메뉴 건너뛰기




Volumn 78, Issue 1, 2003, Pages 1-16

Ectoplasmic specializations in the Sertoli cell: New vistas based on genetic defects and testicular toxicology

Author keywords

Blood testis barrier; Ectoplasmic specialization; Sertoli cell; Spermatogenesis; Testis

Indexed keywords

ACTIN; ACTIN BINDING PROTEIN; DIETHYLSTILBESTROL; ESTROGEN; MEMBRANE PROTEIN; CYTOSKELETON PROTEIN;

EID: 0038519815     PISSN: 14476959     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.0022-7722.2003.00034.x     Document Type: Review
Times cited : (79)

References (132)
  • 2
    • 0027414695 scopus 로고
    • Two classes of tight junctions are revealed by ZO-1 isoforms
    • Balda MS, Anderson JM (1993) Two classes of tight junctions are revealed by ZO-1 isoforms. Am J Physiol 33, C918-C24.
    • (1993) Am. J. Physiol. , vol.33
    • Balda, M.S.1    Anderson, J.M.2
  • 3
    • 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 (1996) 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 109, 1229-39.
    • (1996) J. Cell Sci. , vol.109 , pp. 1229-1239
    • Bartles, J.R.1    Wierda, A.2    Zheng, L.3
  • 4
    • 0033021426 scopus 로고    scopus 로고
    • Spermatid translocation in the rat seminiferous epithelium: Coupling membrane trafficking machinery to a junction plaque
    • Beach SF, Vogl AW (1999) Spermatid translocation in the rat seminiferous epithelium: Coupling membrane trafficking machinery to a junction plaque. Biol Reprod 60, 1036-46.
    • (1999) Biol. Reprod. , vol.60 , pp. 1036-1046
    • Beach, S.F.1    Vogl, A.W.2
  • 5
    • 0021038598 scopus 로고
    • Postnatal formation of the blood-testis barrier in the rat with special reference to the initiation of meiosis
    • Bergmann M, Dierichs R (1983) Postnatal formation of the blood-testis barrier in the rat with special reference to the initiation of meiosis. Anat Embryol 168, 269-75.
    • (1983) Anat. Embryol. , vol.168 , pp. 269-275
    • Bergmann, M.1    Dierichs, R.2
  • 6
    • 0029787210 scopus 로고    scopus 로고
    • Further observations on the early events that contribute to establishing the morphological pattern shown by the oestradiol suppressed testis
    • Blanco-Rodríguez J, Martínez-García C (1996a) Further observations on the early events that contribute to establishing the morphological pattern shown by the oestradiol suppressed testis. Tiss Cell 28, 387-99.
    • (1996) Tiss. Cell , vol.28 , pp. 387-399
    • Blanco-Rodríguez, J.1    Martínez-García, C.2
  • 7
    • 0029909066 scopus 로고    scopus 로고
    • Induction of apoptotic cell death in the seminiferous tubule of the adult rat testis: Assessment of the germ cell types that exhibit the ability to enter apoptosis after hormone suppression by oestradiol treatment
    • Blanco-Rodríguez J, Martínez-García C (1996b) Induction of apoptotic cell death in the seminiferous tubule of the adult rat testis: assessment of the germ cell types that exhibit the ability to enter apoptosis after hormone suppression by oestradiol treatment. Int J Androl 19, 237-47.
    • (1996) Int. J. Androl. , vol.19 , pp. 237-247
    • Blanco-Rodríguez, J.1    Martínez-García, C.2
  • 8
    • 0343980401 scopus 로고
    • Fimbrin is a cytoskeletal protein that crosslinks F-actin in vitro
    • Bretscher A (1981) Fimbrin is a cytoskeletal protein that crosslinks F-actin in vitro. Proc Natl Acad Sci USA 78, 6849-53.
    • (1981) Proc. Natl. Acad. Sci. USA , vol.78 , pp. 6849-6853
    • Bretscher, A.1
  • 9
    • 0019313223 scopus 로고
    • Finbrin, a new microfilament-associated protein present in microvilli and other cell surface structures
    • Bretscher A, Weber K (1980) Finbrin, a new microfilament-associated protein present in microvilli and other cell surface structures. J Cell Bial 86, 335-40.
    • (1980) J. Cell Biol. , vol.86 , pp. 335-340
    • Bretscher, A.1    Weber, K.2
  • 10
    • 0003415734 scopus 로고
    • Fine structure of germ cells and sertoli cells during the cycle of the seminiferous epithelium in the rat
    • Brökelmann J (1963) Fine structure of germ cells and Sertoli cells during the cycle of the seminiferous epithelium in the rat. Zeitscrift Zellforsch 59, 820-50.
    • (1963) Zeitscrift Zellforsch , vol.59 , pp. 820-850
    • Brökelmann, J.1
  • 11
    • 0029833675 scopus 로고    scopus 로고
    • Isolation and characterization of a novel oligodendrocyte-specific protein
    • Bronstein JM, Popper P, Micevych PE, Farber DB (1996) Isolation and characterization of a novel oligodendrocyte-specific protein. Neurology 47, 772-8.
    • (1996) Neurology , vol.47 , pp. 772-778
    • Bronstein, J.M.1    Popper, P.2    Micevych, P.E.3    Farber, D.B.4
  • 12
    • 0001571538 scopus 로고
    • Studies on the fine structure of the mammalian testis. I. Differentiation of the spermatid in the cat (Felis domestica)
    • Burgos MH, Fawcett DW (1955) Studies on the fine structure of the mammalian testis. 1. Differentiation of the spermatid in the cat (Felis domestica). J Biophys Biochem Cytol 1, 287-300.
    • (1955) J. Biophys. Biochem. Cytol. , vol.1 , pp. 287-300
    • Burgos, M.H.1    Fawcett, D.W.2
  • 13
    • 0025874963 scopus 로고
    • Development of sertoli cell junctional specializations and the distribution of the tight-junction-associated protein ZO-1 in the mouse testis
    • Byers S, Graham R, Dai HN, Hoxter B (1991) Development of Sertoli cell junctional specializations and the distribution of the tight-junction-associated protein ZO-1 in the mouse testis. Am J Anat 191, 35-47.
    • (1991) Am. J. Anat. , vol.191 , pp. 35-47
    • Byers, S.1    Graham, R.2    Dai, H.N.3    Hoxter, B.4
  • 14
    • 0002659233 scopus 로고
    • Sertoli cell tight junctions and the blood-testis barrier
    • (Cereijido M, ed.). CRC Press, Boca Raton
    • Byers SW, Pelletier R-M (1992) Sertoli cell tight junctions and the blood-testis barrier. In: Tight Junctions (Cereijido M, ed.). CRC Press, Boca Raton, 279-304.
    • (1992) Tight Junctions , pp. 279-304
    • Byers, S.W.1    Pelletier, R.-M.2
  • 16
  • 18
    • 0023656168 scopus 로고
    • Identification of two testosterone-responsive testicular proteins in Sertoli cell-enriched culture medium whose secretion is suppressed by cells of the intact seminiferous tubule
    • Cheng CY, Bardin CW (1987) Identification of two testosterone-responsive testicular proteins in Sertoli cell-enriched culture medium whose secretion is suppressed by cells of the intact seminiferous tubule. J Biol Chem 262, 12 768-79.
    • (1987) J. Biol. Chem. , vol.262 , Issue.12 , pp. 768-779
    • Cheng, C.Y.1    Bardin, C.W.2
  • 19
    • 0024842846 scopus 로고
    • Testins are structurally related sertoli cell proteins whose secretion is tightly coupled to the presence of germ cells
    • Cheng CY, Grima J, Stahler MS, Lockshin RA, Bardin CW (1989) Testins are structurally related Sertoli cell proteins whose secretion is tightly coupled to the presence of germ cells. J Biol Chem 264, 21 386-93.
