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Volumn 274, Issue 6 43-6, 1998, Pages

Occludin is concentrated at tight junctions of mouse/rat but not human/guinea pig Sertoli cells in testes

Author keywords

Blood testis barrier; Cell adhesion; Phosphorylation; Testis; ZO 1

Indexed keywords

OCCLUDIN;

EID: 0031798631     PISSN: 03636143     EISSN: None     Source Type: Journal    
DOI: 10.1152/ajpcell.1998.274.6.c1708     Document Type: Article
Times cited : (89)

References (39)
  • 1
    • 0023918616 scopus 로고
    • Characterization of ZO-1, a protein component of the tight junction from mouse liver and Madin-Darby canine kidney cells
    • Anderson, J. M., B. R. Stevenson, L. A. Jesaitis, D. A. Goodenough, and M. S. Mooseker. Characterization of ZO-1, a protein component of the tight junction from mouse liver and Madin-Darby canine kidney cells. J. Cell Biol. 106: 1141-1149, 1988.
    • (1988) J. Cell Biol. , vol.106 , pp. 1141-1149
    • Anderson, J.M.1    Stevenson, B.R.2    Jesaitis, L.A.3    Goodenough, D.A.4    Mooseker, M.S.5
  • 3
    • 0027414695 scopus 로고
    • Two classes of tight junctions are revealed by ZO-1 isoforms
    • Cell Physiol. 33
    • Balda, M. S., and J. M. Anderson. Two classes of tight junctions are revealed by ZO-1 isoforms. Am. J. Physiol. 264 (Cell Physiol. 33): C918-C924, 1993.
    • (1993) Am. J. Physiol. , vol.264
    • Balda, M.S.1    Anderson, J.M.2
  • 4
    • 0029799520 scopus 로고    scopus 로고
    • Functional dissociation of paracellular permeability and transepithelial electrical resistance and disruption of the apical-basolateral intramembrane diffusion barrier by expression of a mutant tight junction membrane protein
    • Balda, M. S., J. A. Whitney, C. Flores, S. González, M. Cereijido, and K. Matter. Functional dissociation of paracellular permeability and transepithelial electrical resistance and disruption of the apical-basolateral intramembrane diffusion barrier by expression of a mutant tight junction membrane protein. J. Cell Biol. 134: 1031-1049, 1996.
    • (1996) J. Cell Biol. , vol.134 , pp. 1031-1049
    • Balda, M.S.1    Whitney, J.A.2    Flores, C.3    González, S.4    Cereijido, M.5    Matter, K.6
  • 5
    • 0021038598 scopus 로고
    • Postnatal formation of the blood-testis barrier in the rat with special reference to the initiation of meiosis
    • Bergmann, M., and R. Dierichs. Postnatal formation of the blood-testis barrier in the rat with special reference to the initiation of meiosis. Anat. Embryol. 168: 269-275, 1983.
    • (1983) Anat. Embryol. , vol.168 , pp. 269-275
    • Bergmann, M.1    Dierichs, R.2
  • 6
    • 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., R. Graham, H. N. Dai, and B. Hoxter. 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.
    • (1991) Am. J. Anat. , vol.191 , pp. 35-47
    • Byers, S.1    Graham, R.2    Dai, H.N.3    Hoxter, B.4
  • 7
    • 0024291701 scopus 로고
    • Cingulin, a new peripheral component of tight junctions
    • Citi, S., H. Sabanay, R. Jakes, B. Geiger, and J. Kendrick-Jones. Cingulin, a new peripheral component of tight junctions. Nature 333: 272-276, 1988.
    • (1988) Nature , vol.333 , pp. 272-276
    • Citi, S.1    Sabanay, H.2    Jakes, R.3    Geiger, B.4    Kendrick-Jones, J.5
  • 8
    • 0015608073 scopus 로고
    • The fine structure of the monkey (Macaca) Sertoli cell and its role in maintaining the blood-testis barrier
