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Volumn 69, Issue 4, 2003, Pages 1330-1340

Loss of nectin-2 at sertoli-spermatid junctions leads to male infertility and correlates with severe spermatozoan head and midpiece malformation, impaired binding to the zona pellucida, and oocyte penetration

Author keywords

Fertilization; Sertoli cells; Sperm; Spermatid; Spermatogenesis

Indexed keywords

CELL ADHESION MOLECULE; ESPIN; IMMUNOGLOBULIN; NECTIN 2; PROTEIN; UNCLASSIFIED DRUG;

EID: 0141460514     PISSN: 00063363     EISSN: None     Source Type: Journal    
DOI: 10.1095/biolreprod.102.014670     Document Type: Article
Times cited : (113)

References (55)
  • 1
    • 0025894092 scopus 로고
    • Cadherin cell adhesion receptors as a morphogenetic regulator
    • Takeichi M. Cadherin cell adhesion receptors as a morphogenetic regulator. Science 1991; 251:1451-1455.
    • (1991) Science , vol.251 , pp. 1451-1455
    • Takeichi, M.1
  • 2
    • 0031440104 scopus 로고    scopus 로고
    • Molecular and functional analysis of cadherin-based adherens junctions
    • Yap AS, Brieher WM, Gumbiner BM. Molecular and functional analysis of cadherin-based adherens junctions. Annu Rev Cell Dev Biol 1997; 13:119-146.
    • (1997) Annu Rev Cell Dev Biol , vol.13 , pp. 119-146
    • Yap, A.S.1    Brieher, W.M.2    Gumbiner, B.M.3
  • 3
    • 0033519211 scopus 로고    scopus 로고
    • Nectin/PRR: An immunoglobulin-like cell adhesion molecule recruited to cadherin-based adherens junctions through interaction with Afadin, a PDZ domain-containing protein
    • Takahashi K, Nakanishi H, Miyahara M, Mandai K, Satoh K, Satoh A, Nishioka H, Aoki J, Nomoto A, Mizoguchi A, Takai Y. Nectin/ PRR: an immunoglobulin-like cell adhesion molecule recruited to cadherin-based adherens junctions through interaction with Afadin, a PDZ domain-containing protein. J Cell Biol 1999; 145:539-549.
    • (1999) J Cell Biol , vol.145 , pp. 539-549
    • Takahashi, K.1    Nakanishi, H.2    Miyahara, M.3    Mandai, K.4    Satoh, K.5    Satoh, A.6    Nishioka, H.7    Aoki, J.8    Nomoto, A.9    Mizoguchi, A.10    Takai, Y.11
  • 4
    • 0034616002 scopus 로고    scopus 로고
    • Nectin-3, a new member of immunoglobulin-like cell adhesion molecules that shows homophilic and heterophilic cell-cell adhesion activities
    • Satoh-Horikawa K, Nakanishi H, Takahashi K, Miyahara M, Nishimura M, Tachibana K, Mizoguchi A, Takai Y. Nectin-3, a new member of immunoglobulin-like cell adhesion molecules that shows homophilic and heterophilic cell-cell adhesion activities. J Biol Chem 2000; 275:10291-10299.
    • (2000) J Biol Chem , vol.275 , pp. 10291-10299
    • Satoh-Horikawa, K.1    Nakanishi, H.2    Takahashi, K.3    Miyahara, M.4    Nishimura, M.5    Tachibana, K.6    Mizoguchi, A.7    Takai, Y.8
  • 5
    • 0035900768 scopus 로고    scopus 로고
    • Nectin4/PRR4, a new afadin-associated member of the nectin family that trans-interacts with nectin1/PRR1 through V domain interaction
    • Reymond N, Fabre S, Lecocq E, Adelaide J, Dubreuil P, Lopez M. Nectin4/PRR4, a new afadin-associated member of the nectin family that trans-interacts with nectin1/PRR1 through V domain interaction. J Biol Chem 2001; 276:43205-43215.