    • (1989) J. Biol. Chem. , vol.264 , Issue.21 , pp. 386-393
    • Cheng, C.Y.1    Grima, J.2    Stahler, M.S.3    Lockshin, R.A.4    Bardin, C.W.5
  • 20
    • 0034755902 scopus 로고    scopus 로고
    • A 22-amino acid synthetic peptide corresponding to the second extracellular loop of rat occludin perturbs the blood-testis barrier and disrupts spermatogenesis reversibly in vivo
    • Chung NPY, Mruk D, Mo M-Y, Lee WM, Cheng CY (2001) A 22-amino acid synthetic peptide corresponding to the second extracellular loop of rat occludin perturbs the blood-testis barrier and disrupts spermatogenesis reversibly in vivo. Biol Reprod 65, 1340-51.
    • (2001) Biol. Reprod. , vol.65 , pp. 1340-1351
    • Chung, N.P.Y.1    Mruk, D.2    Mo, M.-Y.3    Lee, W.M.4    Cheng, C.Y.5
  • 21
    • 0027207967 scopus 로고
    • The molecular organization of tight junctions
    • Citi S (1993) The molecular organization of tight junctions. J Cell Biol 121, 485-9.
    • (1993) J. Cell Biol. , vol.121 , pp. 485-489
    • Citi, S.1
  • 23
    • 0018370844 scopus 로고
    • Regulation of microfilaments and microtubules by calcium and cyclic AMP
    • Dedman JR, Brinkley B, Means AR (1979) Regulation of microfilaments and microtubules by calcium and cyclic AMP. Adv Cyclic Nucl Res 11, 131-74.
    • (1979) Adv. Cyclic. Nucl. Res. , vol.11 , pp. 131-174
    • Dedman, J.R.1    Brinkley, B.2    Means, A.R.3
  • 24
    • 0015608073 scopus 로고
    • The fine structure of the monkey (Macaca) sertoli cell and its role in maintaining the blood-testis barrier
    • Dym M (1970) The fine structure of the monkey (Macaca) Sertoli cell and its role in maintaining the blood-testis barrier. Anat Rec 175, 639-56.
    • (1970) Anat. Rec. , vol.175 , pp. 639-656
    • Dym, M.1
  • 25
    • 0014892078 scopus 로고
    • The blood-testis barrier in the rat and the physiological compartmentation of the seminiferous epithelium
    • Dym M, Fawcett DW (1970) The blood-testis barrier in the rat and the physiological compartmentation of the seminiferous epithelium. Biol Reprod 3, 308-26.
    • (1970) Biol. Reprod. , vol.3 , pp. 308-326
    • Dym, M.1    Fawcett, D.W.2
  • 26
    • 0028136264 scopus 로고
    • Long-term alterations in permeability of the blood-testis barrier following a single intratesticular injection of dilute aqueous glycerol
    • Eng F, Wiebe JP, Alima LH (1994) Long-term alterations in permeability of the blood-testis barrier following a single intratesticular injection of dilute aqueous glycerol. J Androl 15,311-7.
    • (1994) J. Androl. , vol.15 , pp. 311-317
    • Eng, F.1    Wiebe, J.P.2    Alima, L.H.3
  • 27
    • 0032491391 scopus 로고    scopus 로고
    • The tight junction protein ZO-1 establishes a link between the transmembrane protein occludin and the actin cytoskeleton
    • Fanning AS, Jameson BJ, Jesaitis LA, Anderson JM (1998) The tight junction protein ZO-1 establishes a link between the transmembrane protein occludin and the actin cytoskeleton. J Biol Chem 273, 29745-53.
    • (1998) J. Biol. Chem. , vol.273 , pp. 29745-29753
    • Fanning, A.S.1    Jameson, B.J.2    Jesaitis, L.A.3    Anderson, J.M.4
  • 28
    • 0015701673 scopus 로고
    • Observations on the organization of the interstitial tissue of the testis and on the occluding cell junctions in the seminiferous epithelium
    • (Raspe G, Bernhard S, eds). Pergamon Press, Oxford
    • Fawcett DW (1973) Observations on the organization of the interstitial tissue of the testis and on the occluding cell junctions in the seminiferous epithelium. In: Advances in Biosciences 10, the Masculine Gender (Raspe G, Bernhard S, eds). Pergamon Press, Oxford, 83-99.
    • (1973) Advances in Biosciences 10, The Masculine Gender , pp. 83-99
    • Fawcett, D.W.1
  • 29
    • 0002236654 scopus 로고
    • Ultrastructure and function of the sertoli cell
    • (Hamilton DW, Greep RO, eds). American Physiololgy Society, Washington DC
    • Fawcett DW (1975) Ultrastructure and function of the Sertoli cell. In: Handbook of Physiology, Endocrinol, Vol. 5 (Hamilton DW, Greep RO, eds). American Physiololgy Society, Washington DC, 21-55.
    • (1975) Handbook of Physiology, Endocrinol. , vol.5 , pp. 21-55
    • Fawcett, D.W.1
  • 30
    • 0015135086 scopus 로고
    • Morphogenetic factors influencing the shape of the sperm head
    • Fawcett DW, Anderson WA, Phillips DM (1971) Morphogenetic factors influencing the shape of the sperm head. Dev Biol 26, 220-51.
    • (1971) Dev. Biol. , vol.26 , pp. 220-251
    • Fawcett, D.W.1    Anderson, W.A.2    Phillips, D.M.3
  • 31
    • 0014884660 scopus 로고
    • Electron microscopic observations on the structural components of the blood-testis barrier
    • Fawcett DW, Leak LV, Heidger PM (1970) Electron microscopic observations on the structural components of the blood-testis barrier. J Reprod Fertil 1O(Suppl.), 105-22.
    • (1970) J. Reprod. Fertil. , vol.10 , Issue.SUPPL. , pp. 105-122
    • Fawcett, D.W.1    Leak, L.V.2    Heidger, P.M.3
  • 32
    • 0014166202 scopus 로고
    • The postnatal development of the sertoli cells of the mouse
    • Flickinger CJ (1967) The postnatal development of the Sertoli cells of the mouse. Zeitscrift Zellforsch 78, 92-113.
    • (1967) Zeitscrift. Zellforsch. , vol.78 , pp. 92-113
    • Flickinger, C.J.1
  • 33
    • 0014093435 scopus 로고
    • The junctional specializations of sertoli cells in the seminiferous epithelium
    • Flickinger C, Fawcett DW (1967) The junctional specializations of Sertoli cells in the seminiferous epithelium. Anat Rec 158, 207-22.
    • (1967) Anat. Rec. , vol.158 , pp. 207-222
    • Flickinger, C.1    Fawcett, D.W.2
  • 34
    • 0021894188 scopus 로고
    • 2+ chelator and a calmodulin blocker interfere with the structure of inter-Sertoli junctions
    • 2+ chelator and a calmodulin blocker interfere with the structure of inter-Sertoli junctions. Tissue Cell 17, 13-25.
    • (1985) Tissue Cell , vol.17 , pp. 13-25
    • Franchi, E.1    Camatini, M.2
  • 35
    • 0017797246 scopus 로고
    • Location of actin in the microfilament bundles associated with the junctional specialization between sertoli cells and spermatids
    • Franke WW, Grund C, Fink A et al. (1978) Location of actin in the microfilament bundles associated with the junctional specialization between Sertoli cells and spermatids. Biol Cell 31, 7-14.
