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Volumn 17, Issue 4, 2015, Pages 568-573

The role of the molecular chaperone heat shock protein A2 (HSPA2) in regulating human sperm-egg recognition

Author keywords

egg; fertilization; heat shock protein A2; molecular chaperone; sperm; sperm egg interactions

Indexed keywords

CHAPERONE; HEAT SHOCK PROTEIN; HEAT SHOCK PROTEIN A2; UNCLASSIFIED DRUG; HEAT SHOCK PROTEIN 70; HSPA2 PROTEIN, HUMAN; HSPA2 PROTEIN, MOUSE;

EID: 84973454182     PISSN: 1008682X     EISSN: 17457262     Source Type: Journal    
DOI: 10.4103/1008-682X.151395     Document Type: Conference Paper
Times cited : (64)

References (95)
  • 1
    • 0035808992 scopus 로고    scopus 로고
    • Male infertility: The case for continued research
    • McLachlan RI, de Kretser DM. Male infertility: the case for continued research. Med J Aust 2001; 174: 116-7.
    • (2001) Med J Aust , vol.174 , pp. 116-117
    • McLachlan, R.I.1    De Kretser, D.M.2
  • 2
    • 84973485746 scopus 로고    scopus 로고
    • Evaluation of the subfertile male
    • Oehninger S, Kruger T, editors. UK: Inferma UK Ltd
    • Cedenho AP. Evaluation of the subfertile male. In: Oehninger S, Kruger T, editors. Male Infertility, Diagnosis and Treatment. UK: Inferma UK Ltd.; 2007. p. 117-40.
    • (2007) Male Infertility, Diagnosis and Treatment , pp. 117-140
    • Cedenho, A.P.1
  • 4
    • 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. Defective sperm-zona pellucida interaction: a major cause of failure of fertilization in clinical in-vitro fertilization. Hum Reprod 2000; 15: 702-8.
    • (2000) Hum Reprod , vol.15 , pp. 702-708
    • Liu, D.Y.1    Baker, H.W.2
  • 5
    • 33744521493 scopus 로고    scopus 로고
    • Predictive value of the hemizona assay for pregnancy outcome in patients undergoing controlled ovarian hyperstimulation with intrauterine insemination
    • Arslan M, Morshedi M, Arslan EO, Taylor S, Kanik A, et al. Predictive value of the hemizona assay for pregnancy outcome in patients undergoing controlled ovarian hyperstimulation with intrauterine insemination. Fertil Steril 2006; 85: 1697-707.
    • (2006) Fertil Steril , vol.85 , pp. 1697-1707
    • Arslan, M.1    Morshedi, M.2    Arslan, E.O.3    Taylor, S.4    Kanik, A.5
  • 6
    • 84934437861 scopus 로고    scopus 로고
    • The hemizona assay for assessment of sperm function
    • Oehninger S, Morshedi M, Franken D. The hemizona assay for assessment of sperm function. Methods Mol Biol 2013; 927: 91-102.
    • (2013) Methods Mol Biol , vol.927 , pp. 91-102
    • Oehninger, S.1    Morshedi, M.2    Franken, D.3
  • 7
    • 0342601939 scopus 로고    scopus 로고
    • Clinical significance of human sperm-zona pellucida binding
    • Oehninger S, Mahony M, Ozgür K, Kolm P, Kruger T, et al. Clinical significance of human sperm-zona pellucida binding. Fertil Steril 1997; 67: 1121-7.
    • (1997) Fertil Steril , vol.67 , pp. 1121-1127
    • Oehninger, S.1    Mahony, M.2    Ozgür, K.3    Kolm, P.4    Kruger, T.5
  • 8
    • 32844470377 scopus 로고    scopus 로고
    • The clinical significance of sperm-zona pellucida binding: 17 years later
    • Franken DR, Oehninger S. The clinical significance of sperm-zona pellucida binding: 17 years later. Front Biosci 2006; 11: 1227-33.
    • (2006) Front Biosci , vol.11 , pp. 1227-1233
    • Franken, D.R.1    Oehninger, S.2
  • 10
    • 34447297822 scopus 로고    scopus 로고
    • Human sperm bound to the zona pellucida have normal nuclear chromatin as assessed by acridine orange fluorescence
    • Liu DY, Baker HW. Human sperm bound to the zona pellucida have normal nuclear chromatin as assessed by acridine orange fluorescence. Hum Reprod 2007; 22: 1597-602.
    • (2007) Hum Reprod , vol.22 , pp. 1597-1602
    • Liu, D.Y.1    Baker, H.W.2
  • 11
    • 79952403577 scopus 로고    scopus 로고
    • Could using the zona pellucida bound sperm for intracytoplasmic sperm injection (ICSI) enhance the outcome of ICSI?
    • Liu DY. Could using the zona pellucida bound sperm for intracytoplasmic sperm injection (ICSI) enhance the outcome of ICSI? Asian J Androl 2011; 13: 197-8.
    • (2011) Asian J Androl , vol.13 , pp. 197-198
    • Liu, D.Y.1
  • 12
    • 78751570959 scopus 로고    scopus 로고
    • Use of zona pellucida-bound sperm for intracytoplasmic sperm injection produces higher embryo quality and implantation than conventional intracytoplasmic sperm injection
    • Liu F, Qiu Y, Zou Y, Deng ZH, Yang H, et al. Use of zona pellucida-bound sperm for intracytoplasmic sperm injection produces higher embryo quality and implantation than conventional intracytoplasmic sperm injection. Fertil Steril 2011; 95: 815-8.
    • (2011) Fertil Steril , vol.95 , pp. 815-818
    • Liu, F.1    Qiu, Y.2    Zou, Y.3    Deng, Z.H.4    Yang, H.5
  • 14
    • 78650971728 scopus 로고    scopus 로고
    • Cellular mechanisms regulating sperm-zona pellucida interaction
    • Reid AT, Redgrove K, Aitken RJ, Nixon B. Cellular mechanisms regulating sperm-zona pellucida interaction. Asian J Androl 2011; 13: 88-96.
