메뉴 건너뛰기




Volumn 636, Issue , 2008, Pages 74-91

Extracellular matrix and its role in spermatogenesis

Author keywords

[No Author keywords available]

Indexed keywords

ANIMAL; EXTRACELLULAR MATRIX; HUMAN; MALE; PHYSIOLOGY; REVIEW; SPERMATOGENESIS;

EID: 73949086560     PISSN: 00652598     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-0-387-09597-4_5     Document Type: Article
Times cited : (84)

References (144)
  • 1
    • 0000585726 scopus 로고
    • The cytology of the testis
    • Knobil E, Neill J, eds, Raven Press
    • de Kretser DM, Kerr JB. The cytology of the testis. In: Knobil E, Neill J, eds. The Physiology of Reproduction. Raven Press, 1988:837-932.
    • (1988) The Physiology of Reproduction , pp. 837-932
    • De Kretser, D.M.1    Kerr, J.B.2
  • 2
    • 0036788073 scopus 로고    scopus 로고
    • Cell junction dynamics in the testis: Sertoli-germ cell interactions and male contraceptive development
    • Cheng CY, Mruk DD. Cell junction dynamics in the testis: Sertoli-germ 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
  • 3
    • 3242879161 scopus 로고    scopus 로고
    • Sertoli-sertoli and sertoli-germ cell interactions and their significance in germ cell movement in the seminiferous epithelium during spermatogenesis
    • DOI 10.1210/er.2003-0022
    • Mruk DD, Cheng CY. Sertoli-Sertoli and Sertoli-germ cell interactions and their significance in germ cell movement in the seminiferous epithelium during spermatogenesis. Endocr Rev 2004;25:747-806. (Pubitemid 39362296)
    • (2004) Endocrine Reviews , vol.25 , Issue.5 , pp. 747-806
    • Mruk, D.D.1    Cheng, C.Y.2
  • 4
    • 0014884660 scopus 로고
    • Electron microscopic observations on the structural components of the blood-testis barrier
    • Fawcett DW, Leak LV, Heidger PM. Electron microscopic observations on the structural components of the blood-testis barrier. J Reprod Fertil 1970; (Suppl 10):105-122.
    • (1970) J Reprod Fertil , Issue.10 SUPPL. , pp. 105-122
    • Fawcett, D.W.1    Leak, L.V.2    Heidger, P.M.3
  • 5
    • 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
  • 6
    • 0015608073 scopus 로고
    • The fine structure of the monkey (Macaca) Sertoli cell and its role in maintaining the blood-tesis barrier
    • Dym M. The fine structure of the monkey (Macaca) Sertoli cell and its role in maintaining the blood-tesis barrier. Anat Rec 1973;175:639-656.
    • (1973) Anat Rec , vol.175 , pp. 639-656
    • Dym, M.1
  • 7
    • 0027958088 scopus 로고
    • Basement membrane regulation of sertoli cells
    • DOI 10.1210/er.15.1.102
    • Dym M. Basement membrane regulation of Sertoli cells. Endocr Rev 1994;15:102-115. (Pubitemid 24058598)
    • (1994) Endocrine Reviews , vol.15 , Issue.1 , pp. 102-115
    • Dym, M.1
  • 8
    • 4644328373 scopus 로고    scopus 로고
    • Dynamic cross-talk between cells and the extracellular matrix in the testis
    • DOI 10.1002/bies.20099
    • Siu MK, Cheng CY. Dynamic cross-talk between cells and the extracellular matrix in the testis. Bioessays 2004;26:978-992. (Pubitemid 39273071)
    • (2004) BioEssays , vol.26 , Issue.9 , pp. 978-992
    • Siu, M.K.Y.1    Cheng, C.Y.2
  • 9
    • 3242786521 scopus 로고    scopus 로고
    • Extracellular matrix: Recent advances on its role in junction dynamics in the seminiferous epithelium during spermatogenesis
    • DOI 10.1095/biolreprod.104.028225
    • Siu MK, Cheng CY. Extracellular matrix: Recent advances on its role in junction dynamics in the seminiferous epithelium during spermatogenesis. Biol Reprod 2004;71:375-391. (Pubitemid 38970510)