    • Dym, M. The fine structure of the monkey (Macaca) Sertoli cell and its role in maintaining the blood-testis barrier. Anat. Rec. 175: 639-656, 1973.
    • (1973) Anat. Rec. , vol.175 , pp. 639-656
    • Dym, M.1
  • 9
    • 0014892078 scopus 로고
    • The blood-testis barrier in the rat and the physiological compartmentation of the seminiferous epithelium
    • Dym, M., and D. W. Fawcett. The blood-testis barrier in the rat and the physiological compartmentation of the seminiferous epithelium. Biol. Reprod. 3: 308-326, 1970.
    • (1970) Biol. Reprod. , vol.3 , pp. 308-326
    • Dym, M.1    Fawcett, D.W.2
  • 10
    • 0000752197 scopus 로고
    • Junctional complexes in various epithelia
    • Farquhar, M. G., and G. E. Palade. Junctional complexes in various epithelia. J. Cell Biol. 17: 375-412, 1963.
    • (1963) J. Cell Biol. , vol.17 , pp. 375-412
    • Farquhar, M.G.1    Palade, G.E.2
  • 11
    • 0014884660 scopus 로고
    • Electron microscopic observations on the structural components of the blood-testis barrier
    • Fawcett, D. W., L. V. Leak, and P. M. Heidger. Electron microscopic observations on the structural components of the blood-testis barrier. J. Reprod. Fertil. Suppl. 10: 105-122, 1970.
    • (1970) J. Reprod. Fertil. Suppl. , vol.10 , pp. 105-122
    • Fawcett, D.W.1    Leak, L.V.2    Heidger, P.M.3
  • 12
    • 0028828220 scopus 로고
    • Freeze-fracture replica electron microscopy combined with SDS digestion for cytochemical labeling of integral membrane proteins
    • Fujimoto, K. Freeze-fracture replica electron microscopy combined with SDS digestion for cytochemical labeling of integral membrane proteins. J. Cell Sci. 108: 3443-3449, 1995.
    • (1995) J. Cell Sci. , vol.108 , pp. 3443-3449
    • Fujimoto, K.1
  • 13
    • 0031046606 scopus 로고    scopus 로고
    • SDS-digested freeze-fracture replica labeling electron microscopy to study the two-dimensional distribution of integral membrane proteins and phospholipids in biomembranes: Practical procedure, interpretation and application
    • Fujimoto, K. SDS-digested freeze-fracture replica labeling electron microscopy to study the two-dimensional distribution of integral membrane proteins and phospholipids in biomembranes: practical procedure, interpretation and application. Histochem. Cell Biol. 107: 87-96, 1997.
    • (1997) Histochem. Cell Biol. , vol.107 , pp. 87-96
    • Fujimoto, K.1
  • 15
    • 0028110309 scopus 로고
    • Direct association of occludin with ZO-1 and its possible involvement in the localization of occludin at tight junctions
    • Furuse, M., M. Itoh, T. Hirase, A. Nagafuchi, S. Yonemura, S. Tsukita, and S. Tsukita. Direct association of occludin with ZO-1 and its possible involvement in the localization of occludin at tight junctions. J. Cell Biol. 127: 1617-1626, 1994.
    • (1994) J. Cell Biol. , vol.127 , pp. 1617-1626
    • Furuse, M.1    Itoh, M.2    Hirase, T.3    Nagafuchi, A.4    Yonemura, S.5    Tsukita, S.6    Tsukita, S.7
  • 16
    • 84907034898 scopus 로고
    • Fine structure and development of Sertoli junctions in human testis
    • Furuya, S., Y. Kumamoto, and S. Sugiyama. Fine structure and development of Sertoli junctions in human testis. Arch. Androl. 1: 211-219, 1978.
    • (1978) Arch. Androl. , vol.1 , pp. 211-219
    • Furuya, S.1    Kumamoto, Y.2    Sugiyama, S.3
  • 17
    • 0023612699 scopus 로고
    • Structure, biochemistry, and assembly of epithelial tight junctions
    • Cell Physiol. 22