    • (1978) Biol. Cell , vol.31 , pp. 7-14
    • Franke, W.W.1    Grund, C.2    Fink, A.3
  • 36
    • 0020533647 scopus 로고
    • Evidence for a defective seminiferous tubule barrier in testes of Tfm and Sxr mice
    • Fritz IB, Lyon MF, Setchell BP (1983) Evidence for a defective seminiferous tubule barrier in testes of Tfm and Sxr mice. J Reprod Fertil 67, 359-63.
    • (1983) J. Reprod. Fertil. , vol.67 , pp. 359-363
    • Fritz, I.B.1    Lyon, M.F.2    Setchell, B.P.3
  • 37
    • 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 Sh (1998a) Claudin-1 and -2: Novel integral membrane proteins localizing at tight junctions with no sequence similarity to occludin. J Cell Biol 141, 1539-50.
    • (1998) J. Cell Biol. , vol.141 , pp. 1539-1550
    • Furuse, M.1    Fujita, K.2    Hiiragi, T.3    Fujimoto, K.4    Tsukita, Sh.5
  • 38
    • 0027744129 scopus 로고
    • Occludin: A novel integral membrane protein localizing at tight junctions
    • Furuse M, Hirase T, Itoh M et al. (1993) Occludin: A novel integral membrane protein localizing at tight junctions. J Cell Biol 123, 1777-88.
    • (1993) J. Cell Biol. , vol.123 , pp. 1777-1788
    • Furuse, M.1    Hirase, T.2    Itoh, M.3
  • 39
    • 0028110309 scopus 로고
    • Direct association of occludin with ZO-1 and its possible involvement in the localization of occludin at tight junctions
    • Furuse M, Itoh M, Hirase T et al. (1994) Direct association of occludin with Z0-1 and its possible involvement in the localization of occludin at tight junctions. J Cell Biol 127, 1617-26.
    • (1994) J. Cell Biol. , vol.127 , pp. 1617-1626
    • Furuse, M.1    Itoh, M.2    Hirase, T.3
  • 40
    • 0032547833 scopus 로고    scopus 로고
    • A single gene product, claudin-1 or -2, reconstitutes tight junction strands and recruits occludin in fibroblasts
    • Furuse M, Sakaki H, Fujimoto K, Tsukita Sh (1998b) A single gene product, claudin-1 or -2, reconstitutes tight junction strands and recruits occludin in fibroblasts. J Cell Biol 143, 391-401.
    • (1998) J. Cell Biol. , vol.143 , pp. 391-401
    • Furuse, M.1    Sakaki, H.2    Fujimoto, K.3    Tsukita, Sh.4
  • 41
    • 0018692430 scopus 로고
    • A 130 K protein from chicken gizzard: Its localization at the termini of microfilament bundles in cultured chicken cells
    • Geiger B (1979) A 130 K protein from chicken gizzard: Its localization at the termini of microfilament bundles in cultured chicken cells. Cell 18, 193-205.
    • (1979) Cell , vol.18 , pp. 193-205
    • Geiger, B.1
  • 42
    • 0019820867 scopus 로고
    • Immunoelectron microscope studies of membrane-microfilament interactions: Distributions of α-actinin, tropomyosin, and vinculin in intestinal epithelial brush border and chicken gizzard smooth muscle cells
    • Geiger B, Dutton AH, Tokuyasu KT, Singer SJ (1981) Immunoelectron microscope studies of membrane-microfilament interactions: Distributions of α-actinin, tropomyosin, and vinculin in intestinal epithelial brush border and chicken gizzard smooth muscle cells. J Cell Biol 91, 614-28.
    • (1981) J. Cell Biol. , vol.91 , pp. 614-628
    • Geiger, B.1    Dutton, A.H.2    Tokuyasu, K.T.3    Singer, S.J.4
  • 43
    • 0013523644 scopus 로고
    • Vinculin, an intracellular protein localized at specialized sites where microfilament bundles terminate at cell membranes
    • Geiger B, Tokuyasu KT, Dutton AH, Singer SJ (1980) Vinculin, an intracellular protein localized at specialized sites where microfilament bundles terminate at cell membranes. Proc Natl Acad Sci USA 77, 4127-31.
    • (1980) Proc. Natl. Acad. Sci. USA , vol.77 , pp. 4127-4131
    • Geiger, B.1    Tokuyasu, K.T.2    Dutton, A.H.3    Singer, S.J.4
  • 44
    • 0017264054 scopus 로고
    • The Sertoli cell occluding junctions and gap junctions in mature and developing mammalian testis
    • Gilula NB, Fawcett DW, Aoki A (1976) The Sertoli cell occluding junctions and gap junctions in mature and developing mammalian testis. Dev Biol 50, 142-68.
    • (1976) Dev. Biol. , vol.50 , pp. 142-168
    • Gilula, N.B.1    Fawcett, D.W.2    Aoki, A.3
  • 45
    • 0019780969 scopus 로고
    • F-actin binding and bundling properties of fimbrin, a major cytoskeletal protein of microvillus core filaments
    • Glenney JR, JrKaulfus P, Matsudaira P, Weber K (1981) F-actin binding and bundling properties of fimbrin, a major cytoskeletal protein of microvillus core filaments. J Biol Chem 256, 9283-8.
    • (1981) J. Biol. Chem. , vol.256 , pp. 9283-9288
    • Glenney J.R., Jr.1    Kaulfus, P.2    Matsudaira, P.3    Weber, K.4
  • 46
    • 0001636804 scopus 로고    scopus 로고
    • CNS myelin and Sertoli cell tight junction strands are absent in Osp/Claudin-11 null mice
    • Gow A, Southwood CM, Li JS et al. (1999) CNS myelin and Sertoli cell tight junction strands are absent in Osp/Claudin-11 null mice. Cell 99, 649-59.
    • (1999) Cell , vol.99 , pp. 649-659
    • Gow, A.1    Southwood, C.M.2    Li, J.S.3
  • 47
    • 0017048494 scopus 로고
    • Light and electron microscopic localization of ATPase in normal and degenerating testes of Syrian hamsters
    • Gravis CJ, Yates RD, Chen I-L (1976) Light and electron microscopic localization of ATPase in normal and degenerating testes of Syrian hamsters. Am J Anat 147, 419-32.
    • (1976) Am. J. Anat. , vol.147 , pp. 419-432
    • Gravis, C.J.1    Yates, R.D.2    Chen, I.-L.3
  • 48
    • 0032516869 scopus 로고    scopus 로고
    • Testin secreted by Sertoli cells is associated with the cell surface, and its expression correlates with the disruption of sertoli-germ cell junctions but not the inter-Sertoli tight junction
    • Grima J, Wong CCS, Zhu L-J, Zong S-D, Cheng CY (1998) Testin secreted by Sertoli cells is associated with the cell surface, and its expression correlates with the disruption of Sertoli-germ cell junctions but not the inter-Sertoli tight junction. J Biol Chem 273, 21040-53.
    • (1998) J. Biol. Chem. , vol.273 , pp. 21040-21053
    • Grima, J.1    Wong, C.C.S.2    Zhu, L.-J.3    Zong, S.-D.4    Cheng, C.Y.5
  • 49
    • 0025234672 scopus 로고
    • Immunofluorescence localization of vinculin in ectoplasmic ('junctional') specializations of rat Sertoli cells
    • Grove BD, Pfeiffer DC, Allen S, Vogl AW (1990) Immunofluorescence localization of vinculin in ectoplasmic ('junctional') specializations of rat Sertoli cells. Am J Anat 188, 44-56.
    • (1990) Am. J. Anat. , vol.188 , pp. 44-56
    • Grove, B.D.1    Pfeiffer, D.C.2    Allen, S.3    Vogl, A.W.4
  • 50
    • 0024325594 scopus 로고
    • Sertoli cell ectoplasmic specializations: A type of actin-associated adhesion junction
    • Grove BD, Vogl AW (1989) Sertoli cell ectoplasmic specializations: a type of actin-associated adhesion junction? J Cell Sci 93, 309-23.