    • (2001) J Biol Chem , vol.276 , pp. 43205-43215
    • Reymond, N.1    Fabre, S.2    Lecocq, E.3    Adelaide, J.4    Dubreuil, P.5    Lopez, M.6
  • 6
    • 0024519677 scopus 로고
    • Cellular receptor for poliovirus: Molecular cloning, nucleotide sequence, and expression of a new member of the immunoglobulin superfamily
    • Mendelsohn CL, Wimmer E, Racaniello VR. Cellular receptor for poliovirus: molecular cloning, nucleotide sequence, and expression of a new member of the immunoglobulin superfamily. Cell 1989; 56: 855-865.
    • (1989) Cell , vol.56 , pp. 855-865
    • Mendelsohn, C.L.1    Wimmer, E.2    Racaniello, V.R.3
  • 8
    • 0026560656 scopus 로고
    • Molecular cloning and expression of a murine homolog of the human poliovirus receptor gene
    • Morrison ME, Racaniello VR. Molecular cloning and expression of a murine homolog of the human poliovirus receptor gene. J Virol 1992; 66:2807-2813.
    • (1992) J Virol , vol.66 , pp. 2807-2813
    • Morrison, M.E.1    Racaniello, V.R.2
  • 9
    • 0029048729 scopus 로고
    • The human PRR2 gene, related to the human poliovirus receptor gene (PVR), is the true homolog of the murine MPH gene
    • Eberle F, Dubreuil P, Mattei MG, Devilard E, Lopez M. The human PRR2 gene, related to the human poliovirus receptor gene (PVR), is the true homolog of the murine MPH gene. Gene 1995; 159:267-272.
    • (1995) Gene , vol.159 , pp. 267-272
    • Eberle, F.1    Dubreuil, P.2    Mattei, M.G.3    Devilard, E.4    Lopez, M.5
  • 10
    • 0028925875 scopus 로고
    • Complementary DNA characterization and chromosomal localization of a human gene related to the poliovirus receptor-encoding gene
    • Lopez M, Eberle F, Mattei MG, Gabert J, Birg F, Bardin F, Maroc C, Dubreuil P. Complementary DNA characterization and chromosomal localization of a human gene related to the poliovirus receptor-encoding gene. Gene 1995; 155:261-265.
    • (1995) Gene , vol.155 , pp. 261-265
    • Lopez, M.1    Eberle, F.2    Mattei, M.G.3    Gabert, J.4    Birg, F.5    Bardin, F.6    Maroc, C.7    Dubreuil, P.8
  • 11
    • 0028232184 scopus 로고
    • A novel member of the immunoglobulin gene superfamily expressed in rat carcinoma cell lines
    • Chadeneau C, LeMoullac B, Denis MG. A novel member of the immunoglobulin gene superfamily expressed in rat carcinoma cell lines. J Biol Chem 1994; 269:15601-15605.
    • (1994) J Biol Chem , vol.269 , pp. 15601-15605
    • Chadeneau, C.1    LeMoullac, B.2    Denis, M.G.3
  • 12
    • 0031572294 scopus 로고    scopus 로고
    • Mouse homolog of poliovirus receptor-related gene 2 product, mPRR2, mediates homophilic cell aggregation
    • Aoki J, Koike S, Asou H, Ise I, Suwa H, Tanaka T, Miyasaka M, Nomoto A. Mouse homolog of poliovirus receptor-related gene 2 product, mPRR2, mediates homophilic cell aggregation. Exp Cell Res 1997; 235:374-384.
    • (1997) Exp Cell Res , vol.235 , pp. 374-384
    • Aoki, J.1    Koike, S.2    Asou, H.3    Ise, I.4    Suwa, H.5    Tanaka, T.6    Miyasaka, M.7    Nomoto, A.8
  • 13
    • 0032534991 scopus 로고    scopus 로고
    • The human poliovirus receptor related 2 protein is a new hematopoietic/endothelial homophilic adhesion molecule
    • Lopez M, Aoubala M, Jordier F, Isnardon D, Gomez S, Dubreuil P. The human poliovirus receptor related 2 protein is a new hematopoietic/endothelial homophilic adhesion molecule. Blood 1998; 92:4602-4611.