    • Gumbiner, B. Structure, biochemistry, and assembly of epithelial tight junctions. Am. J. Physiol. 253 (Cell Physiol. 22): C749-C758, 1987.
    • (1987) Am. J. Physiol. , vol.253
    • Gumbiner, B.1
  • 18
    • 0027715358 scopus 로고
    • Breaking through the tight junction barrier
    • Gumbiner, B. Breaking through the tight junction barrier. J. Cell Biol. 123: 1631-1633, 1993.
    • (1993) J. Cell Biol. , vol.123 , pp. 1631-1633
    • Gumbiner, B.1
  • 19
    • 0026345292 scopus 로고
    • Identification of a 160-kDa polypeptide that binds to the tight junction protein ZO-1
    • Gumbiner, B., T. Lowenkopf, and D. Apatira. Identification of a 160-kDa polypeptide that binds to the tight junction protein ZO-1. Proc. Natl. Acad. Sci. USA 88: 3460-3464, 1991.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 3460-3464
    • Gumbiner, B.1    Lowenkopf, T.2    Apatira, D.3
  • 22
    • 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., A. Nagafuchi, S. Yonemura, T. Kitani-Yasuda, S. Tsukita, and S. Tsukita. 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.
    • (1993) J. Cell Biol. , vol.121 , pp. 491-502
    • Itoh, M.1    Nagafuchi, A.2    Yonemura, S.3    Kitani-Yasuda, T.4    Tsukita, S.5    Tsukita, S.6
  • 23
    • 0029840160 scopus 로고    scopus 로고
    • Symplekin, a novel type of tight junction plaque protein
    • Keon, B. H., S. Schäfer, C. Kuhn, C. Grund, and W. W. Franke. Symplekin, a novel type of tight junction plaque protein. J. Cell Biol. 134: 1003-1018, 1996.
    • (1996) J. Cell Biol. , vol.134 , pp. 1003-1018
    • Keon, B.H.1    Schäfer, S.2    Kuhn, C.3    Grund, C.4    Franke, W.W.5
  • 24
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680-685, 1970.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 26
    • 0017608163 scopus 로고
    • Intercellular junction development in maturing rat seminiferous tubules
    • Meyer, R., Z. Posalaky, and D. McGinley. Intercellular junction development in maturing rat seminiferous tubules. J. Ultrastruct. Res. 61: 271-283, 1977.
    • (1977) J. Ultrastruct. Res. , vol.61 , pp. 271-283
    • Meyer, R.1    Posalaky, Z.2    McGinley, D.3
  • 27
    • 0017089377 scopus 로고
    • The postnatal development of the junctional complexes of the mouse Sertoli cells as revealed by freeze-fracture
    • Nagano, T., and F. Suzuki. The postnatal development of the junctional complexes of the mouse Sertoli cells as revealed by freeze-fracture. Anat. Rec. 185: 403-418, 1976.
    • (1976) Anat. Rec. , vol.185 , pp. 403-418
    • Nagano, T.1    Suzuki, F.2
  • 28
    • 0023793109 scopus 로고
    • Cyclic modulation of Sertoli cell junctional complexes in a seasonal breeder: The mink (Mustela vison)
    • Pelletier, R. M. Cyclic modulation of Sertoli cell junctional complexes in a seasonal breeder: the mink (Mustela vison). Am. J. Anat. 183: 68-102, 1988.
    • (1988) Am. J. Anat. , vol.183 , pp. 68-102
    • Pelletier, R.M.1
  • 29
    • 0021044050 scopus 로고
    • The Sertoli cell junctional complex: Structure and permeability to filipin in the neonatal and adult guinea pig
    • Pelletier, R. M., and D. S. Friend. The Sertoli cell junctional complex: structure and permeability to filipin in the neonatal and adult guinea pig. Am. J. Anat. 168: 213-228, 1983.
    • (1983) Am. J. Anat. , vol.168 , pp. 213-228
    • Pelletier, R.M.1    Friend, D.S.2
  • 30
    • 0017894554 scopus 로고
    • The blood-testis barrier and its formation relative to spermatocyte maturation in the adult rat: A lanthanum tracer study
