd Ed
    • Yanagimachi R (1994) Mammalian fertilization. The Physiology of Reproduction, eds Knobil E, Neil JD (Raven, New York), 2nd Ed, pp 189-317.
    • (1994) The Physiology of Reproduction , pp. 189-317
    • Yanagimachi, R.1
  • 41
    • 67449155901 scopus 로고    scopus 로고
    • Nongenomic activation of spermatozoa by steroid hormones: Facts and fictions
    • Baldi E, et al. (2009) Nongenomic activation of spermatozoa by steroid hormones: Facts and fictions. Mol Cell Endocrinol 308:39-46.
    • (2009) Mol Cell Endocrinol , vol.308 , pp. 39-46
    • Baldi, E.1
  • 42
    • 79952800026 scopus 로고    scopus 로고
    • Progesterone activates the principal Ca2+ channel of human sperm
    • Lishko PV, Botchkina IL, Kirichok Y (2011) Progesterone activates the principal Ca2+ channel of human sperm. Nature 471:387-391.
    • (2011) Nature , vol.471 , pp. 387-391
    • Lishko, P.V.1    Botchkina, I.L.2    Kirichok, Y.3
  • 43
    • 80053133500 scopus 로고    scopus 로고
    • Human sperm binding is mediated by the sialyl-Lewis(x) oligosaccharide on the zona pellucida
    • Pang PC, et al. (2011) Human sperm binding is mediated by the sialyl-Lewis(x) oligosaccharide on the zona pellucida. Science 333:1761-1764.
    • (2011) Science , vol.333 , pp. 1761-1764
    • Pang, P.C.1
  • 44
    • 0032528978 scopus 로고    scopus 로고
    • The gene for the human tMDC I sperm surface protein is non-functional: Implications for its proposed role in mammalian sperm-egg recognition
    • Frayne J, Hall L (1998) The gene for the human tMDC I sperm surface protein is nonfunctional: Implications for its proposed role in mammalian sperm-egg recognition. Biochem J 334:171-176. (Pubitemid 28420986)
    • (1998) Biochemical Journal , vol.334 , Issue.1 , pp. 171-176
    • Frayne, J.1    Hall, L.2
  • 45
    • 29544450106 scopus 로고    scopus 로고
    • Sperm transport in the female reproductive tract
    • DOI 10.1093/humupd/dmi047
    • Suarez SS, Pacey AA (2006) Sperm transport in the female reproductive tract. Hum Reprod Update 12:23-37. (Pubitemid 43013744)
    • (2006) Human Reproduction Update , vol.12 , Issue.1 , pp. 23-37
    • Suarez, S.S.1    Pacey, A.A.2
  • 46
    • 0023942614 scopus 로고
    • The hemizona assay (HZA): Development of a diagnostic test for the binding of human spermatozoa to the human hemizona pellucida to predict fertilization potential
    • Burkman LJ, et al. (1988) The hemizona assay (HZA): Development of a diagnostic test for the binding of human spermatozoa to the human hemizona pellucida to predict fertilization potential. Fertil Steril 49:688-697.
    • (1988) Fertil Steril , vol.49 , pp. 688-697
    • Burkman, L.J.1
  • 47
    • 0034104557 scopus 로고    scopus 로고
    • Defective sperm-zona pellucida interaction: A major cause of failure of fertilization in clinical in-vitro fertilization
    • Liu DY, Baker HW (2000) Defective sperm-zona pellucida interaction: A major cause of failure of fertilization in clinical in-vitro fertilization. Hum Reprod 15:702-708. (Pubitemid 30142388)
    • (2000) Human Reproduction , vol.15 , Issue.3 , pp. 702-708
    • Liu, D.Y.1    Baker, H.W.G.2
  • 48
    • 0026486420 scopus 로고
    • Characterization of male meiotic germ cell-specific antigen (Meg 1) by monoclonal antibody TRA 369 in mice
    • Watanabe D, Sawada K, Koshimizu U, Kagawa T, Nishimune Y (1992) Characterization of male meiotic germ cell-specific antigen (Meg 1) by monoclonal antibody TRA 369 in mice. Mol Reprod Dev 33:307-312.
    • (1992) Mol Reprod Dev , vol.33 , pp. 307-312
    • Watanabe, D.1    Sawada, K.2    Koshimizu, U.3    Kagawa, T.4    Nishimune, Y.5
  • 49
    • 34748822250 scopus 로고    scopus 로고
    • Loss of zona pellucida binding proteins in the acrosomal matrix disrupts acrosome biogenesis and sperm morphogenesis
    • DOI 10.1128/MCB.01029-07
    • Lin YN, Roy A, Yan W, Burns KH, Matzuk MM (2007) Loss of zona pellucida binding proteins in the acrosomal matrix disrupts acrosome biogenesis and sperm morphogenesis. Mol Cell Biol 27:6794-6805. (Pubitemid 47483630)
    • (2007) Molecular and Cellular Biology , vol.27 , Issue.19 , pp. 6794-6805
    • Lin, Y.-N.1    Roy, A.2    Yan, W.3    Burns, K.H.4    Matzuk, M.M.5
  • 50
    • 67649654442 scopus 로고    scopus 로고
    • Disruption of ADAM3 impairs the migration of sperm into oviduct in mouse
    • Yamaguchi R, et al. (2009) Disruption of ADAM3 impairs the migration of sperm into oviduct in mouse. Biol Reprod 81:142-146.
    • (2009) Biol Reprod , vol.81 , pp. 142-146
    • Yamaguchi, R.1
  • 51
    • 0026935860 scopus 로고
    • Production of normal young following insemination of frozenthawed mouse spermatozoa into fallopian tubes of pseudopregnant females
    • Nakagata N (1992) Production of normal young following insemination of frozenthawed mouse spermatozoa into fallopian tubes of pseudopregnant females. Jikken Dobutsu 41:519-522.
    • (1992) Jikken Dobutsu , vol.41 , pp. 519-522
    • Nakagata, N.1
  • 52
    • 0000617199 scopus 로고
    • Studies on the fertilization of mouse eggs in vitro I: In vitro fertilization of eggs by fresh epididymal sperm
    • Toyoda Y, Yokoyama M, Hoshi T (1971) Studies on the fertilization of mouse eggs in vitro I: In vitro fertilization of eggs by fresh epididymal sperm. Jpn J Anim Reprod 16:147-151.
    • (1971) Jpn J Anim Reprod , vol.16 , pp. 147-151
    • Toyoda, Y.1    Yokoyama, M.2    Hoshi, T.3


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