    • (1989) J. Cell Sci. , vol.93 , pp. 309-323
    • Grove, B.D.1    Vogl, A.W.2
  • 51
    • 0026345292 scopus 로고
    • Identification of a 160 kDa polypeptide that binds to the tight junction protein ZO-1
    • Gumbiner B, Lowenkopf T, Apatira D (1991) Identification of a 160 kDa polypeptide that binds to the tight junction protein Z0-1. Proc Natl Acad Sci USA 88, 3460-4.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 3460-3464
    • Gumbiner, B.1    Lowenkopf, T.2    Apatira, D.3
  • 52
    • 0032489875 scopus 로고    scopus 로고
    • ZO-3, a novel member of the MAGUK protein family found at the tight junction, interacts with ZO-1 and occludin
    • Haskins J, Gu L, Wittchen ES, Hibbard J, Stevenson BR (1998) ZO-3, a novel member of the MAGUK protein family found at the tight junction, interacts with ZO-1 and occludin. J Cell Biol 141, 199-208.
    • (1998) J. Cell Biol. , vol.141 , pp. 199-208
    • Haskins, J.1    Gu, L.2    Wittchen, E.S.3    Hibbard, J.4    Stevenson, B.R.5
  • 54
    • 0036040748 scopus 로고    scopus 로고
    • Development of the blood-testis barrier in the mouse is delayed by neonatally administered diethylstilbestrol but not by β-estradiol 3-benzoate
    • Hosoi I, Toyama Y, Maekawa M, Yuasa S. (2002) Development of the blood-testis barrier in the mouse is delayed by neonatally administered diethylstilbestrol but not by β-estradiol 3-benzoate. Andrologia 34: 255-62.
    • (2002) Andrologia , vol.34 , pp. 255-262
    • Hosoi, I.1    Toyama, Y.2    Maekawa, M.3    Yuasa, S.4
  • 55
    • 0032520149 scopus 로고    scopus 로고
    • A null mutation in basigin, an immunoglobulin superfamily member, indicates its important roles in peri-implantation development and spermatogenesis
    • Igakura T, Kadomatsu K, Kaname T et al. (1998) A null mutation in basigin, an immunoglobulin superfamily member, indicates its important roles in peri-implantation development and spermatogenesis. Dev Biol 194, 152-65.
    • (1998) Dev. Biol. , vol.194 , pp. 152-165
    • Igakura, T.1    Kadomatsu, K.2    Kaname, T.3
  • 56
    • 0028364498 scopus 로고
    • Suppression of spermatogenesis by low-level glycerol treatment
    • Igdoura SA, Wiebe JP (1994) Suppression of spermatogenesis by low-level glycerol treatment. J Androl 14, 234-43.
    • (1994) J. Androl. , vol.14 , pp. 234-243
    • Igdoura, S.A.1    Wiebe, J.P.2
  • 57
    • 0026905579 scopus 로고
    • An aspermia rat mutant (as/as) with spermatogenic failure at meiosis
    • Ikadai H, Noguchi J, Yoshida M, Imamichi T (1992) An aspermia rat mutant (as/as) with spermatogenic failure at meiosis. J Vet Med Sci 54, 745-9.
    • (1992) J. Vet. Med. Sci. , vol.54 , pp. 745-749
    • Ikadai, H.1    Noguchi, J.2    Yoshida, M.3    Imamichi, T.4
  • 58
    • 0014608608 scopus 로고
    • Formation of arrowhead complexes with heavy meromyosin in a variety of cell types
    • Ishikawa H, Bishoff R, Holtzer H (1969) Formation of arrowhead complexes with heavy meromyosin in a variety of cell types. J Cell Biol 43, 312-28.
    • (1969) J. Cell Biol. , vol.43 , pp. 312-328
    • Ishikawa, H.1    Bishoff, R.2    Holtzer, H.3
  • 59
    • 0027300689 scopus 로고
    • The 220 kD protein colocalizing with cadherins in non-epithelial cells is identical to ZO-1, a tight junction-associated protein in epithelial cells: cDNA cloning and immunoelectron microscopy
    • Itoh M, Nagafuchi A, Yonemura S, Kitani-Yasuda T, Tsukita Sa, Tsukita Sh (1993) The 220 kD protein colocalizing with cadherins in non-epithelial cells is identical to ZO-1, a tight junction-associated protein in epithelial cells: cDNA cloning and immunoelectron microscopy. J Cell Biol 121, 491-502.
    • (1993) J. Cell Biol. , vol.121 , pp. 491-502
    • Itoh, M.1    Nagafuchi, A.2    Yonemura, S.3    Kitani-Yasuda, T.4    Tsukita, Sa.5    Tsukita, Sh.6
  • 60
    • 0025888954 scopus 로고
    • A 220-kD undercoat-constitutive protein: Its specific localization at cadherin-based cell-cell adhesion sites
    • Itoh M, Yonemura S, Nagafuchi A, Tsukita Sa, Tsukita Sh (1991) A 220-kD undercoat-constitutive protein: Its specific localization at cadherin-based cell-cell adhesion sites. J Cell Biol 115, 1449-62.
    • (1991) J. Cell Biol. , vol.115 , pp. 1449-1462
    • Itoh, M.1    Yonemura, S.2    Nagafuchi, A.3    Tsukita, Sa.4    Tsukita, Sh.5
  • 61
    • 0014609437 scopus 로고
    • Exogeneous cytochrome c as an ultrastructural tracer
    • Karnovsky MJ, Rice DF (1969) Exogeneous cytochrome c as an ultrastructural tracer. J Histochem Cytochem 17, 751-3.
    • (1969) J. Histochem. Cytochem. , vol.17 , pp. 751-753
    • Karnovsky, M.J.1    Rice, D.F.2
  • 63
    • 0017873769 scopus 로고
    • Biochemistry of actomyosin-dependent cell motility
    • Korn ED (1978) Biochemistry of actomyosin-dependent cell motility. Proc Natl Acad Sci USA 75, 588-99.
    • (1978) Proc. Natl. Acad. Sci. USA , vol.75 , pp. 588-599
    • Korn, E.D.1
  • 64
    • 0028008657 scopus 로고
    • Comparison of actin-filament bundles in myoid cells and Sertoli cells of the rat, golden hamster and mouse
    • Maekawa M, Nagano T, Murakami T (1994) Comparison of actin-filament bundles in myoid cells and Sertoli cells of the rat, golden hamster and mouse. Cell Tissue Res 275, 395-8.
    • (1994) Cell Tissue Res. , vol.275 , pp. 395-398
    • Maekawa, M.1    Nagano, T.2    Murakami, T.3
  • 65
    • 0036136374 scopus 로고    scopus 로고
    • Fyn tyrosine kinase in sertoli cells is involved in mouse spermatogenesis
    • Maekawa M, Toyama Y, Yasuda M, Yagi T, Yuasa S (2002) Fyn tyrosine kinase in Sertoli cells is involved in mouse spermatogenesis. Biol Reprod 66, 211-21.
    • (2002) Biol. Reprod. , vol.66 , pp. 211-221
    • Maekawa, M.1    Toyama, Y.2    Yasuda, M.3    Yagi, T.4    Yuasa, S.5
  • 66
    • 0019275289 scopus 로고
    • Experimental modulation of occluding junctions in guinea pig pancreatic acinar cells. Effect of drugs
    • Martinez-Palomo A, Meza I, Beaty G, Cereijido M (1980) Experimental modulation of occluding junctions in guinea pig pancreatic acinar cells. Effect of drugs. J Cell Biol 87, 736-45.