    • (1998) Blood , vol.92 , pp. 4602-4611
    • Lopez, M.1    Aoubala, M.2    Jordier, F.3    Isnardon, D.4    Gomez, S.5    Dubreuil, P.6
  • 15
    • 0017709496 scopus 로고
    • Observations on rat Sertoli ectoplasmic ('junctional') specializations in their association with germ cells of the rat testis
    • Russell L. Observations on rat Sertoli ectoplasmic ('junctional') specializations in their association with germ cells of the rat testis. Tissue Cell 1977; 9:475-498.
    • (1977) Tissue Cell , vol.9 , pp. 475-498
    • Russell, L.1
  • 16
    • 0024891608 scopus 로고
    • Distribution and function of organized concentrations of actin filaments in mammalian spermatogenic cells and Sertoli cells
    • Vogl AW. Distribution and function of organized concentrations of actin filaments in mammalian spermatogenic cells and Sertoli cells. Int Rev Cytol 1989; 119:1-56.
    • (1989) Int Rev Cytol , vol.119 , pp. 1-56
    • Vogl, A.W.1
  • 17
    • 0034115882 scopus 로고    scopus 로고
    • Unique and multifunctional adhesion junctions in the testis: Ectoplasmic specializations
    • Vogl AW, Pfeiffer DC, Mulholland D, Kimel G, Guttman J. Unique and multifunctional adhesion junctions in the testis: ectoplasmic specializations. Arch Histol Cytol 2000; 63:1-15.
    • (2000) Arch Histol Cytol , vol.63 , pp. 1-15
    • Vogl, A.W.1    Pfeiffer, D.C.2    Mulholland, D.3    Kimel, G.4    Guttman, J.5
  • 18
    • 0026398660 scopus 로고
    • Ectoplasmic ("junctional") specializations in mammalian Sertoli cells: Influence on spermatogenic cells
    • Vogl AW, Pfeiffer DC, Redenbach DM. Ectoplasmic ("junctional") specializations in mammalian Sertoli cells: influence on spermatogenic cells. Ann N Y Acad Sci 1991; 637:175-202.
    • (1991) Ann N Y Acad Sci , vol.637 , pp. 175-202
    • Vogl, A.W.1    Pfeiffer, D.C.2    Redenbach, D.M.3
  • 19
    • 0036788073 scopus 로고    scopus 로고
    • Cell junction dynamics in the testis: Sertoligerm cell interactions and male contraceptive development
    • Cheng CY, Mruk DD. Cell junction dynamics in the testis: Sertoligerm cell interactions and male contraceptive development. Physiol Rev 2002; 82:825-874.
    • (2002) Physiol Rev , vol.82 , pp. 825-874
    • Cheng, C.Y.1    Mruk, D.D.2
  • 21
    • 0032577975 scopus 로고    scopus 로고
    • Claudin-1 and -2: Novel integral membrane proteins localizing at tight junctions with no sequence similarity to occludin
    • Furuse M, Fujita K, Hiiragi T, Fujimoto K, Tsukita S. Claudin-1 and -2: novel integral membrane proteins localizing at tight junctions with no sequence similarity to occludin. J Cell Biol 1998; 141:1539-1550.
    • (1998) J Cell Biol , vol.141 , pp. 1539-1550
    • Furuse, M.1    Fujita, K.2    Hiiragi, T.3    Fujimoto, K.4    Tsukita, S.5
  • 22
    • 0031798631 scopus 로고    scopus 로고
    • Occludin is concentrated at tight junctions of mouse/rat but not human/guinea pig Sertoli cells in testes
    • Moroi S, Saitou M, Fujimoto K, Sakakibara A, Furuse M, Yoshida O, Tsukita S. Occludin is concentrated at tight junctions of mouse/rat but not human/guinea pig Sertoli cells in testes. Am J Physiol 1998; 274:C1708-C1717.
    • (1998) Am J Physiol , vol.274
    • Moroi, S.1    Saitou, M.2    Fujimoto, K.3    Sakakibara, A.4    Furuse, M.5    Yoshida, O.6    Tsukita, S.7
  • 23
    • 0033519348 scopus 로고    scopus 로고
    • Claudin-11/OSP-based tight junctions of myelin sheaths in brain and Sertoli cells in testis
    • Morita K, Sasaki H, Fujimoto K, Furuse M, Tsukita S. Claudin-11/ OSP-based tight junctions of myelin sheaths in brain and Sertoli cells in testis. J Cell Biol 1999; 145:579-588.