    • (2004) Biology of Reproduction , vol.71 , Issue.2 , pp. 375-391
    • Siu, M.K.Y.1    Cheng, C.Y.2
  • 10
    • 0023214669 scopus 로고
    • Role of immunological factors in male infertility. Immunohistochemical and serological evidence
    • Lehmann D, Temminck B, Da Rugna D et al. Role of immunological factors in male infertility. Immunohistochemical and serological evidence. Lab Invest 1987;57:21-28. (Pubitemid 17101239)
    • (1987) Laboratory Investigation , vol.57 , Issue.1 , pp. 21-28
    • Lehmann, D.1    Temminck, B.2    Da Rugna, D.3
  • 11
    • 0020421943 scopus 로고
    • Immune complex orchitis in infertile men. Immunoelectron microscopy of abnormal basement membrane structures
    • Salomon F, Saremaslani P, Jakob M et al. Immune complex orchitis in infertile men: Immunoelectron microscopy of abnormal basement membrane structures. Lab Invest 1982;47:555-567. (Pubitemid 13223528)
    • (1982) Laboratory Investigation , vol.47 , Issue.6 , pp. 555-567
    • Salomon, F.1    Saremaslani, P.2    Jakob, M.3    Hedinger, C.E.4
  • 12
    • 33747881517 scopus 로고    scopus 로고
    • Tumor necrosis factor α reversibly disrupts the blood-testis barrier and impairs Sertoli-germ cell adhesion in the seminiferous epithelium of adult rat testes
    • DOI 10.1677/joe.1.06781
    • Li MW, Xia W, Mruk DD et al. Tumor necrosis factor α reversibly disrupts the blood-testis barrier and impairs Sertoli-germ cell adhesion in the seminiferous epithelium of adult rat testes. J Endocrinol 2006;190:313-329. (Pubitemid 44288369)
    • (2006) Journal of Endocrinology , vol.190 , Issue.2 , pp. 313-329
    • Li, M.W.M.1    Xia, W.2    Mruk, D.D.3    Wang, C.Q.F.4    Yan, H.H.N.5    Siu, M.K.Y.6    Lui, W.-Y.7    Lee, W.M.8    Cheng, C.Y.9
  • 13
    • 1242281830 scopus 로고    scopus 로고
    • Interactions of Proteases, Protease Inhibitors, and the β1 Integrin/Laminin γ3 Protein Complex in the Regulation of Ectoplasmic Specialization Dynamics in the Rat Testis
    • DOI 10.1095/biolreprod.103.023606
    • Siu MK, Cheng CY. Interactions of proteases, protease inhibitors, and the β1 integrin/laminin γ3 protein complex in the regulation of ectoplasmic specialization dynamics in the rat testis. Biol Reprod 2004;70:945-964. (Pubitemid 38387703)
    • (2004) Biology of Reproduction , vol.70 , Issue.4 , pp. 945-964
    • Siu, M.K.Y.1    Cheng, C.Y.2
  • 14
    • 0037230154 scopus 로고    scopus 로고
    • The interplay of collagen IV, tumor necrosis factor-α, gelatinase B (matrix metalloprotease-9), and tissue inhibitor of metalloproteases-1 in the basal lamina regulates sertoli cell-tight junction dynamics in the rat testis
    • DOI 10.1210/en.2002-220786
    • Siu MK, Lee WM, Cheng CY. The interplay of collagen IV, tumor necrosis factor-α gelatinase B (matrix metalloprotease-9), and tissue inhibitor of metalloproteases-1 in the basal lamina regulates Sertoli cell-tight junction dynamics in the rat testis. Endocrinology 2003;144:371-387. (Pubitemid 36076127)
    • (2003) Endocrinology , vol.144 , Issue.1 , pp. 371-387
    • Siu, M.K.Y.1    Lee, W.M.2    Cheng, C.Y.3
  • 15
    • 0038070531 scopus 로고    scopus 로고
    • Adhering junction dynamics in the testis are regulated by an interplay of β1-integrin and focal adhesion complex-associated proteins
    • DOI 10.1210/en.2002-221035
    • Siu MK, Mruk DD, Lee WM et al. Adhering junction dynamics in the testis are regulated by an interplay of β1-integrin and focal adhesion complex-associated proteins. Endocrinology 2003;144:2141-2163. (Pubitemid 36543354)