    • (1980) J. Cell Biol. , vol.87 , pp. 736-745
    • Martinez-Palomo, A.1    Meza, I.2    Beaty, G.3    Cereijido, M.4
  • 67
    • 0020655456 scopus 로고
    • Role of fimbrin and villin in determining the interfilament distances of actin bundle
    • Matsudaira P, Mandelkow E, Renner W, Hesterberg LK, Weber K (1983) Role of fimbrin and villin in determining the interfilament distances of actin bundle. Nature 301, 209-14.
    • (1983) Nature , vol.301 , pp. 209-214
    • Matsudaira, P.1    Mandelkow, E.2    Renner, W.3    Hesterberg, L.K.4    Weber, K.5
  • 68
    • 0031727426 scopus 로고    scopus 로고
    • Occludin and the functions of tight junctions
    • Matter K, Balda MS (1999) Occludin and the functions of tight junctions. Int Rev Cytol 186, 117-46.
    • (1999) Int. Rev. Cytol. , vol.186 , pp. 117-146
    • Matter, K.1    Balda, M.S.2
  • 69
    • 0033851771 scopus 로고    scopus 로고
    • Molecular physiology and pathophysiology of tight junctions. I. Tight junction structure and function: Lessons from mutant animals and proteins
    • Mitic LL, Van Itallie CM, Anderson JM (2000) Molecular physiology and pathophysiology of tight junctions. l. Tight junction structure and function: lessons from mutant animals and proteins. Am J Physiol 279, G250-4.
    • (2000) Am. J. Physiol. , vol.279
    • Mitic, L.L.1    Van Itallie, C.M.2    Anderson, J.M.3
  • 70
    • 0025129356 scopus 로고
    • Basigin, a new, broadly distributed member of the immunoglobulin super family, has strong homology with both immunoglobulin V domain and the β-chain of major histocompatibility complex class II antigen
    • Miyauchi T, Kanekura T, Yamaoka A, Ozawa M, Miyazawa S, Muramatsu T (1990) Basigin, a new, broadly distributed member of the immunoglobulin super family, has strong homology with both immunoglobulin V domain and the β-chain of major histocompatibility complex class II antigen. J Biochem 107, 316-23.
    • (1990) J. Biochem. , vol.107 , pp. 316-323
    • Miyauchi, T.1    Kanekura, T.2    Yamaoka, A.3    Ozawa, M.4    Miyazawa, S.5    Muramatsu, T.6
  • 71
    • 0033582334 scopus 로고    scopus 로고
    • Claudin multigene family encoding four-transmembrane domain protein components of tight junction strands
    • Morita K, Furuse M, Fujimoto K, Tsukita Sh (1999a) Claudin multigene family encoding four-transmembrane domain protein components of tight junction strands. Proc Natl Acad Sci USA 96, 511-6.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 511-516
    • Morita, K.1    Furuse, M.2    Fujimoto, K.3    Tsukita, Sh.4
  • 72
    • 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 Sh (1999b) Claudin- 11/OSP-based tight junctions of myelin sheaths in brain and Sertoli cells in testis. J Cell Biol 145, 579-88.
    • (1999) J. Cell Biol. , vol.145 , pp. 579-588
    • Morita, K.1    Sasaki, H.2    Fujimoto, K.3    Furuse, M.4    Tsukita, Sh.5
  • 73
    • 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 et al. (1998) Occludin is concentrated at tight junctions of mouse/rat but not human/guinea pig Sertoli cells in testes. Am J Physiol 274, C1708-17.
    • (1998) Am. J. Physiol. , vol.274
    • Moroi, S.1    Saitou, M.2    Fujimoto, K.3
  • 74
    • 0035160160 scopus 로고    scopus 로고
    • Rat seminiferous epithelium contains a unique junction (ectoplasmic specialization) with signaling properties both of cell/cell and cell/matrix junctions
    • Mulholland DJ, Dedhar S, Vogl AW (2001) Rat seminiferous epithelium contains a unique junction (ectoplasmic specialization) with signaling properties both of cell/cell and cell/matrix junctions. Biol Reprod 64, 396-407.
    • (2001) Biol. Reprod. , vol.64 , pp. 396-407
    • Mulholland, D.J.1    Dedhar, S.2    Vogl, A.W.3
  • 75
    • 0013999287 scopus 로고
    • Some observations on the fine structure of the Sertoli cell in the human testis
    • Nagano T (1966) Some observations on the fine structure of the Sertoli cell in the human testis. Zeitscrift Zellforsch 73, 89-106.
    • (1966) Zeitscrift. Zellforsch. , vol.73 , pp. 89-106
    • Nagano, T.1
  • 76
    • 0020061112 scopus 로고
    • Further observations on the Sertoli cell junctions of the mouse testis after metal contact freeze-fracture, and comparisons with cellular junctions of other epithelial cells
    • Nagano T, Toyama Y, Suzuki F (1982) Further observations on the Sertoli cell junctions of the mouse testis after metal contact freeze-fracture, and comparisons with cellular junctions of other epithelial cells. Am J Anat 163, 47-58.
    • (1982) Am. J. Anat. , vol.163 , pp. 47-58
    • Nagano, T.1    Toyama, Y.2    Suzuki, F.3
  • 77
    • 0000585214 scopus 로고
    • The blood-testis barrier
    • (Johnson AD, Gomes WR, eds). Academic Press, New York
    • Neaves WB (1977) The blood-testis barrier. In: The Testis, Vol. 4 (Johnson AD, Gomes WR, eds). Academic Press, New York, 125-62.
    • (1977) The Testis , vol.4 , pp. 125-162
    • Neaves, W.B.1
  • 78
    • 0042398082 scopus 로고
    • Some ultrastructural features of mammalian sertoli cells
    • Nicander L (1963) Some ultrastructural features of mammalian Sertoli cells. J Ultrastruct Res 8, 190-1.
    • (1963) J. Ultrastruct. Res. , vol.8 , pp. 190-191
    • Nicander, L.1
  • 79
    • 0014159123 scopus 로고
    • An electron microscopical study of cell contacts in the seminiferous tubules of some mammals
    • Nicander L (1967) An electron microscopical study of cell contacts in the seminiferous tubules of some mammals. Zeitscrift Zellforsch 83, 375-97.
    • (1967) Zeitscrift. Zellforsch. , vol.83 , pp. 375-397
    • Nicander, L.1
  • 80
    • 0032788066 scopus 로고    scopus 로고
    • A locus responsible for arrest of spermatogenesis is located on rat chromosome 12
    • Noguchi J, Kobayashi E, Shimada A et al. (1999) A locus responsible for arrest of spermatogenesis is located on rat Chromosome 12. Mammal Genome 10, 189-90.
    • (1999) Mammal Genome , vol.10 , pp. 189-190
    • Noguchi, J.1    Kobayashi, E.2    Shimada, A.3
  • 81
    • 0036721504 scopus 로고    scopus 로고
    • Hereditary defects in both germ cells and the blood-testis barrier system in as-mutant rats: Evidences by spermatogonial transplantation and tracer-permeability analysis
    • Noguchi J, Toyama Y, Yuasa S, Kikuchi K, Kaneko H. (2002) Hereditary defects in both germ cells and the blood-testis barrier system in as-mutant rats: evidences by spermatogonial transplantation and tracer-permeability analysis. Biol Reprod 67, 880-8.
    • (2002) Biol. Reprod. , vol.67 , pp. 880-888
    • Noguchi, J.1    Toyama, Y.2    Yuasa, S.3    Kikuchi, K.4    Kaneko, H.5
  • 82
    • 0027190803 scopus 로고
    • Age-related changes in blood-concentrations of FSH, LH and testosterone and testicular morphology in a new rat sterile mutant with hereditary aspermia
    • Noguchi J, Yoshida M, Ikadai H, Imamichi T, Watanabe G, Taya K (1993) Age-related changes in blood-concentrations of FSH, LH and testosterone and testicular morphology in a new rat sterile mutant with hereditary aspermia. J Reprod Fertil 97, 433-9.