    • (2011) Asian J Androl , vol.13 , pp. 88-96
    • Reid, A.T.1    Redgrove, K.2    Aitken, R.J.3    Nixon, B.4
  • 15
    • 34548398028 scopus 로고    scopus 로고
    • Analysis of chaperone proteins associated with human spermatozoa during capacitation
    • Mitchell LA, Nixon B, Aitken RJ. Analysis of chaperone proteins associated with human spermatozoa during capacitation. Mol Hum Reprod 2007; 13: 605-13.
    • (2007) Mol Hum Reprod , vol.13 , pp. 605-613
    • Mitchell, L.A.1    Nixon, B.2    Aitken, R.J.3
  • 16
    • 4444254836 scopus 로고    scopus 로고
    • Tyrosine phosphorylation activates surface chaperones facilitating sperm-zona recognition
    • Asquith KL, Baleato RM, McLaughlin EA, Nixon B, Aitken RJ. Tyrosine phosphorylation activates surface chaperones facilitating sperm-zona recognition. J Cell Sci 2004; 117: 3645-57.
    • (2004) J Cell Sci , vol.117 , pp. 3645-3657
    • Asquith, K.L.1    Baleato, R.M.2    McLaughlin, E.A.3    Nixon, B.4    Aitken, R.J.5
  • 17
    • 84866380388 scopus 로고    scopus 로고
    • Mammalian zona pellucida glycoproteins: Structure and function during fertilization
    • Gupta SK, Bhandari B, Shrestha A, Biswal BK, Palaniappan C, et al. Mammalian zona pellucida glycoproteins: structure and function during fertilization. Cell Tissue Res 2012; 349: 665-78.
    • (2012) Cell Tissue Res , vol.349 , pp. 665-678
    • Gupta, S.K.1    Bhandari, B.2    Shrestha, A.3    Biswal, B.K.4    Palaniappan, C.5
  • 18
    • 84874290379 scopus 로고    scopus 로고
    • The role of carbohydrate recognition during human sperm-egg binding
    • Clark GF. The role of carbohydrate recognition during human sperm-egg binding. Hum Reprod 2013; 28: 566-77.
    • (2013) Hum Reprod , vol.28 , pp. 566-577
    • Clark, G.F.1
  • 19
    • 84903184002 scopus 로고    scopus 로고
    • A single domain of the ZP2 zona pellucida protein mediates gamete recognition in mice and humans
    • Avella MA, Baibakov B, Dean J. A single domain of the ZP2 zona pellucida protein mediates gamete recognition in mice and humans. J Cell Biol 2014; 205: 801-9.
    • (2014) J Cell Biol , vol.205 , pp. 801-809
    • Avella, M.A.1    Baibakov, B.2    Dean, J.3
  • 20
    • 84876995619 scopus 로고    scopus 로고
    • The molecular basis of gamete recognition in mice and humans
    • Avella MA, Xiong B, Dean J. The molecular basis of gamete recognition in mice and humans. Mol Hum Reprod 2013; 19: 279-89.
    • (2013) Mol Hum Reprod , vol.19 , pp. 279-289
    • Avella, M.A.1    Xiong, B.2    Dean, J.3
  • 21
    • 77956930530 scopus 로고    scopus 로고
    • Sperm-zona pellucida interaction: Molecular mechanisms and the potential for contraceptive intervention
    • Dun MD, Mitchell LA, Aitken RJ, Nixon B. Sperm-zona pellucida interaction: molecular mechanisms and the potential for contraceptive intervention. Handb Exp Pharmacol 2010; 198: 139-78.
    • (2010) Handb Exp Pharmacol , vol.198 , pp. 139-178
    • Dun, M.D.1    Mitchell, L.A.2    Aitken, R.J.3    Nixon, B.4
  • 22
    • 84863477544 scopus 로고    scopus 로고
    • The role of molecular chaperones in spermatogenesis and the post-testicular maturation of mammalian spermatozoa
    • Dun MD, Aitken RJ, Nixon B. The role of molecular chaperones in spermatogenesis and the post-testicular maturation of mammalian spermatozoa. Hum Reprod Update 2012; 18: 420-35.
    • (2012) Hum Reprod Update , vol.18 , pp. 420-435
    • Dun, M.D.1    Aitken, R.J.2    Nixon, B.3
  • 23
    • 80054688942 scopus 로고    scopus 로고
    • The chaperonin containing TCP1 complex (CCT/TRiC) is involved in mediating sperm-oocyte interaction
    • Dun MD, Smith ND, Baker MA, Lin M, Aitken RJ, et al. The chaperonin containing TCP1 complex (CCT/TRiC) is involved in mediating sperm-oocyte interaction. J Biol Chem 2011; 286: 36875-87.
    • (2011) J Biol Chem , vol.286 , pp. 36875-36887
    • Dun, M.D.1    Smith, N.D.2    Baker, M.A.3    Lin, M.4    Aitken, R.J.5
  • 24
    • 79960558511 scopus 로고    scopus 로고
    • Involvement of multimeric protein complexes in mediating the capacitation-dependent binding of human spermatozoa to homologous zonae pellucidae
    • Redgrove KA, Anderson AL, Dun MD, McLaughlin EA, O'Bryan MK, et al. Involvement of multimeric protein complexes in mediating the capacitation-dependent binding of human spermatozoa to homologous zonae pellucidae. Dev Biol 2011; 356: 460-74.
    • (2011) Dev Biol , vol.356 , pp. 460-474
    • Redgrove, K.A.1    Anderson, A.L.2    Dun, M.D.3    McLaughlin, E.A.4    O'Bryan, M.K.5
  • 25
    • 84876460101 scopus 로고    scopus 로고
    • Investigation of the mechanisms by which the molecular chaperone HSPA2 regulates the expression of sperm surface receptors involved in human sperm-oocyte recognition
    • Redgrove KA, Anderson AL, McLaughlin EA, O'Bryan MK, Aitken RJ, et al. Investigation of the mechanisms by which the molecular chaperone HSPA2 regulates the expression of sperm surface receptors involved in human sperm-oocyte recognition. Mol Hum Reprod 2013; 19: 120-35.