    • (1999) J Cell Biol , vol.145 , pp. 579-588
    • Morita, K.1    Sasaki, H.2    Fujimoto, K.3    Furuse, M.4    Tsukita, S.5
  • 26
    • 0027284704 scopus 로고
    • Immunohistochemical localization of adherens junction components in blood-brain barrier microvessels of the rat
    • Schulze C, Firth JA. Immunohistochemical localization of adherens junction components in blood-brain barrier microvessels of the rat. J Cell Sci 1993; 104:773-782.
    • (1993) J Cell Sci , vol.104 , pp. 773-782
    • Schulze, C.1    Firth, J.A.2
  • 27
    • 0022569860 scopus 로고
    • A functional assay for proteins involved in establishing an epithelial occluding barrier: Identification of a uvomorulin-like polypeptide
    • Gumbiner B, Simons K. A functional assay for proteins involved in establishing an epithelial occluding barrier: identification of a uvomorulin-like polypeptide. J Cell Biol 1986; 102:457-468.
    • (1986) J Cell Biol , vol.102 , pp. 457-468
    • Gumbiner, B.1    Simons, K.2
  • 28
    • 0033973460 scopus 로고    scopus 로고
    • Tight junctions of the blood-brain barrier
    • Kniesel U, Wolburg H. Tight junctions of the blood-brain barrier. Cell Mol Neurobiol 2000; 20:57-76.
    • (2000) Cell Mol Neurobiol , vol.20 , pp. 57-76
    • Kniesel, U.1    Wolburg, H.2
  • 32
    • 0029896454 scopus 로고    scopus 로고
    • Identification and characterization of espin, an actin-binding protein localized to the F-actin-rich junctional plaques of Sertoli cell ectoplasmic specializations
    • Bartles JR, Wierda A, Zheng L. Identification and characterization of espin, an actin-binding protein localized to the F-actin-rich junctional plaques of Sertoli cell ectoplasmic specializations. J Cell Sci 1996; 109:1229-1239.
    • (1996) J Cell Sci , vol.109 , pp. 1229-1239
    • Bartles, J.R.1    Wierda, A.2    Zheng, L.3
  • 33
    • 0032741307 scopus 로고    scopus 로고
    • Espin contains an additional actin-binding site in its N terminus and is a major actin-bundling protein of the Sertoli cell-spermatid ectoplasmic specialization junctional plaque
    • Chen B, Li A, Wang D, Wang M, Zheng L, Bartles JR. Espin contains an additional actin-binding site in its N terminus and is a major actin-bundling protein of the Sertoli cell-spermatid ectoplasmic specialization junctional plaque. Mol Biol Cell 1999; 10:4327-4339.
    • (1999) Mol Biol Cell , vol.10 , pp. 4327-4339
    • Chen, B.1    Li, A.2    Wang, D.3    Wang, M.4    Zheng, L.5    Bartles, J.R.6
  • 34
    • 0034029901 scopus 로고    scopus 로고
    • Defects in nuclear and cytoskeletal morphology and mitochondrial localization in spermatozoa of mice lacking nectin-2, a component of cell-cell adherens junctions
    • Bouchard MJ, Dong Y, McDermott BM Jr, Lam DH, Brown KR, Shelanski M, Bellve AR, Racaniello VR. Defects in nuclear and cytoskeletal morphology and mitochondrial localization in spermatozoa of mice lacking nectin-2, a component of cell-cell adherens junctions. Mol Cell Biol 2000; 20:2865-2873.
    • (2000) Mol Cell Biol , vol.20 , pp. 2865-2873
    • Bouchard, M.J.1    Dong, Y.2    McDermott B.M., Jr.3    Lam, D.H.4    Brown, K.R.5    Shelanski, M.6    Bellve, A.R.7    Racaniello, V.R.8
  • 35
    • 0025780879 scopus 로고
    • Neonatal lethality and lymphopenia in mice with a homozygous disruption of the c-abl proto-oncogene
    • Tybulewicz VL, Crawford CE, Jackson PK, Bronson RT, Mulligan RC. Neonatal lethality and lymphopenia in mice with a homozygous disruption of the c-abl proto-oncogene. Cell 1991; 65:1153-1163.