    • (1993) J. Reprod. Fertil. , vol.97 , pp. 433-439
    • Noguchi, J.1    Yoshida, M.2    Ikadai, H.3    Imamichi, T.4    Watanabe, G.5    Taya, K.6
  • 83
    • 85056037863 scopus 로고    scopus 로고
    • The tight junctions in the testis, epididymis, and vas deferens
    • (Cereijido M, Anderson J, eds). CRC Press, Boca Raton
    • Pelletier R-M (2001) The tight junctions in the testis, epididymis, and vas deferens. In: Tight Junctions (Cereijido M, Anderson J, eds). CRC Press, Boca Raton, 599-628.
    • (2001) Tight Junctions , pp. 599-628
    • Pelletier, R.-M.1
  • 85
    • 0026518565 scopus 로고
    • The blood-testis barrier and Sertoli cell junctions: Structural considerations
    • Pelletier R-M, Byers'SW (1992) The blood-testis barrier and Sertoli cell junctions: Structural considerations. Microsc Res Tech 20, 3-33.
    • (1992) Microsc. Res. Tech. , vol.20 , pp. 3-33
    • Pelletier, R.-M.1    Byers, S.W.2
  • 86
    • 0020569361 scopus 로고
    • Effects of extracellular calcium depletion on membrane topography and occluding junctions of mammary epithelial cells in culture
    • Pitelka DR, Taggart BN, Hamamoto ST (1983) Effects of extracellular calcium depletion on membrane topograplhy and occluding junctions of mammary epithelial cells in culture. J Cell Biol 96, 613-24.
    • (1983) J. Cell Biol. , vol.96 , pp. 613-624
    • Pitelka, D.R.1    Taggart, B.N.2    Hamamoto, S.T.3
  • 87
    • 0025938012 scopus 로고
    • Testicular toxicity and mutagenicity of steroidal and nonsteroidal estrogen in the male mouse
    • Plykkänen L, Jahnukainen K, Parvinen M, Santti R (1991) Testicular toxicity and mutagenicity of steroidal and nonsteroidal estrogen in the male mouse. Mut Res 261, 181-91.
    • (1991) Mut. Res. , vol.261 , pp. 181-191
    • Plykkänen, L.1    Jahnukainen, K.2    Parvinen, M.3    Santti, R.4
  • 89
    • 0018409022 scopus 로고
    • Characterization of sertoli cell-germ cell junctional specializations in dissociated testicular cells
    • Romrell LJ, Ross MH (1979) Characterization of Sertoli cell-germ cell junctional specializations in dissociated testicular cells. Anat Rec 193, 23-42.
    • (1979) Anat. Rec. , vol.193 , pp. 23-42
    • Romrell, L.J.1    Ross, M.H.2
  • 90
    • 0017102386 scopus 로고
    • The Sertoli cell junctional specialization during spermiogenesis and at spermiation
    • Ross MH (1976) The Sertoli cell junctional specialization during spermiogenesis and at spermiation. Anat Rec 186, 79-104.
    • (1976) Anat. Rec. , vol.186 , pp. 79-104
    • Ross, M.H.1
  • 91
    • 0017578775 scopus 로고
    • Sertoli-Sertoli junctions and Sertoli-spermatid junctions after efferent ductule ligation and lanthanum treatment
    • Ross MH (1977) Sertoli-Sertoli junctions and Sertoli-spermatid junctions after efferent ductule ligation and lanthanum treatment. Am J Anat 148, 49-56.
    • (1977) Am. J. Anat. , vol.148 , pp. 49-56
    • Ross, M.H.1
  • 92
    • 0017709496 scopus 로고
    • Observations on rat Sertoli ectoplasmic ('junctional') specializations in their associations with germ cells of the rat testis
    • Russell LD (1977) Observations on rat Sertoli ectoplasmic ('junctional') specializations in their associations with germ cells of the rat testis. Tissue Cell 9, 475-98.
    • (1977) Tissue Cell , vol.9 , pp. 475-498
    • Russell, L.D.1
  • 93
    • 0019119141 scopus 로고
    • Sertoli-germ cell interrelations: A review
    • Russell LD (1980) Sertoli-germ cell interrelations: a review. Gamete Res 3, 179-202.
    • (1980) Gamete Res. , vol.3 , pp. 179-202
    • Russell, L.D.1
  • 94
    • 0024066432 scopus 로고
    • The consequences of actin disruption at Sertoli ectoplasmic specialization sites facing spermatids after in vivo exposure of rat testis to cytochalasin D
    • Russell LD, Goh JC, Rashed RM, Vogl AW (1988) The consequences of actin disruption at Sertoli ectoplasmic specialization sites facing spermatids after in vivo exposure of rat testis to cytochalasin D. Biol Reprod 39, 105-8.
    • (1988) Biol. Reprod. , vol.39 , pp. 105-108
    • Russell, L.D.1    Goh, J.C.2    Rashed, R.M.3    Vogl, A.W.4
  • 96
    • 0040486525 scopus 로고
    • Sertoli ectoplasmic specializations during sprmatogenesis
    • (Steinberger A, Steinberger E, eds). Raven Press, New York
    • Russell L, Myers P, Ostenburg J, Malone J (1980) Sertoli ectoplasmic specializations during sprmatogenesis. In: Testicular Development, Structure and Function (Steinberger A, Steinberger E, eds). Raven Press, New York, 55-63.
    • (1980) Testicular Development, Structure and Function , pp. 55-63
    • Russell, L.1    Myers, P.2    Ostenburg, J.3    Malone, J.4
  • 97
    • 0021892796 scopus 로고
    • Sertoli cell junctions: Morphological and functional correlates
    • Russell LD, Peterson RN (1985) Sertoli cell junctions: Morphological and functional correlates. Int Rev Cytol 94, 177-211.
    • (1985) Int. Rev. Cytol. , vol.94 , pp. 177-211
    • Russell, L.D.1    Peterson, R.N.2
  • 98
    • 0032550221 scopus 로고    scopus 로고
    • Occludin-deficient embryonic stem cells can differentiate into polarized epithelial cells bearing tight junctions
    • Saitou M, Fujimoto K, Doi Y et al. (1998) Occludin-deficient embryonic stem cells can differentiate into polarized epithelial cells bearing tight junctions. J Cell Biol 141, 397-408.
    • (1998) J. Cell Biol. , vol.141 , pp. 397-408
    • Saitou, M.1    Fujimoto, K.2    Doi, Y.3
  • 99
    • 0028932170 scopus 로고
    • Disorganization of actin bundles of ectoplasmic specialization
    • Sakai Y, Yamashina S (1995) Disorganization of actin bundles of ectoplasmic specialization. Dev Growth Differ 37, 21-30.
    • (1995) Dev. Growth Differ. , vol.37 , pp. 21-30
    • Sakai, Y.1    Yamashina, S.2
  • 100
    • 0031885613 scopus 로고    scopus 로고
    • Junctional contacts between Sertoli cells in normal and aspermatogenic rat seminiferous epithelium contain α6β1 integrins, and their formation is controlled by follicle-stimulating hormone
    • Salanova M, Ricci G, Boitani C, Stefanini M, De Grossi S, Palombi F (1998) Junctional contacts between Sertoli cells in normal and aspermatogenic rat seminiferous epithelium contain α6ß1 integrins, and their formation is controlled by follicle-stimulating hormone. Biol Reprod 58, 371-8.