    • (2003) Endocrinology , vol.144 , Issue.5 , pp. 2141-2163
    • Siu, M.K.Y.1    Mruk, D.D.2    Lee, W.M.3    Cheng, C.Y.4
  • 16
    • 21644457437 scopus 로고    scopus 로고
    • Sertoli-germ cell anchoring junction dynamics in the testis are regulated by an interplay of lipid and protein kinases
    • DOI 10.1074/jbc.M501049200
    • Siu MK, Wong CH, Lee WM et al. Sertoli-germ cell anchoring junction dynamics in the testis are regulated by an interplay of lipid and protein kinases. J Biol Chem 2005;280:25029-25047. (Pubitemid 40934595)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.26 , pp. 25029-25047
    • Siu, M.K.Y.1    Wong, C.-H.2    Lee, W.M.3    Cheng, C.Y.4
  • 17
    • 0023606109 scopus 로고
    • Immunocytochemistry of extracellular matrix in the lamina propria of the rat testis: Electron microscopic localization
    • Hadley MA, Dym M. Immunocytochemistry of extracellular matrix in the lamina propria of the rat testis: Electron microscopic localization. Biol Reprod 1987;37:1283-1289. (Pubitemid 18049208)
    • (1987) Biology of Reproduction , vol.37 , Issue.5 , pp. 1283-1289
    • Hadley, M.A.1    Dym, M.2
  • 18
    • 0026671132 scopus 로고
    • Localization and synthesis of entactin in seminiferous tubules of the mouse
    • Lian G, Miller KA, Enders GC. Localization and synthesis of entactin in seminiferous tubules of the mouse. Biol Reprod 1992;47:316-325.
    • (1992) Biol Reprod , vol.47 , pp. 316-325
    • Lian, G.1    Miller, K.A.2    Enders, G.C.3
  • 19
    • 0003152836 scopus 로고
    • Sertoli cell cytoskeleton
    • Russell L, Griswold M, eds, Cache River Press
    • Vogl A, Pfeiffer D, Redenbach D et al. Sertoli cell cytoskeleton. In: Russell L, Griswold M, eds. The Sertoli Cell. Cache River Press, 1993:39-86.
    • (1993) The Sertoli Cell , pp. 39-86
    • Vogl, A.1    Pfeiffer, D.2    Redenbach, D.3
  • 20
    • 0019314869 scopus 로고
    • A study of Sertoli-spermatid tubulobulbar complexes in selected mammals
    • DOI 10.1016/0040-8166(80)90005-1
    • Russell LD, Malone JP. A study of Sertoli-spermatid tubulobulbar complexes in selected mammals. Tissue Cell 1980;12:263-285. (Pubitemid 10016254)
    • (1980) Tissue and Cell , vol.12 , Issue.2 , pp. 263-285
    • Russell, L.D.1    Malone, J.P.2
  • 21
    • 1242321238 scopus 로고    scopus 로고
    • Non-Muscle Cofilin Is a Component of Tubulobulbar Complexes in the Testis
    • DOI 10.1095/biolreprod.103.022723
    • Guttman JA, Obinata T, Shima J et al. Non-muscle cofilin is a component of tubulobulbar complexes in the testis. Biol Reprod 2004;70:805-812. (Pubitemid 38233720)
    • (2004) Biology of Reproduction , vol.70 , Issue.3 , pp. 805-812
    • Guttman, J.A.1    Obinata, T.2    Shima, J.3    Griswold, M.4    Vogl, A.W.5
  • 22
    • 0017362507 scopus 로고
    • Desmosome like junctions between Sertoli and germ cells in the rat testis
    • Russell L. Desmosome-like junctions between Sertoli and germ cells in the rat testis. Am J Anat 1977;148:301-312. (Pubitemid 8075866)
    • (1977) American Journal of Anatomy , vol.148 , Issue.3 , pp. 301-312
    • Russell, L.1
  • 23
    • 0002042150 scopus 로고    scopus 로고
    • Cell junctions, cell adhesion, and the extracellular matrix
    • 4th ed. New York: Garland Science
    • Alberts B, Johnson A, Lewis J et al. Cell junctions, cell adhesion, and the extracellular matrix. Molecular Biology of the Cell. 4th ed. New York: Garland Science, 2002:1065-1126.
