메뉴 건너뛰기




Volumn 57, Issue 2, 1997, Pages 367-376

Differential distribution of the tight-junction-associated protein ZO-1 isoforms α+ and α- in guinea pig sertoli cells: A possible association with F-actin and G-actin

Author keywords

[No Author keywords available]

Indexed keywords

F ACTIN; G ACTIN;

EID: 0030762957     PISSN: 00063363     EISSN: None     Source Type: Journal    
DOI: 10.1095/biolreprod57.2.367     Document Type: Article
Times cited : (37)

References (46)
  • 1
    • 0018095313 scopus 로고
    • Cell to cell relationships in the seminiferous epithelium in the mouse embryo
    • Nagano T, Suzuki F. Cell to cell relationships in the seminiferous epithelium in the mouse embryo. Cell Tissue Res 1978; 189:389-401.
    • (1978) Cell Tissue Res , vol.189 , pp. 389-401
    • Nagano, T.1    Suzuki, F.2
  • 2
    • 0018894507 scopus 로고
    • Ultrastructural study of Sertoli cells in rat seminiferous tubules during intrauterine life and the postnatal period
    • Hatier R, Grignon G. Ultrastructural study of Sertoli cells in rat seminiferous tubules during intrauterine life and the postnatal period. Anat Embryol 1980; 160:11-27.
    • (1980) Anat Embryol , vol.160 , pp. 11-27
    • Hatier, R.1    Grignon, G.2
  • 3
    • 0014892078 scopus 로고
    • The blood-testis barrier in the rat and the physiological compartmentation of the seminiferous epithelium
    • Dym M, Fawcett DW. The blood-testis barrier in the rat and the physiological compartmentation of the seminiferous epithelium. Biol Reprod 1970; 3:308-326.
    • (1970) Biol Reprod , vol.3 , pp. 308-326
    • Dym, M.1    Fawcett, D.W.2
  • 4
    • 0021044050 scopus 로고
    • The Sertoli cell junctional complex: Structure and permeability to filipin in the neonatal and adult guinea pig
    • Pelletier R-M, Friend DS. The Sertoli cell junctional complex: structure and permeability to filipin in the neonatal and adult guinea pig. Am J Anat 1983; 168:213-228.
    • (1983) Am J Anat , vol.168 , pp. 213-228
    • Pelletier, R.-M.1    Friend, D.S.2
  • 5
    • 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. The normal development of the blood-testis barrier and the effects of clomiphene and estrogen treatment. Anat Rec 1973; 176:333-344.
    • (1973) Anat Rec , vol.176 , pp. 333-344
    • Vitale, R.1    Fawcett, D.W.2    Dym, M.3
  • 6
    • 0014439405 scopus 로고
    • A blood-testis barrier restricting passage from blood into rete testis fluid but not into lymph
    • Setchell BP, Voglmayr JK, Waites GMH, A blood-testis barrier restricting passage from blood into rete testis fluid but not into lymph. J Physiol 1969; 200:73-85.
    • (1969) J Physiol , vol.200 , pp. 73-85
    • Setchell, B.P.1    Voglmayr, J.K.2    Waites, G.M.H.3
  • 7
    • 0001892618 scopus 로고    scopus 로고
    • Blood-tissue barriers in the male reproductive system
    • Martinez-Garcia F, Regadera J (eds.). London: Churchill Livingstone; in press
    • Pelletier R-M. Blood-tissue barriers in the male reproductive system. In: Martinez-Garcia F, Regadera J (eds.), Progress in Biology and Pathology on Male Reproduction. London: Churchill Livingstone; 1997; (in press).
    • (1997) Progress in Biology and Pathology on Male Reproduction
    • Pelletier, R.-M.1
  • 8
    • 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 1988; 183:68-102.
    • (1988) Am J Anat , vol.183 , pp. 68-102
    • Pelletier, R.-M.1
  • 9
    • 0026518565 scopus 로고
    • The blood-testis barrier and Sertoli cell junctions: Structural considerations
    • Pelletier R-M, Byers SW. The blood-testis barrier and Sertoli cell junctions: structural considerations. Microsc Res Tech 1992; 20:3-33.