    • (2013) Mol Hum Reprod , vol.19 , pp. 120-135
    • Redgrove, K.A.1    Anderson, A.L.2    McLaughlin, E.A.3    O'Bryan, M.K.4    Aitken, R.J.5
  • 26
    • 84870562813 scopus 로고    scopus 로고
    • The molecular chaperone HSPA2 plays a key role in regulating the expression of sperm surface receptors that mediate sperm-egg recognition
    • Redgrove KA, Nixon B, Baker MA, Hetherington L, Baker G, et al. The molecular chaperone HSPA2 plays a key role in regulating the expression of sperm surface receptors that mediate sperm-egg recognition. PLoS One 2012; 7: e50851.
    • (2012) PLoS One , vol.7 , pp. e50851
    • Redgrove, K.A.1    Nixon, B.2    Baker, M.A.3    Hetherington, L.4    Baker, G.5
  • 27
    • 0025382818 scopus 로고
    • The molecular chaperone concept
    • Ellis RJ. The molecular chaperone concept. Semin Cell Biol 1990; 1: 1-9.
    • (1990) Semin Cell Biol , vol.1 , pp. 1-9
    • Ellis, R.J.1
  • 28
    • 0030154255 scopus 로고    scopus 로고
    • Discovery of the heat shock response
    • Ritossa F. Discovery of the heat shock response. Cell Stress Chaperones 1996; 1: 97-8.
    • (1996) Cell Stress Chaperones , vol.1 , pp. 97-98
    • Ritossa, F.1
  • 29
    • 84886412961 scopus 로고    scopus 로고
    • Chaperone machines for protein folding, unfolding and disaggregation
    • Saibil H. Chaperone machines for protein folding, unfolding and disaggregation. Nat Rev Mol Cell Biol 2013; 14: 630-42.
    • (2013) Nat Rev Mol Cell Biol , vol.14 , pp. 630-642
    • Saibil, H.1
  • 31
    • 46849116411 scopus 로고    scopus 로고
    • Structural and functional diversities between members of the human HSPB, HSPH, HSPA, and DNAJ chaperone families
    • Vos MJ, Hageman J, Carra S, Kampinga HH. Structural and functional diversities between members of the human HSPB, HSPH, HSPA, and DNAJ chaperone families. Biochemistry 2008; 47: 7001-11.
    • (2008) Biochemistry , vol.47 , pp. 7001-7011
    • Vos, M.J.1    Hageman, J.2    Carra, S.3    Kampinga, H.H.4
  • 32
    • 33646127577 scopus 로고    scopus 로고
    • Molecular chaperones and protein quality control
    • Bukau B, Weissman J, Horwich A. Molecular chaperones and protein quality control. Cell 2006; 125: 443-51.
    • (2006) Cell , vol.125 , pp. 443-451
    • Bukau, B.1    Weissman, J.2    Horwich, A.3
  • 33
    • 39149143645 scopus 로고    scopus 로고
    • Chaperone machines in action
    • Saibil HR. Chaperone machines in action. Curr Opin Struct Biol 2008; 18: 35-42.
    • (2008) Curr Opin Struct Biol , vol.18 , pp. 35-42
    • Saibil, H.R.1
  • 34
    • 84884589727 scopus 로고    scopus 로고
    • Hsp70 chaperone dynamics and molecular mechanism
    • Mayer MP. Hsp70 chaperone dynamics and molecular mechanism. Trends Biochem Sci 2013; 38: 507-14.
    • (2013) Trends Biochem Sci , vol.38 , pp. 507-514
    • Mayer, M.P.1
  • 35
    • 17044387386 scopus 로고    scopus 로고
    • Hsp70 chaperones: Cellular functions and molecular mechanism
    • Mayer MP, Bukau B. Hsp70 chaperones: cellular functions and molecular mechanism. Cell Mol Life Sci 2005; 62: 670-84.
    • (2005) Cell Mol Life Sci , vol.62 , pp. 670-684
    • Mayer, M.P.1    Bukau, B.2
  • 36
    • 77954947810 scopus 로고    scopus 로고
    • The HSP70 chaperone machinery: J proteins as drivers of functional specificity
    • Kampinga HH, Craig EA. The HSP70 chaperone machinery: J proteins as drivers of functional specificity. Nat Rev Mol Cell Biol 2010; 11: 579-92.
    • (2010) Nat Rev Mol Cell Biol , vol.11 , pp. 579-592
    • Kampinga, H.H.1    Craig, E.A.2
  • 37
    • 0033064556 scopus 로고    scopus 로고
    • Role of heat shock protein HSP70-2 in spermatogenesis
    • Eddy EM. Role of heat shock protein HSP70-2 in spermatogenesis. Rev Reprod 1999; 4: 23-30.
    • (1999) Rev Reprod , vol.4 , pp. 23-30
    • Eddy, E.M.1
  • 38
    • 33845999596 scopus 로고    scopus 로고
    • Post-meiotic shifts in HSPA2/HSP70.2 chaperone activity during mouse spermatogenesis
    • Govin J, Caron C, Escoffier E, Ferro M, Kuhn L, et al. Post-meiotic shifts in HSPA2/HSP70.2 chaperone activity during mouse spermatogenesis. J Biol Chem 2006; 281: 37888-92.
    • (2006) J Biol Chem , vol.281 , pp. 37888-37892
    • Govin, J.1    Caron, C.2    Escoffier, E.3    Ferro, M.4    Kuhn, L.5
  • 40
    • 0023959196 scopus 로고
    • A novel hsp70-like protein (P70) is present in mouse spermatogenic cells
    • Allen RL, O'Brien DA, Eddy EM. A novel hsp70-like protein (P70) is present in mouse spermatogenic cells. Mol Cell Biol 1988; 8: 828-32.