    • (2002) Molecular Biology of the Cell , pp. 1065-1126
    • Alberts, B.1    Johnson, A.2    Lewis, J.3
  • 24
    • 85056037863 scopus 로고    scopus 로고
    • The tight junctions in the testis, epididymis, and vas deferens
    • Cereijido M, Anderson J, eds, CRC Press
    • Pelletier R. The tight junctions in the testis, epididymis, and vas deferens. In: Cereijido M, Anderson J, eds. Tight Junctions. CRC Press, 2001:599-628.
    • (2001) Tight Junctions , pp. 599-628
    • Pelletier, R.1
  • 25
    • 0030087944 scopus 로고    scopus 로고
    • Supramolecular assembly of basement membranes
    • Timpl R, Brown JC. Supramolecular assembly of basement membranes. Bioessays 1996;18:123-132.
    • (1996) Bioessays , vol.18 , pp. 123-132
    • Timpl, R.1    Brown, J.C.2
  • 26
    • 0027494603 scopus 로고
    • Type IV collagen: Structure, gene organization, and role in human diseases. Molecular basis of goodpasture and alport syndromes and diffuse leiomyomatosis
    • Hudson BG, Reeders ST, Tryggvason K. Type IV collagen: Structure, gene organization, and role in human diseases: Molecular basis of Goodpasture and Alport syndromes and diffuse leiomyomatosis. J Biol Chem 1993;268:26033-26036. (Pubitemid 23361657)
    • (1993) Journal of Biological Chemistry , vol.268 , Issue.35 , pp. 26033-26036
    • Hudson, B.G.1    Reeders, S.T.2    Tryggvason, K.3
  • 27
    • 0037113093 scopus 로고    scopus 로고
    • New functional roles for non-collagenous domains of basement membrane collagens
    • DOI 10.1242/jcs.00106
    • Ortega N, Werb Z. New functional roles for non-collagenous domains of basement membrane collagens. J Cell Sci 2002;115:4201-4214. (Pubitemid 35460692)
    • (2002) Journal of Cell Science , vol.115 , Issue.22 , pp. 4201-4214
    • Ortega, N.1    Werb, Z.2
  • 29
    • 0028869213 scopus 로고
    • Developmental changes in seminiferous tubule extracellular matrix components of the mouse testis: α3 (IV) collagen chain expressed at the initiation of spermatogenesis
    • Enders GC, Kahsai TZ, Lian G et al. Developmental changes in seminiferous tubule extracellular matrix components of the mouse testis: α3 (IV) collagen chain expressed at the initiation of spermatogenesis. Biol Reprod 1995;53:1489-1499.
    • (1995) Biol Reprod , vol.53 , pp. 1489-1499
    • Enders, G.C.1    Kahsai, T.Z.2    Lian, G.3
  • 30
    • 0031878487 scopus 로고    scopus 로고
    • Differential distribution of type IV collagen chains in the developing rat testis and ovary
    • DOI 10.1007/s002580050237
    • Frojdman K, Pelliniemi LJ, Virtanen I. Differential distribution of type IV collagen chains in the developing rat testis and ovary. Differentiation 1998;63:125-130. (Pubitemid 28362376)
    • (1998) Differentiation , vol.63 , Issue.3 , pp. 125-130
    • Frojdman, K.1    Pelliniemi, L.J.2    Virtanen, I.3
  • 32
    • 0028891349 scopus 로고
    • Basement membrane gene expression by Sertoli and peritubular myoid cells in vitro in the rat
    • Richardson LL, Kleinman HK, Dym M. Basement membrane gene expression by Sertoli and peritubular myoid cells in vitro in the rat. Biol Reprod 1995;52:320-330.