    • (1992) Microsc Res Tech , vol.20 , pp. 3-33
    • Pelletier, R.-M.1    Byers, S.W.2
  • 10
    • 0023918616 scopus 로고
    • Characterization of ZO-1, a protein component of the tight junction from mouse liver and Madin-Darby canine kidney cells
    • Anderson JM, Stevenson B, Jesaitis LA, Goodenough DA, Mooseker MS. Characterization of ZO-1, a protein component of the tight junction from mouse liver and Madin-Darby canine kidney cells. J Cell Biol 1988; 106:1141-1149.
    • (1988) J Cell Biol , vol.106 , pp. 1141-1149
    • Anderson, J.M.1    Stevenson, B.2    Jesaitis, L.A.3    Goodenough, D.A.4    Mooseker, M.S.5
  • 11
    • 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. Identification of ZO-1: a high molecular weight polypeptide associated with the tight junction (zonula occludens) in a variety of epithelia. J Cell Biol 1986; 103:755-766.
    • (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
  • 12
    • 0026345292 scopus 로고
    • Identification of a 160-kDa polypeptide that binds to the tight junction protein ZO-1
    • Gumbiner B, Lowenkopf T, Apatira D. Identification of a 160-kDa polypeptide that binds to the tight junction protein ZO-1. Proc Natl Acad Sci USA 1991; 88:3460-3464.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 3460-3464
    • Gumbiner, B.1    Lowenkopf, T.2    Apatira, D.3
  • 14
    • 0027240084 scopus 로고
    • The tight junction protein ZO-1 is homologous to the Drosophila disc-large tumor suppressor protein of septate junctions
    • Willott E, Balda MS, Fanning AS, Jameson B, Van Itallie C, Anderson JM. The tight junction protein ZO-1 is homologous to the Drosophila disc-large tumor suppressor protein of septate junctions. Proc Natl Acad Sci USA 1993; 90:7834-7838.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 7834-7838
    • Willott, E.1    Balda, M.S.2    Fanning, A.S.3    Jameson, B.4    Van Itallie, C.5    Anderson, J.M.6
  • 15
    • 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 S, Tsukita S. A 220-kD undercoat-constitutive protein: its specific localization at cadherin-based cell-cell adhesion sites. J Cell Biol 1991; 115:1449-1462.
    • (1991) J Cell Biol , vol.115 , pp. 1449-1462
    • Itoh, M.1    Yonemura, S.2    Nagafuchi, A.3    Tsukita, S.4    Tsukita, S.5
  • 16
    • 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, Ysukita S, Tsukita S. 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 1993; 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    Ysukita, S.5    Tsukita, S.6
  • 17
    • 0028287035 scopus 로고
    • Molecular characterization and tissue distribution of ZO-2, a tight junction protein homologous to ZO-1 and the Drosophila discs-large tumor suppressor protein
    • Jesaitis LA, Goodenough DA. Molecular characterization and tissue distribution of ZO-2, a tight junction protein homologous to ZO-1 and the Drosophila discs-large tumor suppressor protein. J Cell Biol 1994; 124:949-961.
    • (1994) J Cell Biol , vol.124 , pp. 949-961
    • Jesaitis, L.A.1    Goodenough, D.A.2
  • 18
    • 0002659233 scopus 로고
    • Sertoli cell tight junctions and the blood-testis barrier
    • Cerejido M (ed.). Boca Raton, FL: CRC Press
    • Byers SW, Pelletier R-M. Sertoli cell tight junctions and the blood-testis barrier. In: Cerejido M (ed.), Tight Junctions. Boca Raton, FL: CRC Press; 1992: 279-304.
    • (1992) Tight Junctions , pp. 279-304
    • Byers, S.W.1    Pelletier, R.-M.2
  • 19
    • 0026751782 scopus 로고
    • Localization and differential expression of two isoforms of the tight junction protein ZO-1
    • Cell Physiol 31
    • Willott E, Balda MS, Heintzelman M, Jameson B, Anderson JM. Localization and differential expression of two isoforms of the tight junction protein ZO-1. Am J Physiol 1992; 262 (Cell Physiol 31):C1119-C1124.