    • (1988) Mol Cell Biol , vol.8 , pp. 828-832
    • Allen, R.L.1    O'Brien, D.A.2    Eddy, E.M.3
  • 41
    • 0023394476 scopus 로고
    • Stage-specific protein synthesis by isolated spermatogenic cells throughout meiosis and early spermiogenesis in the mouse
    • O'Brien DA. Stage-specific protein synthesis by isolated spermatogenic cells throughout meiosis and early spermiogenesis in the mouse. Biol Reprod 1987; 37: 147-57.
    • (1987) Biol Reprod , vol.37 , pp. 147-157
    • O'Brien, D.A.1
  • 42
    • 0023921692 scopus 로고
    • Identification and sequence analysis of a new member of the mouse HSP70 gene family and characterization of its unique cellular and developmental pattern of expression in the male germ line
    • Zakeri ZF, Wolgemuth DJ, Hunt CR. Identification and sequence analysis of a new member of the mouse HSP70 gene family and characterization of its unique cellular and developmental pattern of expression in the male germ line. Mol Cell Biol 1988; 8: 2925-32.
    • (1988) Mol Cell Biol , vol.8 , pp. 2925-2932
    • Zakeri, Z.F.1    Wolgemuth, D.J.2    Hunt, C.R.3
  • 43
    • 0026517306 scopus 로고
    • Identification of the gene for the developmentally expressed 70 kDa heat-shock protein (P70) of mouse spermatogenic cells
    • Rosario MO, Perkins SL, O'Brien DA, Allen RL, Eddy EM. Identification of the gene for the developmentally expressed 70 kDa heat-shock protein (P70) of mouse spermatogenic cells. Dev Biol 1992; 150: 1-11.
    • (1992) Dev Biol , vol.150 , pp. 1-11
    • Rosario, M.O.1    Perkins, S.L.2    O'Brien, D.A.3    Allen, R.L.4    Eddy, E.M.5
  • 44
    • 0030034672 scopus 로고    scopus 로고
    • Distinct transcripts are recognized by sense and antisense riboprobes for a member of the murine HSP70 gene family, HSP70.2, in various reproductive tissues
    • Murashov AK, Wolgemuth DJ. Distinct transcripts are recognized by sense and antisense riboprobes for a member of the murine HSP70 gene family, HSP70.2, in various reproductive tissues. Mol Reprod Dev 1996; 43: 17-24.
    • (1996) Mol Reprod Dev , vol.43 , pp. 17-24
    • Murashov, A.K.1    Wolgemuth, D.J.2
  • 45
    • 0029879539 scopus 로고    scopus 로고
    • Developmentally regulated expression of Hsp70-2 and a Hsp70-2/lacZ transgene during spermatogenesis
    • Dix DJ, Rosario-Herrle M, Gotoh H, Mori C, Goulding EH, et al. Developmentally regulated expression of Hsp70-2 and a Hsp70-2/lacZ transgene during spermatogenesis. Dev Biol 1996; 174: 310-21.
    • (1996) Dev Biol , vol.174 , pp. 310-321
    • Dix, D.J.1    Rosario-Herrle, M.2    Gotoh, H.3    Mori, C.4    Goulding, E.H.5
  • 46
    • 0030721027 scopus 로고    scopus 로고
    • HSP70-2 is required for desynapsis of synaptonemal complexes during meiotic prophase in juvenile and adult mouse spermatocytes
    • Dix DJ, Allen JW, Collins BW, Poorman-Allen P, Mori C, et al. HSP70-2 is required for desynapsis of synaptonemal complexes during meiotic prophase in juvenile and adult mouse spermatocytes. Development 1997; 124: 4595-603.
    • (1997) Development , vol.124 , pp. 4595-4603
    • Dix, D.J.1    Allen, J.W.2    Collins, B.W.3    Poorman-Allen, P.4    Mori, C.5
  • 47
    • 0029991234 scopus 로고    scopus 로고
    • Targeted gene disruption of Hsp70-2 results in failed meiosis, germ cell apoptosis, and male infertility
    • Dix DJ, Allen JW, Collins BW, Mori C, Nakamura N, et al. Targeted gene disruption of Hsp70-2 results in failed meiosis, germ cell apoptosis, and male infertility. Proc Natl Acad Sci U S A 1996; 93: 3264-8.
    • (1996) Proc Natl Acad Sci U S A , vol.93 , pp. 3264-3268
    • Dix, D.J.1    Allen, J.W.2    Collins, B.W.3    Mori, C.4    Nakamura, N.5
  • 48
    • 0031033802 scopus 로고    scopus 로고
    • Morphological analysis of germ cell apoptosis during postnatal testis development in normal and Hsp 70-2 knockout mice
    • Mori C, Nakamura N, Dix DJ, Fujioka M, Nakagawa S, et al. Morphological analysis of germ cell apoptosis during postnatal testis development in normal and Hsp 70-2 knockout mice. Dev Dyn 1997; 208: 125-36.
    • (1997) Dev Dyn , vol.208 , pp. 125-136
    • Mori, C.1    Nakamura, N.2    Dix, D.J.3    Fujioka, M.4    Nakagawa, S.5
  • 49
    • 0029981194 scopus 로고    scopus 로고
    • HSP70-2 is part of the synaptonemal complex in mouse and hamster spermatocytes
    • Allen JW, Dix DJ, Collins BW, Merrick BA, He C, et al. HSP70-2 is part of the synaptonemal complex in mouse and hamster spermatocytes. Chromosoma 1996; 104: 414-21.
    • (1996) Chromosoma , vol.104 , pp. 414-421
    • Allen, J.W.1    Dix, D.J.2    Collins, B.W.3    Merrick, B.A.4    He, C.5
  • 50
    • 0030864750 scopus 로고    scopus 로고
    • HSP70-2 is required for CDC2 kinase activity in meiosis I of mouse spermatocytes
    • Zhu D, Dix DJ, Eddy EM. HSP70-2 is required for CDC2 kinase activity in meiosis I of mouse spermatocytes. Development 1997; 124: 3007-14.