    • (1991) Cell , vol.65 , pp. 1153-1163
    • Tybulewicz, V.L.1    Crawford, C.E.2    Jackson, P.K.3    Bronson, R.T.4    Mulligan, R.C.5
  • 37
    • 0017140969 scopus 로고
    • The use of zona-free animal ova as a test-system for the assessment of the fertilizing capacity of human spermatozoa
    • Yanagimachi R, Yanagimachi H, Rogers BJ. The use of zona-free animal ova as a test-system for the assessment of the fertilizing capacity of human spermatozoa. Biol Reprod 1976; 15:471-476.
    • (1976) Biol Reprod , vol.15 , pp. 471-476
    • Yanagimachi, R.1    Yanagimachi, H.2    Rogers, B.J.3
  • 38
    • 0032956726 scopus 로고    scopus 로고
    • An investigation of the latency period between sperm oolemmal adhesion and oocyte penetration
    • Bronson RA, Bronson SK, Oula L, Fusi FM, Calzi F, Phillips DM. An investigation of the latency period between sperm oolemmal adhesion and oocyte penetration. Mol Reprod Dev 1999; 52:319-327.
    • (1999) Mol Reprod Dev , vol.52 , pp. 319-327
    • Bronson, R.A.1    Bronson, S.K.2    Oula, L.3    Fusi, F.M.4    Calzi, F.5    Phillips, D.M.6
  • 40
    • 0021924974 scopus 로고
    • Arrangement and possible function of actin filament bundles in ectoplasmic specializations of ground squirrel Sertoli cells
    • Vogl AW, Soucy LJ. Arrangement and possible function of actin filament bundles in ectoplasmic specializations of ground squirrel Sertoli cells. J Cell Biol 1985; 100:814-825.
    • (1985) J Cell Biol , vol.100 , pp. 814-825
    • Vogl, A.W.1    Soucy, L.J.2
  • 41
    • 0023714244 scopus 로고
    • Changes in the distribution of microtubules in rat Sertoli cells during spermatogenesis
    • Vogl AW. Changes in the distribution of microtubules in rat Sertoli cells during spermatogenesis. Anat Rec 1988; 222:34-41.
    • (1988) Anat Rec , vol.222 , pp. 34-41
    • Vogl, A.W.1
  • 42
    • 0033021426 scopus 로고    scopus 로고
    • Spermatid translocation in the rat seminiferous epithelium: Coupling membrane trafficking machinery to a junction plaque
    • Beach SF, Vogl AW. Spermatid translocation in the rat seminiferous epithelium: coupling membrane trafficking machinery to a junction plaque. Biol Reprod 1999; 60:1036-1046.
    • (1999) Biol Reprod , vol.60 , pp. 1036-1046
    • Beach, S.F.1    Vogl, A.W.2
  • 43
    • 0027082608 scopus 로고
    • Binding between mammalian spermatid-ectoplasmic specialization complexes and microtubules
    • Redenbach DM, Boekelheide K, Vogl AW. Binding between mammalian spermatid-ectoplasmic specialization complexes and microtubules. Eur J Cell Biol 1992; 59:433-448.
    • (1992) Eur J Cell Biol , vol.59 , pp. 433-448
    • Redenbach, D.M.1    Boekelheide, K.2    Vogl, A.W.3
  • 44
    • 0025753031 scopus 로고
    • Microtubule polarity in Sertoli cells: A model for microtubule-based spermatid transport
    • Redenbach DM, Vogl AW. Microtubule polarity in Sertoli cells: a model for microtubule-based spermatid transport. Eur J Cell Biol 1991; 54:277-290.
    • (1991) Eur J Cell Biol , vol.54 , pp. 277-290
    • Redenbach, D.M.1    Vogl, A.W.2
  • 45
    • 0033945047 scopus 로고    scopus 로고
    • Dynein and plus-end microtubule-dependent motors are associated with specialized Sertoli cell junction plaques (ectoplasmic specializations)
    • Guttman JA, Kimel GH, Vogl AW. Dynein and plus-end microtubule-dependent motors are associated with specialized Sertoli cell junction plaques (ectoplasmic specializations). J Cell Sci 2000; 113:2167-2176.