    • (1998) Biol. Reprod. , vol.58 , pp. 371-378
    • Salanova, M.1    Ricci, G.2    Boitani, C.3    Stefanini, M.4    De Grossi, S.5    Palombi, F.6
  • 101
    • 0028984244 scopus 로고
    • Integrin receptor α6β1 is localized at specific sites of cell-to-cell contact in rat seminiferous epithelium
    • Salanova M, Stefanini M, De Curtis I, Palombi F (1995) Integrin receptor α6β1 is localized at specific sites of cell-to-cell contact in rat seminiferous epithelium. Biol Reprod 52, 79-87.
    • (1995) Biol. Reprod. , vol.52 , pp. 79-87
    • Salanova, M.1    Stefanini, M.2    De Curtis, I.3    Palombi, F.4
  • 102
    • 0001383505 scopus 로고
    • Anatomy, vasculature, innervation and fluids of the male reproductive tract
    • (Knobil E, Neill J, eds). Raven Press, New York
    • Setchell BP, Brooks DE (1988) Anatomy, vasculature, innervation and fluids of the male reproductive tract. In: The Physiology of Reproduction (Knobil E, Neill J, eds). Raven Press, New York, 753-835.
    • (1988) The Physiology of Reproduction , pp. 753-835
    • Setchell, B.P.1    Brooks, D.E.2
  • 103
    • 0014439405 scopus 로고
    • A blood-testis barrier restricting passage from blood into rete testis fluid but not into the lymph
    • Setchell BP, Voglmayer JK, Waites GMH (1969) A blood-testis barrier restricting passage from blood into rete testis fluid but not into the lymph. J Physiol 200, 73-85.
    • (1969) J. Physiol. , vol.200 , pp. 73-85
    • Setchell, B.P.1    Voglmayer, J.K.2    Waites, G.M.H.3
  • 104
    • 0000297982 scopus 로고
    • The blood-testis barrier
    • (Hamilton DW, Greep RO, eds). American Physiological Society, Washington D.C
    • Setchell BP, Waites GMH (1975) The blood-testis barrier. In: Handbook of Physiology (Hamilton DW, Greep RO, eds). American Physiological Society, Washington D.C., 143-72.
    • (1975) Handbook of Physiology , pp. 143-172
    • Setchell, B.P.1    Waites, G.M.H.2
  • 105
    • 0023030826 scopus 로고
    • Identification of ZO-1: A high molecular weight polypeptide associated with the tight junction (zonula occludens) in a variety of epithelia
    • Stevenson BR, Siliciano JD, Mooseker MS, Goodenough DA (1986) Identification of ZO-1: A high molecular weight polypeptide associated with the tight junction (zonula occludens) in a variety of epithelia. J Cell Biol 103, 755-66.
    • (1986) J. Cell Biol. , vol.103 , pp. 755-766
    • Stevenson, B.R.1    Siliciano, J.D.2    Mooseker, M.S.3    Goodenough, D.A.4
  • 106
    • 0031439247 scopus 로고    scopus 로고
    • Cellular functions regulated by Src family kinases
    • Thomas SM, Brugge JS (1997) Cellular functions regulated by Src family kinases. Ann Rev Cell Dev Biol 13, 513-609.
    • (1997) Ann. Rev. Cell Dev. Biol. , vol.13 , pp. 513-609
    • Thomas, S.M.1    Brugge, J.S.2
  • 107
    • 0016691623 scopus 로고
    • Ultrastructural study of crystalloids in Sertoli cells of the normal, intersex and experimental cryptorchid swine
    • Toyama Y (1975) Ultrastructural study of crystalloids in Sertoli cells of the normal, intersex and experimental cryptorchid swine. Cell Tissue Res 158, 205-13.
    • (1975) Cell Tissue Res. , vol.158 , pp. 205-213
    • Toyama, Y.1
  • 108
    • 0017098322 scopus 로고
    • Actin-like filaments in the Sertoli cell junctional specializations in the swine and mouse testis
    • Toyama Y (1976) Actin-like filaments in the Sertoli cell junctional specializations in the swine and mouse testis. Anat Rec 186, 477-92.
    • (1976) Anat. Rec. , vol.186 , pp. 477-492
    • Toyama, Y.1
  • 109
    • 0017333775 scopus 로고
    • Actin-like filaments in the myoid cell of the testis
    • Toyama Y (1977) Actin-like filaments in the myoid cell of the testis. Cell Tissue Res 177, 221-6.
    • (1977) Cell Tissue Res. , vol.177 , pp. 221-226
    • Toyama, Y.1
  • 110
    • 0025101273 scopus 로고
    • Ultrastructural study of crystalloids in Sertoli cells of the three-toed sloth (Bradypus tridactylus)
    • Toyama Y, Calderón FU, Quesada R (1990) Ultrastructural study of crystalloids in Sertoli cells of the three-toed sloth (Bradypus tridactylus). Cell Tissue Res 259, 599-602.
    • (1990) Cell Tissue Res. , vol.259 , pp. 599-602
    • Toyama, Y.1    Calderón, F.U.2    Quesada, R.3
  • 111
    • 0035912963 scopus 로고    scopus 로고
    • β-estradiol 3-benzoate affects spermatogenesis in the adult mouse
    • Toyama Y, Hosoi I, Ichikawa S et al. (2001b) β-estradiol 3-benzoate affects spermatogenesis in the adult mouse. Mol Cell Endocrinol 178, 161-8.
    • (2001) Mol. Cell Endocrinol. , vol.178 , pp. 161-168
    • Toyama, Y.1    Hosoi, I.2    Ichikawa, S.3
  • 113
    • 0018721814 scopus 로고
    • Crystalloids of actin-like filaments in the sertoll cell of the swine testis
    • Toyama Y, Obinata T, Holtzer H (1979) Crystalloids of actin-like filaments in the Sertoll cell of the swine testis. Anat Rec 195, 47-62.
    • (1979) Anat. Rec. , vol.195 , pp. 47-62
    • Toyama, Y.1    Obinata, T.2    Holtzer, H.3
  • 114
    • 0035059232 scopus 로고    scopus 로고
    • Neonatally administered diethylstilbestrol retards the development of the blood-testis barrier in the rat
    • Toyama Y, Ohkawa M, Oku R, Maekawa M, Yuasa S (2001a) Neonatally administered diethylstilbestrol retards the development of the blood-testis barrier in the rat. J Androl 22, 413-23.
    • (2001) J. Androl. , vol.22 , pp. 413-423
    • Toyama, Y.1    Ohkawa, M.2    Oku, R.3    Maekawa, M.4    Yuasa, S.5
  • 115
    • 0015828838 scopus 로고
    • The normal development of the blood-testis barrier and the effects of clomiphene and estrogen treatment
    • Vitale R, Fawcett DW, Dym M (1973) The normal development of the blood-testis barrier and the effects of clomiphene and estrogen treatment. Anat Rec 176, 333-44.
    • (1973) Anat. Rec. , vol.176 , pp. 333-344
    • Vitale, R.1    Fawcett, D.W.2    Dym, M.3
  • 116
    • 0014806707 scopus 로고
    • The mechanism of spermiation in the hamster. I. Ultrastructure of spontaneous spermiation
    • Vitale-Calpe R, Burgos MH (1970) The mechanism of spermiation in the hamster. l. Ultrastructure of spontaneous spermiation. J Ultrastruct Res 31, 381-93.
    • (1970) J. Ultrastruct. Res. , vol.31 , pp. 381-393
    • Vitale-Calpe, R.1    Burgos, M.H.2
  • 117
    • 0024891608 scopus 로고
    • The distribution and function of organized concentrations of actin filaments in mammalian spermatogenic cells and Sertoli cells
    • Vogl AW (1989) The distribution and function of organized concentrations of actin filaments in mammalian spermatogenic cells and Sertoli cells. Int Rev Cytol 119, 1-56.