    • (1997) Development , vol.124 , pp. 3007-3014
    • Zhu, D.1    Dix, D.J.2    Eddy, E.M.3
  • 51
    • 84900536604 scopus 로고    scopus 로고
    • SHCBP1L, a conserved protein in mammals, is predominantly expressed in male germ cells and maintains spindle stability during meiosis in testis
    • Liu M, Shi X, Bi Y, Qi L, Guo X, et al. SHCBP1L, a conserved protein in mammals, is predominantly expressed in male germ cells and maintains spindle stability during meiosis in testis. Mol Hum Reprod 2014; 20: 463-75.
    • (2014) Mol Hum Reprod , vol.20 , pp. 463-475
    • Liu, M.1    Shi, X.2    Bi, Y.3    Qi, L.4    Guo, X.5
  • 52
    • 74049152341 scopus 로고    scopus 로고
    • Linker histones stimulate HSPA2 ATPase activity through NASP binding and inhibit CDC2/Cyclin B1 complex formation during meiosis in the mouse
    • Alekseev OM, Richardson RT, O'Rand MG. Linker histones stimulate HSPA2 ATPase activity through NASP binding and inhibit CDC2/Cyclin B1 complex formation during meiosis in the mouse. Biol Reprod 2009; 81: 739-48.
    • (2009) Biol Reprod , vol.81 , pp. 739-748
    • Alekseev, O.M.1    Richardson, R.T.2    O'Rand, M.G.3
  • 53
    • 77955409741 scopus 로고    scopus 로고
    • MOV10L1 is necessary for protection of spermatocytes against retrotransposons by Piwi-interacting RNAs
    • Frost RJ, Hamra FK, Richardson JA, Qi X, Bassel-Duby R, et al. MOV10L1 is necessary for protection of spermatocytes against retrotransposons by Piwi-interacting RNAs. Proc Natl Acad Sci U S A 2010; 107: 11847-52.
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 11847-11852
    • Frost, R.J.1    Hamra, F.K.2    Richardson, J.A.3    Qi, X.4    Bassel-Duby, R.5
  • 54
    • 49749130037 scopus 로고    scopus 로고
    • Bat3 deficiency accelerates the degradation of Hsp70-2/HspA2 during spermatogenesis
    • Sasaki T, Marcon E, McQuire T, Arai Y, Moens PB, et al. Bat3 deficiency accelerates the degradation of Hsp70-2/HspA2 during spermatogenesis. J Cell Biol 2008; 182: 449-58.
    • (2008) J Cell Biol , vol.182 , pp. 449-458
    • Sasaki, T.1    Marcon, E.2    McQuire, T.3    Arai, Y.4    Moens, P.B.5
  • 55
    • 0035282773 scopus 로고    scopus 로고
    • Reversible inhibition of Hsp70 chaperone function by Scythe and Reaper
    • Thress K, Song J, Morimoto RI, Kornbluth S. Reversible inhibition of Hsp70 chaperone function by Scythe and Reaper. EMBO J 2001; 20: 1033-41.
    • (2001) EMBO J , vol.20 , pp. 1033-1041
    • Thress, K.1    Song, J.2    Morimoto, R.I.3    Kornbluth, S.4
  • 56
    • 15844380966 scopus 로고    scopus 로고
    • Chromatin remodelling and epigenetic features of germ cells
    • Kimmins S, Sassone-Corsi P. Chromatin remodelling and epigenetic features of germ cells. Nature 2005; 434: 583-9.
    • (2005) Nature , vol.434 , pp. 583-589
    • Kimmins, S.1    Sassone-Corsi, P.2
  • 57
    • 34547096281 scopus 로고    scopus 로고
    • CatSperbeta, a novel transmembrane protein in the CatSper channel complex
    • Liu J, Xia J, Cho KH, Clapham DE, Ren D. CatSperbeta, a novel transmembrane protein in the CatSper channel complex. J Biol Chem 2007; 282: 18945-52.
    • (2007) J Biol Chem , vol.282 , pp. 18945-18952
    • Liu, J.1    Xia, J.2    Cho, K.H.3    Clapham, D.E.4    Ren, D.5
  • 58
    • 0027965687 scopus 로고
    • Cloning, sequencing, and mapping of the human chromosome 14 heat shock protein gene (HSPA2)
    • Bonnycastle LL, Yu CE, Hunt CR, Trask BJ, Clancy KP, et al. Cloning, sequencing, and mapping of the human chromosome 14 heat shock protein gene (HSPA2). Genomics 1994; 23: 85-93.
    • (1994) Genomics , vol.23 , pp. 85-93
    • Bonnycastle, L.L.1    Yu, C.E.2    Hunt, C.R.3    Trask, B.J.4    Clancy, K.P.5
  • 59
    • 0032697684 scopus 로고    scopus 로고
    • Specific expression of heat shock protein HspA2 in human male germ cells
    • Son WY, Hwang SH, Han CT, Lee JH, Kim S, et al. Specific expression of heat shock protein HspA2 in human male germ cells. Mol Hum Reprod 1999; 5: 1122-6.
    • (1999) Mol Hum Reprod , vol.5 , pp. 1122-1126
    • Son, W.Y.1    Hwang, S.H.2    Han, C.T.3    Lee, J.H.4    Kim, S.5
  • 60
    • 0033837992 scopus 로고    scopus 로고
    • Putative creatine kinase M-isoform in human sperm is identifiedas the 70-kilodalton heat shock protein HspA2
    • Huszar G, Stone K, Dix D, Vigue L. Putative creatine kinase M-isoform in human sperm is identifiedas the 70-kilodalton heat shock protein HspA2. Biol Reprod 2000; 63: 925-32.
    • (2000) Biol Reprod , vol.63 , pp. 925-932
    • Huszar, G.1    Stone, K.2    Dix, D.3    Vigue, L.4
  • 61
    • 33746020449 scopus 로고    scopus 로고
    • Oligozoospermia and heat-shock protein expression in ejaculated spermatozoa
    • Cedenho AP, Lima SB, Cenedeze MA, Spaine DM, Ortiz V, et al. Oligozoospermia and heat-shock protein expression in ejaculated spermatozoa. Hum Reprod 2006; 21: 1791-4.