    • (1992) Am J Physiol , vol.262
    • Willott, E.1    Balda, M.S.2    Heintzelman, M.3    Jameson, B.4    Anderson, J.M.5
  • 20
    • 0026736220 scopus 로고
    • Diversity among tight junctions in rat kidney: Glomerular slit diaphragms and endothelial junctions express only one isoform of the tight junction protein ZO-1
    • Kurihara H, Anderson JM, Farquhar MG. Diversity among tight junctions in rat kidney: glomerular slit diaphragms and endothelial junctions express only one isoform of the tight junction protein ZO-1. Proc Natl Acad Sci USA 1992; 89:7075-7079.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 7075-7079
    • Kurihara, H.1    Anderson, J.M.2    Farquhar, M.G.3
  • 21
    • 0025008077 scopus 로고
    • The tight junction protein ZO-1 is concentrated along slit diaphragms of the glomerular epithelium
    • Schnabel E, Anderson JM, Farquhar MG. The tight junction protein ZO-1 is concentrated along slit diaphragms of the glomerular epithelium. J Cell Biol 1990; 11:1255-1263.
    • (1990) J Cell Biol , vol.11 , pp. 1255-1263
    • Schnabel, E.1    Anderson, J.M.2    Farquhar, M.G.3
  • 22
    • 0028953668 scopus 로고
    • Increased Tyr phosphorylation of ZO-1 during modification of tight junctions between glomerular foot processes
    • Renal Fluid Electrolyte Physiol 37
    • Kurihara H, Anderson JM, Farquhar MG. Increased Tyr phosphorylation of ZO-1 during modification of tight junctions between glomerular foot processes. Am J Physiol 1995; 268 (Renal Fluid Electrolyte Physiol 37):F514-F524.
    • (1995) Am J Physiol , vol.268
    • Kurihara, H.1    Anderson, J.M.2    Farquhar, M.G.3
  • 23
    • 0000344610 scopus 로고
    • Cycle of the seminiferous epithelium of the guinea pig: A method for identification of the stages
    • Clermont Y. Cycle of the seminiferous epithelium of the guinea pig: a method for identification of the stages. Fertil Steril 1960; 11:563-573.
    • (1960) Fertil Steril , vol.11 , pp. 563-573
    • Clermont, Y.1
  • 24
    • 0027414695 scopus 로고
    • Two classes of tight junctions are revealed by ZO-1 isoforms
    • Cell Physiol 33
    • Balda MS, Anderson JM. Two classes of tight junctions are revealed by ZO-1 isoforms. Am J Physiol 1993; 264 (Cell Physiol 33):C918-C924.
    • (1993) Am J Physiol , vol.264
    • Balda, M.S.1    Anderson, J.M.2
  • 25
    • 0024076555 scopus 로고
    • Antigens recognized by monoclonal antibody to mouse acrosomal components differ in guinea pig spermatogenic cells and sperm
    • Gerton GL, O'Brien DA, Eddy EM. Antigens recognized by monoclonal antibody to mouse acrosomal components differ in guinea pig spermatogenic cells and sperm. Biol Reprod 1988; 39:431-441.
    • (1988) Biol Reprod , vol.39 , pp. 431-441
    • Gerton, G.L.1    O'Brien, D.A.2    Eddy, E.M.3
  • 26
    • 0025237448 scopus 로고
    • Preparation and short-term culture of enriched populations of guinea pig spermatocytes and spermatids
    • Joshi MS, Anakwe OO, Gerton GL. Preparation and short-term culture of enriched populations of guinea pig spermatocytes and spermatids. J Androl 1990; 11:120-130.
    • (1990) J Androl , vol.11 , pp. 120-130
    • Joshi, M.S.1    Anakwe, O.O.2    Gerton, G.L.3
  • 27
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 1976; 72:248-254.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 28
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin H, Staehelin T, Dordon J. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc Natl Acad Sci USA 1979; 76:4350-4354.