    • (2000) J Cell Sci , vol.113 , pp. 2167-2176
    • Guttman, J.A.1    Kimel, G.H.2    Vogl, A.W.3
  • 46
    • 0032981916 scopus 로고    scopus 로고
    • Rat testis motor proteins associated with spermatid translocation (dynein) and spermatid flagella (kinesin-II)
    • Miller MG, Mulholland DJ, Vogl AW. Rat testis motor proteins associated with spermatid translocation (dynein) and spermatid flagella (kinesin-II). Biol Reprod 1999; 60:1047-1056.
    • (1999) Biol Reprod , vol.60 , pp. 1047-1056
    • Miller, M.G.1    Mulholland, D.J.2    Vogl, A.W.3
  • 47
    • 0037040905 scopus 로고    scopus 로고
    • Interaction of the poliovirus receptor CD155 with the dynein light chain Tctex-1 and its implication for poliovirus pathogenesis
    • Mueller S, Cao X, Welker R, Wimmer E. Interaction of the poliovirus receptor CD155 with the dynein light chain Tctex-1 and its implication for poliovirus pathogenesis. J Biol Chem 2002; 277:7897-7904.
    • (2002) J Biol Chem , vol.277 , pp. 7897-7904
    • Mueller, S.1    Cao, X.2    Welker, R.3    Wimmer, E.4
  • 48
    • 0024418238 scopus 로고
    • Tctex-1: A candidate gene family for a mouse t complex sterility locus
    • Lader E, Ha HS, O'Neill M, Artzt K, Bennett D. Tctex-1: a candidate gene family for a mouse t complex sterility locus. Cell 1989; 58:969-979.
    • (1989) Cell , vol.58 , pp. 969-979
    • Lader, E.1    Ha, H.S.2    O'Neill, M.3    Artzt, K.4    Bennett, D.5
  • 49
    • 0033304710 scopus 로고    scopus 로고
    • Cellular immunolocalization of occludin during embryonic and postnatal development of the mouse testis and epididymis
    • Cyr DG, Hermo L, Egenberger N, Mertineit C, Trasler JM, Laird DW. Cellular immunolocalization of occludin during embryonic and postnatal development of the mouse testis and epididymis. Endocrinology 1999; 140:3815-3825.
    • (1999) Endocrinology , vol.140 , pp. 3815-3825
    • Cyr, D.G.1    Hermo, L.2    Egenberger, N.3    Mertineit, C.4    Trasler, J.M.5    Laird, D.W.6
  • 51
    • 0028922059 scopus 로고
    • Structure and turnover of junctional complexes between principal cells of the rat epididymis
    • Cyr DG, Robaire B, Hermo L. Structure and turnover of junctional complexes between principal cells of the rat epididymis. Microsc Res Tech 1995; 30:54-66.
    • (1995) Microsc Res Tech , vol.30 , pp. 54-66
    • Cyr, D.G.1    Robaire, B.2    Hermo, L.3
  • 52
    • 0036744723 scopus 로고    scopus 로고
    • Animal models of genetic causes of male infertility
    • Christensen GL, Carrell DT. Animal models of genetic causes of male infertility. Asian J Androl 2002; 4:213-219.
    • (2002) Asian J Androl , vol.4 , pp. 213-219
    • Christensen, G.L.1    Carrell, D.T.2
  • 54
    • 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, Ward DC, Huszar G. FISH assessment of aneuploidy frequencies in mature and immature human spermatozoa classified by the absence or presence of cytoplasmic retention. Hum Reprod 2001; 16:1209-1217.
    • (2001) Hum Reprod , vol.16 , pp. 1209-1217
    • Kovanci, E.1    Kovacs, T.2    Moretti, E.3    Vigue, L.4    Bray-Ward, P.5    Ward, D.C.6    Huszar, G.7
  • 55
    • 0042733027 scopus 로고    scopus 로고
    • 3 integrin containing membrane microdomains
    • May 10.1074/jbc.M304166200
    • 3 integrin containing membrane microdomains. J Biol Chem. May 2003; 10.1074/ jbc.M304166200.
    • (2003) J Biol Chem
    • Mueller, S.1    Wimmer, E.2


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