    • (2006) Hum Reprod , vol.21 , pp. 1791-1794
    • Cedenho, A.P.1    Lima, S.B.2    Cenedeze, M.A.3    Spaine, D.M.4    Ortiz, V.5
  • 62
    • 0034076573 scopus 로고    scopus 로고
    • Repression of hspA2 messenger RNA in human testes with abnormal spermatogenesis
    • Son WY, Han CT, Hwang SH, Lee JH, Kim S, et al. Repression of hspA2 messenger RNA in human testes with abnormal spermatogenesis. Fertil Steril 2000; 73: 1138-44.
    • (2000) Fertil Steril , vol.73 , pp. 1138-1144
    • Son, W.Y.1    Han, C.T.2    Hwang, S.H.3    Lee, J.H.4    Kim, S.5
  • 63
    • 0030978645 scopus 로고    scopus 로고
    • Sperm plasma membrane remodeling during spermiogenetic maturation in men: Relationship among plasma membrane beta 1,4-galactosyltransferase, cytoplasmic creatine phosphokinase, and creatine phosphokinase isoform ratios
    • Huszar G, Sbracia M, Vigue L, Miller DJ, Shur BD. Sperm plasma membrane remodeling during spermiogenetic maturation in men: relationship among plasma membrane beta 1,4-galactosyltransferase, cytoplasmic creatine phosphokinase, and creatine phosphokinase isoform ratios. Biol Reprod 1997; 56: 1020-4.
    • (1997) Biol Reprod , vol.56 , pp. 1020-1024
    • Huszar, G.1    Sbracia, M.2    Vigue, L.3    Miller, D.J.4    Shur, B.D.5
  • 64
    • 0036257410 scopus 로고    scopus 로고
    • Sperm maturity and treatment choice of in vitro fertilization (IVF) or intracytoplasmic sperm injection: Diminished sperm HspA2 chaperone levels predict IVF failure
    • Ergur AR, Dokras A, Giraldo JL, Habana A, Kovanci E, et al. Sperm maturity and treatment choice of in vitro fertilization (IVF) or intracytoplasmic sperm injection: diminished sperm HspA2 chaperone levels predict IVF failure. Fertil Steril 2002; 77: 910-8.
    • (2002) Fertil Steril , vol.77 , pp. 910-918
    • Ergur, A.R.1    Dokras, A.2    Giraldo, J.L.3    Habana, A.4    Kovanci, E.5
  • 65
    • 33744967944 scopus 로고    scopus 로고
    • Hyaluronic acid binding ability of human sperm reflects cellular maturity and fertilizing potential: Selection of sperm for intracytoplasmic sperm injection
    • Huszar G, Ozkavukcu S, Jakab A, Celik-Ozenci C, Sati GL, et al. Hyaluronic acid binding ability of human sperm reflects cellular maturity and fertilizing potential: selection of sperm for intracytoplasmic sperm injection. Curr Opin Obstet Gynecol 2006; 18: 260-7.
    • (2006) Curr Opin Obstet Gynecol , vol.18 , pp. 260-267
    • Huszar, G.1    Ozkavukcu, S.2    Jakab, A.3    Celik-Ozenci, C.4    Sati, G.L.5
  • 66
    • 0038276009 scopus 로고    scopus 로고
    • Hyaluronic acid binding by human sperm indicates cellular maturity, viability, and unreacted acrosomal status
    • Huszar G, Ozenci CC, Cayli S, Zavaczki Z, Hansch E, et al. Hyaluronic acid binding by human sperm indicates cellular maturity, viability, and unreacted acrosomal status. Fertil Steril 2003; 79 Suppl 3: 1616-24.
    • (2003) Fertil Steril , vol.79 , pp. 1616-1624
    • Huszar, G.1    Ozenci, C.C.2    Cayli, S.3    Zavaczki, Z.4    Hansch, E.5
  • 67
    • 0034964960 scopus 로고    scopus 로고
    • FISH assessment of aneuploidy frequencies in mature and immature human spermatozoa classified by the absence or presence of cytoplasmic retention
    • Kovanci E, Kovacs T, Moretti E, Vigue L, Bray-Ward P, et al. FISH assessment of aneuploidy frequencies in mature and immature human spermatozoa classified by the absence or presence of cytoplasmic retention. Hum Reprod 2001; 16: 1209-17.
    • (2001) Hum Reprod , vol.16 , pp. 1209-1217
    • Kovanci, E.1    Kovacs, T.2    Moretti, E.3    Vigue, L.4    Bray-Ward, P.5
  • 68
    • 34248635671 scopus 로고    scopus 로고
    • Fertility testing and ICSI sperm selection by hyaluronic acid binding: Clinical and genetic aspects
    • Huszar G, Jakab A, Sakkas D, Ozenci CC, Cayli S, et al. Fertility testing and ICSI sperm selection by hyaluronic acid binding: clinical and genetic aspects. Reprod Biomed Online 2007; 14: 650-63.
    • (2007) Reprod Biomed Online , vol.14 , pp. 650-663
    • Huszar, G.1    Jakab, A.2    Sakkas, D.3    Ozenci, C.C.4    Cayli, S.5
  • 69
    • 73149115984 scopus 로고    scopus 로고
    • Heat shock proteins on the human sperm surface
    • Naaby-Hansen S, Herr JC. Heat shock proteins on the human sperm surface. J Reprod Immunol 2010; 84: 32-40.
    • (2010) J Reprod Immunol , vol.84 , pp. 32-40
    • Naaby-Hansen, S.1    Herr, J.C.2
  • 71
    • 84925465588 scopus 로고    scopus 로고
    • Expression, function, and regulation of the testis-enriched heat shock HSPA2 gene in rodents and humans
    • Scieglinska D, Krawczyk Z. Expression, function, and regulation of the testis-enriched heat shock HSPA2 gene in rodents and humans. Cell Stress Chaperones 2014; 20: 221-35.