    • (1979) Proc Natl Acad Sci USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Dordon, J.3
  • 29
    • 84985708280 scopus 로고
    • The fine structure of testicular interstitial cells in guinea pigs
    • Christensen AK. The fine structure of testicular interstitial cells in guinea pigs. J Cell Biol 1965; 26:911-935.
    • (1965) J Cell Biol , vol.26 , pp. 911-935
    • Christensen, A.K.1
  • 30
    • 0024390276 scopus 로고
    • Light microscopic immunocytochemical study of fibrous sheath and outer dense fiber formation in the rat spermatid
    • Oko R, Clermont Y. Light microscopic immunocytochemical study of fibrous sheath and outer dense fiber formation in the rat spermatid. Anat Rec 1989; 225:46-55.
    • (1989) Anat Rec , vol.225 , pp. 46-55
    • Oko, R.1    Clermont, Y.2
  • 31
    • 0020132168 scopus 로고
    • Imidazole increases the sensitivity of the cytochemical reaction for peroxidase with diaminobenzidine at neutral pH
    • Straus W. Imidazole increases the sensitivity of the cytochemical reaction for peroxidase with diaminobenzidine at neutral pH. J Histochem Cytochem 1982; 30:491-493.
    • (1982) J Histochem Cytochem , vol.30 , pp. 491-493
    • Straus, W.1
  • 32
    • 0027435176 scopus 로고
    • Localization and dynamics of non filamentous actin in cultured cells
    • Cao L-G, Fishking DJ, Wang Y-L. Localization and dynamics of non filamentous actin in cultured cells. J Cell Biol 1993; 123:173-181.
    • (1993) J Cell Biol , vol.123 , pp. 173-181
    • Cao, L.-G.1    Fishking, D.J.2    Wang, Y.-L.3
  • 33
    • 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 RH, Dai N, Hoxter B. Development of Sertoli cell junctional specializations and the distribution of the tight-junction-associated protein ZO-1 in the mouse testis. Am J Anat 1991; 191:35-47.
    • (1991) Am J Anat , vol.191 , pp. 35-47
    • Byers, S.1    Graham, R.H.2    Dai, N.3    Hoxter, B.4
  • 34
    • 0024573781 scopus 로고
    • Biogenesis of podocalyxin, the major glomerular sialoglycoprotein, in the newborn rat kidney
    • Schnabel E, Dekan G, Miettinen A, Farquhar MG. Biogenesis of podocalyxin, the major glomerular sialoglycoprotein, in the newborn rat kidney. Eur J Cell Biol 1989; 48:313-326.
    • (1989) Eur J Cell Biol , vol.48 , pp. 313-326
    • Schnabel, E.1    Dekan, G.2    Miettinen, A.3    Farquhar, M.G.4
  • 35
    • 1842411011 scopus 로고
    • Expression of tight junction protein, ZO-1, in mouse embryos
    • abstract 1118 193a
    • Sheth BJ, Collins E, Fleming TP. Expression of tight junction protein, ZO-1, in mouse embryos. Mol Biol Cell 1995; 6(suppl):abstract 1118 193a.
    • (1995) Mol Biol Cell , vol.6 , Issue.SUPPL.
    • Sheth, B.J.1    Collins, E.2    Fleming, T.P.3
  • 36
    • 0000297982 scopus 로고
    • The blood-testis barrier
    • Hamilton DM, Creep RO (eds.). Washington, DC: American Physiological Society
    • Setchell B P, Waites GMH. The blood-testis barrier. In: Hamilton DM, Creep RO (eds.), Handbook of Physiology, Vol 5. Washington, DC: American Physiological Society; 1975: 143-172.
    • (1975) Handbook of Physiology , vol.5 , pp. 143-172
    • Setchell, B.P.1    Waites, G.M.H.2
  • 37
    • 0001383505 scopus 로고
    • Anatomy, vasculature, innervation and fluids of the male reproductive tract
    • Knobil E, Neill J (eds.). New York: Raven Press
    • Setchell BP, Brooks DE. Anatomy, vasculature, innervation and fluids of the male reproductive tract. In: Knobil E, Neill J (eds.), The Physiology of Reproduction. New York: Raven Press; 1988: 753-835.