    • Russell, L. D. The blood-testis barrier and its formation relative to spermatocyte maturation in the adult rat: a lanthanum tracer study. Anat. Rec. 190: 99-112, 1978.
    • (1978) Anat. Rec. , vol.190 , pp. 99-112
    • Russell, L.D.1
  • 31
    • 0021892796 scopus 로고
    • Sertoli cell junctions: Morphological and functional correlates
    • Russell, L. D., and R. N. Peterson. Sertoli cell junctions: morphological and functional correlates. Int. Rev. Cytol. 94: 177-211, 1985.
    • (1985) Int. Rev. Cytol. , vol.94 , pp. 177-211
    • Russell, L.D.1    Peterson, R.N.2
  • 33
    • 0030982357 scopus 로고    scopus 로고
    • Possible involvement of phosphorylation of occludin in tight junction formation
    • Sakakibara, A., M. Furuse, M. Saitou, Y. Ando-Akatsuka, and S. Tsukita. Possible involvement of phosphorylation of occludin in tight junction formation. J. Cell Biol. 137: 1393-1401, 1997.
    • (1997) J. Cell Biol. , vol.137 , pp. 1393-1401
    • Sakakibara, A.1    Furuse, M.2    Saitou, M.3    Ando-Akatsuka, Y.4    Tsukita, S.5
  • 34
    • 0026752739 scopus 로고
    • Structure, function, and regulation of cellular tight junctions
    • Lung Cell. Mol. Physiol. 6
    • Schneeberger, E. E., and R. D. Lynch. Structure, function, and regulation of cellular tight junctions. Am. J. Physiol. 262 (Lung Cell. Mol. Physiol. 6): L647-L661, 1992.
    • (1992) Am. J. Physiol. , vol.262
    • Schneeberger, E.E.1    Lynch, R.D.2
  • 35
    • 0015846194 scopus 로고
    • Further observations on the fine structure of freeze-cleaved tight junctions
    • Staehlin, L. A. Further observations on the fine structure of freeze-cleaved tight junctions. J. Cell Sci. 13: 763-786, 1973.
    • (1973) J. Cell Sci. , vol.13 , pp. 763-786
    • Staehlin, L.A.1
  • 36
    • 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, B. R., J. D. Siliciano, M. S. Mooseker, and D. A. Goodenough. 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: 755-766, 1986.
    • (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
  • 37
    • 0015828838 scopus 로고
    • The normal development of the blood-testis barrier and the effects of clomiphene and estrogen treatment
    • Vitale, R., D. W. Fawcett, and M. Dym. The normal development of the blood-testis barrier and the effects of clomiphene and estrogen treatment. Anat. Rec. 176: 333-344, 1973.
    • (1973) Anat. Rec. , vol.176 , pp. 333-344
    • Vitale, R.1    Fawcett, D.W.2    Dym, M.3
  • 38
    • 0031047483 scopus 로고    scopus 로고
    • A synthetic peptide corresponding to the extracellular domain of occludin perturbs the tight junction permeability barrier
    • Wong, V., and B. M. Gumbiner. A synthetic peptide corresponding to the extracellular domain of occludin perturbs the tight junction permeability barrier. J. Cell Biol. 136: 399-409, 1997.
    • (1997) J. Cell Biol. , vol.136 , pp. 399-409
    • Wong, V.1    Gumbiner, B.M.2
  • 39
    • 0027393734 scopus 로고
    • Monoclonal antibody 7H6 reacts with a novel tight junction-associated protein distinct from ZO-1, cingulin and ZO-2
    • Zhong, Y., T. Saitoh, T. Minase, N. Sawada, K. Enomoto, and M. Mori. Monoclonal antibody 7H6 reacts with a novel tight junction-associated protein distinct from ZO-1, cingulin and ZO-2. J. Cell Biol. 120: 477-483, 1993.
    • (1993) J. Cell Biol. , vol.120 , pp. 477-483
    • Zhong, Y.1    Saitoh, T.2    Minase, T.3    Sawada, N.4    Enomoto, K.5    Mori, M.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.