    • (2014) Cell Stress Chaperones , vol.20 , pp. 221-235
    • Scieglinska, D.1    Krawczyk, Z.2
  • 73
    • 84864344828 scopus 로고    scopus 로고
    • Sperm arylsulfatase A binds to mZP2 and mZP3 glycoproteins in a nonenzymatic manner
    • Xu H, Liu F, Srakaew N, Koppisetty C, Nyholm PG, et al. Sperm arylsulfatase A binds to mZP2 and mZP3 glycoproteins in a nonenzymatic manner. Reproduction 2012; 144: 209-19.
    • (2012) Reproduction , vol.144 , pp. 209-219
    • Xu, H.1    Liu, F.2    Srakaew, N.3    Koppisetty, C.4    Nyholm, P.G.5
  • 74
    • 34548483869 scopus 로고    scopus 로고
    • Sperm surface arylsulfatase A can disperse the cumulus matrix of cumulus oocyte complexes
    • Wu A, Anupriwan A, Iamsaard S, Chakrabandhu K, Santos DC, et al. Sperm surface arylsulfatase A can disperse the cumulus matrix of cumulus oocyte complexes. J Cell Physiol 2007; 213: 201-11.
    • (2007) J Cell Physiol , vol.213 , pp. 201-211
    • Wu, A.1    Anupriwan, A.2    Iamsaard, S.3    Chakrabandhu, K.4    Santos, D.C.5
  • 76
    • 0036086126 scopus 로고    scopus 로고
    • Arylsulfatase a is present on the pig sperm surface and is involved in sperm-zona pellucida binding
    • Carmona E, Weerachatyanukul W, Soboloff T, Fluharty AL, White D, et al. Arylsulfatase a is present on the pig sperm surface and is involved in sperm-zona pellucida binding. Dev Biol 2002; 247: 182-96.
    • (2002) Dev Biol , vol.247 , pp. 182-196
    • Carmona, E.1    Weerachatyanukul, W.2    Soboloff, T.3    Fluharty, A.L.4    White, D.5
  • 77
    • 84863828568 scopus 로고    scopus 로고
    • Functional characterization of double-knockout mouse sperm lacking SPAM1 and ACR or SPAM1 and PRSS21 in fertilization
    • Zhou C, Kang W, Baba T. Functional characterization of double-knockout mouse sperm lacking SPAM1 and ACR or SPAM1 and PRSS21 in fertilization. J Reprod Dev 2012; 58: 330-7.
    • (2012) J Reprod Dev , vol.58 , pp. 330-337
    • Zhou, C.1    Kang, W.2    Baba, T.3
  • 78
    • 80053386835 scopus 로고    scopus 로고
    • Germ-cell hyaluronidases: Their roles in sperm function
    • Martin-Deleon PA. Germ-cell hyaluronidases: their roles in sperm function. Int J Androl 2011; 34: e306-18.
    • (2011) Int J Androl , vol.34 , pp. e306-e318
    • Martin-Deleon, P.A.1
  • 79
    • 73349141731 scopus 로고    scopus 로고
    • Functional roles of mouse sperm hyaluronidases, HYAL5 and SPAM1, in fertilization
    • Kimura M, Kim E, Kang W, Yamashita M, Saigo M, et al. Functional roles of mouse sperm hyaluronidases, HYAL5 and SPAM1, in fertilization. Biol Reprod 2009; 81: 939-47.
    • (2009) Biol Reprod , vol.81 , pp. 939-947
    • Kimura, M.1    Kim, E.2    Kang, W.3    Yamashita, M.4    Saigo, M.5
  • 80
    • 2642527705 scopus 로고    scopus 로고
    • Cellular maturity and apoptosis in human sperm: Creatine kinase, caspase-3 and Bcl-XL levels in mature and diminished maturity sperm
    • Cayli S, Sakkas D, Vigue L, Demir R, Huszar G. Cellular maturity and apoptosis in human sperm: creatine kinase, caspase-3 and Bcl-XL levels in mature and diminished maturity sperm. Mol Hum Reprod 2004; 10: 365-72.
    • (2004) Mol Hum Reprod , vol.10 , pp. 365-372
    • Cayli, S.1    Sakkas, D.2    Vigue, L.3    Demir, R.4    Huszar, G.5
  • 82
    • 79951518607 scopus 로고    scopus 로고
    • Molecular targets of oxidative stress
    • Avery SV. Molecular targets of oxidative stress. Biochem J 2011; 434: 201-10.
    • (2011) Biochem J , vol.434 , pp. 201-210
    • Avery, S.V.1
  • 83
    • 77950923479 scopus 로고    scopus 로고
    • Surfing the wave, cycle, life history, and genes/proteins expressed by testicular germ cells. Part 1: Background to spermatogenesis, spermatogonia, and spermatocytes
    • Hermo L, Pelletier RM, Cyr DG, Smith CE. Surfing the wave, cycle, life history, and genes/proteins expressed by testicular germ cells. Part 1: background to spermatogenesis, spermatogonia, and spermatocytes. Microsc Res Tech 2010; 73: 241-78.
    • (2010) Microsc Res Tech , vol.73 , pp. 241-278
    • Hermo, L.1    Pelletier, R.M.2    Cyr, D.G.3    Smith, C.E.4
  • 84
    • 33751170221 scopus 로고    scopus 로고
    • Expression of the HSPA2 gene in ejaculated spermatozoa from adolescents with and without varicocele
    • Lima SB, Cenedeze MA, Bertolla RP, Filho PA, Oehninger S, et al. Expression of the HSPA2 gene in ejaculated spermatozoa from adolescents with and without varicocele. Fertil Steril 2006; 86: 1659-63.