    • (1988) The Physiology of Reproduction , pp. 753-835
    • Setchell, B.P.1    Brooks, D.E.2
  • 38
    • 0029799520 scopus 로고    scopus 로고
    • Functional dissociation of pericellular permeability and transepithelial electrical resistance and disruption of the apical-basolateral intramembrane diffusion barrier by expression of a mutant tight junction membrane protein
    • Balda MS, Whitney JA, Flores C, González S, Cereijido M, Matter K. Functional dissociation of pericellular 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 1996; 134:1031-1049.
    • (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
  • 39
    • 0025944756 scopus 로고
    • Distribution of actin isoforms within cells of the seminiferous epithelium of the rat testis: Evidence for a muscle form of actin in spermatids
    • Oko R, Hermo L, Hecht NB. Distribution of actin isoforms within cells of the seminiferous epithelium of the rat testis: evidence for a muscle form of actin in spermatids. Anat Rec 1991; 231:63-81.
    • (1991) Anat Rec , vol.231 , pp. 63-81
    • Oko, R.1    Hermo, L.2    Hecht, N.B.3
  • 40
    • 0021647270 scopus 로고
    • Further observations on the microfilament bundles of Sertoli cell junctional complexes
    • Suárez-Quian CA, Dym M. Further observations on the microfilament bundles of Sertoli cell junctional complexes. Ann NY Acad Sci 1984; 438:476-480.
    • (1984) Ann NY Acad Sci , vol.438 , pp. 476-480
    • Suárez-Quian, C.A.1    Dym, M.2
  • 41
    • 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
  • 42
    • 0022451875 scopus 로고
    • Effects of cytoehalasin D on occluding junctions of intestinal absorptive cells: Further evidence that the cytoskeleton may influence paracellular permeability and junctional charge selectivity
    • Madara JL, Barenberg D, Carlson S. Effects of cytoehalasin D on occluding junctions of intestinal absorptive cells: further evidence that the cytoskeleton may influence paracellular permeability and junctional charge selectivity. J Cell Biol 1986; 102:2125-2136.
    • (1986) J Cell Biol , vol.102 , pp. 2125-2136
    • Madara, J.L.1    Barenberg, D.2    Carlson, S.3
  • 44
    • 0028922237 scopus 로고
    • Epidermal growth factor induces tyrosine phosphorylation and reorganization of the tight junction protein ZO-I in A431 cells
    • Van Itallie CM, Balda MS, Anderson JM. Epidermal growth factor induces tyrosine phosphorylation and reorganization of the tight junction protein ZO-I in A431 cells. J Cell Sci 1995; 108:1735-1742.
    • (1995) J Cell Sci , vol.108 , pp. 1735-1742
    • Van Itallie, C.M.1    Balda, M.S.2    Anderson, J.M.3
  • 45
    • 0023948077 scopus 로고
    • Effects of cytokalasin D on the integrity of the Sertoli cell (blood-testis) barrier
    • Weber JE, Turner TT, Tung KSK, Russell LD. Effects of cytokalasin D on the integrity of the Sertoli cell (blood-testis) barrier. Am J Anat 1988; 182:130-147.
    • (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
  • 46
    • 0024066432 scopus 로고
    • The consequences of actin distribution at Sertoli ectoplasmic specialization sites facing spermatids after in vivo exposure of rat testis to cytokalasin D
    • Russell LD, Goh JC, Rashed RMA, Vogl AW. The consequences of actin distribution at Sertoli ectoplasmic specialization sites facing spermatids after in vivo exposure of rat testis to cytokalasin D. Biol Reprod 1988; 39:105-118.
    • (1988) Biol Reprod , vol.39 , pp. 105-118
    • Russell, L.D.1    Goh, J.C.2    Rashed, R.M.A.3    Vogl, A.W.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.