    • (1989) Int. Rev. Cytol. , vol.119 , pp. 1-56
    • Vogl, A.W.1
  • 118
    • 0020610214 scopus 로고
    • Sertoli cells of the golden mantled ground squirrel (Spermophilus lateralis): A model system for the study of shape change
    • Vogl AW, Lin YC, Dym M, Fawcett DW (1983) Sertoli cells of the golden mantled ground squirrel (Spermophilus lateralis): a model system for the study of shape change. Am J Anat 168,83-98.
    • (1983) Am. J. Anat. , vol.168 , pp. 83-98
    • Vogl, A.W.1    Lin, Y.C.2    Dym, M.3    Fawcett, D.W.4
  • 119
  • 120
    • 0026398660 scopus 로고
    • Ectoplasmic ('junctional') specializations in mammalian Sertoli cells: Influence on spermatogenic cells
    • Vogl AW, Pfeiffer DC, Redenbach DM (1991) Ectoplasmic ('junctional') specializations in mammalian Sertoli cells: Influence on spermatogenic cells. Ann NY Acad Sci 637, 175-202.
    • (1991) Ann. NY Acad. Sci. , vol.637 , pp. 175-202
    • Vogl, A.W.1    Pfeiffer, D.C.2    Redenbach, D.M.3
  • 121
    • 0021924974 scopus 로고
    • Arrangement and possible function of actin filament bundles in ectoplasmic specializations of ground squirrel Sertoli cells
    • Vogl AW, Soucy LJ (1985) Arrangement and possible function of actin filament bundles in ectoplasmic specializations of ground squirrel Sertoli cells. J Cell Biol 100, 814-25.
    • (1985) J. Cell Biol. , vol.100 , pp. 814-825
    • Vogl, A.W.1    Soucy, L.J.2
  • 122
    • 0023948077 scopus 로고
    • Effects of cytochalasin D on the integrity of the sertoli cell (blood-testis) barrier
    • Weber JE, Turner TT, Tung KSK, Russell LD (1988) Effects of cytochalasin D on the integrity of the Sertoli cell (blood-testis) barrier. Am J Anat 182, 130-47.
    • (1988) Am. J. Anat. , vol.182 , pp. 130-147
    • Weber, J.E.1    Turner, T.T.2    Tung, K.S.K.3    Russell, L.D.4
  • 123
    • 0021260494 scopus 로고
    • The control of male fertility by 1, 2, 3-trihydroxypropane (THP; glycerol): Rapid arrest of spermatogenesis without altering libido, accessory organs, gonadal steroidogenesis, and serum testosterone, LH and FSH
    • Wiebe JP, Barr KJ (1984a) The control of male fertility by 1, 2, 3-trihydroxypropane (THP; glycerol): rapid arrest of spermatogenesis without altering libido, accessory organs, gonadal steroidogenesis, and serum testosterone, LH and FSH. Contraception 29, 291-302.
    • (1984) Contraception , vol.29 , pp. 291-302
    • Wiebe, J.P.1    Barr, K.J.2
  • 124
    • 0021257001 scopus 로고
    • Suppression of spermatogenesis without inhibition of steroidogenesis by a 1, 2, 3-trihydroxypropane solution
    • Wiebe JP, Barr KJ (1984b) Suppression of spermatogenesis without inhibition of steroidogenesis by a 1, 2, 3-trihydroxypropane solution. Life Sci 34, 1747-54.
    • (1984) Life Sci. , vol.34 , pp. 1747-1754
    • Wiebe, J.P.1    Barr, K.J.2
  • 125
    • 0024518624 scopus 로고
    • Sustained azoospermia in squirrel monkey, Saimiri sciureus, resulting from a single intratesticular glycerol injection
    • Wiebe JP, Barr KJ, Buckingham KD (1989) Sustained azoospermia in squirrel monkey, Saimiri sciureus, resulting from a single intratesticular glycerol injection. Contraception 39, 447-57.
    • (1989) Contraception , vol.39 , pp. 447-457
    • Wiebe, J.P.1    Barr, K.J.2    Buckingham, K.D.3
  • 126
    • 0033812826 scopus 로고    scopus 로고
    • Glycerol disrupts tight junction-associated actin microfilaments, occludin, and microtubules in sertoli cells
    • Wiebe JP, Kowalik A, Gallardi RL, Egeler O, Clubb BH (2000) Glycerol disrupts tight junction-associated actin microfilaments, occludin, and microtubules in Sertoli cells. J Androl 21, 625-35.
    • (2000) J. Androl. , vol.21 , pp. 625-635
    • Wiebe, J.P.1    Kowalik, A.2    Gallardi, R.L.3    Egeler, O.4    Clubb, B.H.5
  • 127
    • 0026751782 scopus 로고
    • Localization and differential expression of two isoforms of the tight junction protein ZO-1
    • Willott E, Balda MS, Heintzelman M, Jameson B, Anderson JM (1992) Localization and differential expression of two isoforms of the tight junction protein ZO-1. Am J Physiol 31, C1119-C24.
    • (1992) Am. J. Physiol. , vol.31
    • Willott, E.1    Balda, M.S.2    Heintzelman, M.3    Jameson, B.4    Anderson, J.M.5
  • 128
    • 0031047483 scopus 로고    scopus 로고
    • A synthetic peptide corresponding to the extracellular domain of occludin perturbs the tight junction permeability barrier
    • Wong V, Gumbiner BM (1997) A synthetic peptide corresponding to the extracellular domain of occludin perturbs the tight junction permeability barrier. J Cell Biol 136, 399-409.
    • (1997) J. Cell Biol. , vol.136 , pp. 399-409
    • Wong, V.1    Gumbiner, B.M.2
  • 129
    • 0015589364 scopus 로고
    • Testicular biopsy in the study of male infertility. I. Testicular causes of infertility
    • Wong T-W, Straus FH, Warner NE (1973) Testicular biopsy in the study of male infertility. 1. Testicular causes of infertility. Arch Pathol 95, 151-9.
    • (1973) Arch. Pathol. , vol.95 , pp. 151-159
    • Wong, T.-W.1    Straus, F.H.2    Warner, N.E.3
  • 130
    • 0034786797 scopus 로고    scopus 로고
    • Postnatal development of the testis in Japanese children based on observations of undescended testes
    • Yuasa J, Ito H, Toyama Y, Yuasa S (2001) Postnatal development of the testis in Japanese children based on observations of unclescencled testes. Int J Urol 8, 490-4.
    • (2001) Int. J. Urol. , vol.8 , pp. 490-494
    • Yuasa, J.1    Ito, H.2    Toyama, Y.3    Yuasa, S.4
  • 131
    • 0034604349 scopus 로고    scopus 로고
    • The deaf jerker mouse has a mutation in the gene encoding the espin actin-bundling proteins of hair cell stereocilia and lacks espins
    • Zheng L, Sekerková G, Vranich K, Tilney LG, Mugnaini E, Bartles JR (2000) The deaf jerker mouse has a mutation in the gene encoding the espin actin-bundling proteins of hair cell stereocilia and lacks espins. Cell 102, 377-85.
    • (2000) Cell , vol.102 , pp. 377-385
    • Zheng, L.1    Sekerková, G.2    Vranich, K.3    Tilney, L.G.4    Mugnaini, E.5    Bartles, J.R.6
  • 132
    • 0026768708 scopus 로고
    • Testins are localized to the junctional complexes of rat sertoli and eplididymal cells
    • Zong SD, Bardin CW, Phillips D, Cheng CY (1992) Testins are localized to the junctional complexes of rat Sertoli and eplididymal cells. Biol Reprod 47, 568-72.
    • (1992) Biol. Reprod. , vol.47 , pp. 568-572
    • Zong, S.D.1    Bardin, C.W.2    Phillips, D.3    Cheng, C.Y.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.