    • (2006) Fertil Steril , vol.86 , pp. 1659-1663
    • Lima, S.B.1    Cenedeze, M.A.2    Bertolla, R.P.3    Filho, P.A.4    Oehninger, S.5
  • 85
    • 0031805926 scopus 로고    scopus 로고
    • Analysis of the impact of intracellular reactive oxygen species generation on the structural and functional integrity of human spermatozoa: Lipid peroxidation, DNA fragmentation and effectiveness of antioxidants
    • Twigg J, Fulton N, Gomez E, Irvine DS, Aitken RJ. Analysis of the impact of intracellular reactive oxygen species generation on the structural and functional integrity of human spermatozoa: lipid peroxidation, DNA fragmentation and effectiveness of antioxidants. Hum Reprod 1998; 13: 1429-36.
    • (1998) Hum Reprod , vol.13 , pp. 1429-1436
    • Twigg, J.1    Fulton, N.2    Gomez, E.3    Irvine, D.S.4    Aitken, R.J.5
  • 86
    • 0027952740 scopus 로고
    • Correlation between the rate of lipid peroxidation and cellular maturity as measured by creatine kinase activity in human spermatozoa
    • Huszar G, Vigue L. Correlation between the rate of lipid peroxidation and cellular maturity as measured by creatine kinase activity in human spermatozoa. J Androl 1994; 15: 71-7.
    • (1994) J Androl , vol.15 , pp. 71-77
    • Huszar, G.1    Vigue, L.2
  • 87
    • 77950342737 scopus 로고    scopus 로고
    • Phosphoglycerate kinase 2 (PGK2) is essential for sperm function and male fertility in mice
    • Danshina PV, Geyer CB, Dai Q, Goulding EH, Willis WD, et al. Phosphoglycerate kinase 2 (PGK2) is essential for sperm function and male fertility in mice. Biol Reprod 2010; 82: 136-45.
    • (2010) Biol Reprod , vol.82 , pp. 136-145
    • Danshina, P.V.1    Geyer, C.B.2    Dai, Q.3    Goulding, E.H.4    Willis, W.D.5
  • 88
    • 33646731568 scopus 로고    scopus 로고
    • Expression profiling reveals meiotic male germ cell mRNAs that are translationally up- and down-regulated
    • Iguchi N, Tobias JW, Hecht NB. Expression profiling reveals meiotic male germ cell mRNAs that are translationally up- and down-regulated. Proc Natl Acad Sci U S A 2006; 103: 7712-7.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 7712-7717
    • Iguchi, N.1    Tobias, J.W.2    Hecht, N.B.3
  • 89
    • 84866529392 scopus 로고    scopus 로고
    • Electrophilic aldehydes generated by sperm metabolism activate mitochondrial reactive oxygen species generation and apoptosis by targeting succinate dehydrogenase
    • Aitken RJ, Whiting S, De Iuliis GN, McClymont S, Mitchell LA, et al. Electrophilic aldehydes generated by sperm metabolism activate mitochondrial reactive oxygen species generation and apoptosis by targeting succinate dehydrogenase. J Biol Chem 2012; 287: 33048-60.
    • (2012) J Biol Chem , vol.287 , pp. 33048-33060
    • Aitken, R.J.1    Whiting, S.2    De Iuliis, G.N.3    McClymont, S.4    Mitchell, L.A.5
  • 90
    • 0032780007 scopus 로고    scopus 로고
    • 4-hydroxynonenal triggers an epidermal growth factor receptor-linked signal pathway for growth inhibition
    • Liu W, Akhand AA, Kato M, Yokoyama I, Miyata T, et al. 4-hydroxynonenal triggers an epidermal growth factor receptor-linked signal pathway for growth inhibition. J Cell Sci 1999; 112 (Pt 14): 2409-17.
    • (1999) J Cell Sci , vol.112 , pp. 2409-2417
    • Liu, W.1    Akhand, A.A.2    Kato, M.3    Yokoyama, I.4    Miyata, T.5
  • 91
    • 0041669528 scopus 로고    scopus 로고
    • The proteasomal system and HNE-modified proteins
    • Grune T, Davies KJ. The proteasomal system and HNE-modified proteins. Mol Aspects Med 2003; 24: 195-204.
    • (2003) Mol Aspects Med , vol.24 , pp. 195-204
    • Grune, T.1    Davies, K.J.2
  • 92
    • 84862736551 scopus 로고    scopus 로고
    • Degradation of damaged proteins: The main function of the 20S proteasome
    • Pickering AM, Davies KJ. Degradation of damaged proteins: the main function of the 20S proteasome. Prog Mol Biol Transl Sci 2012; 109: 227-48.
    • (2012) Prog Mol Biol Transl Sci , vol.109 , pp. 227-248
    • Pickering, A.M.1    Davies, K.J.2
  • 93
    • 0034798361 scopus 로고    scopus 로고
    • Protein oxidation and 20S proteasome-dependent proteolysis in mammalian cells
    • Shringarpure R, Grune T, Davies KJ. Protein oxidation and 20S proteasome-dependent proteolysis in mammalian cells. Cell Mol Life Sci 2001; 58: 1442-50.
    • (2001) Cell Mol Life Sci , vol.58 , pp. 1442-1450
    • Shringarpure, R.1    Grune, T.2    Davies, K.J.3
  • 94
    • 9444236763 scopus 로고    scopus 로고
    • Ubiquitin-dependent lysosomal degradation of the HNE-modified proteins in lens epithelial cells
    • Marques C, Pereira P, Taylor A, Liang JN, Reddy VN, et al. Ubiquitin-dependent lysosomal degradation of the HNE-modified proteins in lens epithelial cells. FASEB J 2004; 18: 1424-6.
    • (2004) FASEB J , vol.18 , pp. 1424-1426
    • Marques, C.1    Pereira, P.2    Taylor, A.3    Liang, J.N.4    Reddy, V.N.5
  • 95
    • 84874068095 scopus 로고    scopus 로고
    • The function of chaperone proteins in the assemblage of protein complexes involved in gamete adhesion and fusion processes
    • Bromfield EG, Nixon B. The function of chaperone proteins in the assemblage of protein complexes involved in gamete adhesion and fusion processes. Reproduction 2013; 145: R31-42.
    • (2013) Reproduction , vol.145 , pp. R31-42
    • Bromfield, E.G.1    Nixon, B.2


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