    • (1995) Biol Reprod , vol.52 , pp. 320-330
    • Richardson, L.L.1    Kleinman, H.K.2    Dym, M.3
  • 33
    • 0021848539 scopus 로고
    • Cooperativity between Sertoli cells and testicular peritubular cells in the production and deposition of extracellular matrix components
    • DOI 10.1083/jcb.100.6.1941
    • Skinner MK, Tung PS, Fritz IB. Cooperativity between Sertoli cells and testicular peritubular cells in the production and deposition of extracellular matrix components. J Cell Biol 1985;100:1941-1947. (Pubitemid 15042090)
    • (1985) Journal of Cell Biology , vol.100 , Issue.6 , pp. 1941-1947
    • Skinner, M.K.1    Tung, P.S.2    Fritz, I.B.3
  • 34
    • 0037230154 scopus 로고    scopus 로고
    • The interplay of collagen IV, tumor necrosis factor-α, gelatinase B (matrix metalloprotease-9), and tissue inhibitor of metalloproteases-1 in the basal lamina regulates sertoli cell-tight junction dynamics in the rat testis
    • DOI 10.1210/en.2002-220786
    • Siu MK, Lee WM, Cheng CY. The interplay of collagen IV, tumor necrosis factor-α, gelatinase B (matrix metalloprotease-9) and tissue inhibitor of metalloproteases-1 in the basal lamina regulates Sertoli cell tight junction dynamics in the rat testis. Endocrinology 2003;144:371-387. (Pubitemid 36076127)
    • (2003) Endocrinology , vol.144 , Issue.1 , pp. 371-387
    • Siu, M.K.Y.1    Lee, W.M.2    Cheng, C.Y.3
  • 35
    • 0034733782 scopus 로고    scopus 로고
    • Modulation of tight junction structure and function by cytokines
    • DOI 10.1016/S0169-409X(00)00048-X, PII S0169409X0000048X
    • Walsh SV, Hopkins AM, Nusrat A. Modulation of tight junction structure and function by cytokines. Adv Drug Deliv Rev 2000;41:303-313. (Pubitemid 30347380)
    • (2000) Advanced Drug Delivery Reviews , vol.41 , Issue.3 , pp. 303-313
    • Walsh, S.V.1    Hopkins, A.M.2    Nusrat, A.3
  • 37
    • 0032832808 scopus 로고    scopus 로고
    • Activation of Jun. N-terminal kinase/stress-activated protein kinase pathway by tumor necrosis factor α leads to intercellular adhesion molecule-1 expression
    • De Cesaris P, Starace D, Starace G et al. Activation of Jun. N-terminal kinase/stress-activated protein kinase pathway by tumor necrosis factor α leads to intercellular adhesion molecule-1 expression. J Biol Chem 1999;274:28978-28982.
    • (1999) J Biol Chem , vol.274 , pp. 28978-28982
    • De Cesaris, P.1    Starace, D.2    Starace, G.3
  • 39
    • 1642403674 scopus 로고    scopus 로고
    • Molecular mechanism of suppression of testicular steroidogenesis by proinflammatory cytokine tumor necrosis factor alpha
    • DOI 10.1128/MCB.24.7.2593-2604.2004
    • Hong CY, Park JH, Ahn RS et al. Molecular mechanism of suppression of testicular steroidogenesis by proinflammatory cytokine tumor necrosis factor α. Mol Cell Biol 2004;24:2593-2604. (Pubitemid 38381254)
    • (2004) Molecular and Cellular Biology , vol.24 , Issue.7 , pp. 2593-2604
    • Hong, C.Y.1    Park, J.H.2    Ahn, R.S.3    Im, S.Y.4    Choi, H.-S.5    Soh, J.6    Mellon, S.H.7    Lee, K.8
  • 40
    • 0019980538 scopus 로고
    • Proliferation of Sertoli cells in fetal and postnatal rats: A quantitative autoradiographic study
    • DOI 10.1002/ar.1092030408
    • Orth JM. Proliferation of Sertoli cells in fetal and postnatal rats: A quantitative autoradiographic study. Anat Rec 1982;203:485-492. (Pubitemid 12048185)
    • (1982) Anatomical Record , vol.203 , Issue.4 , pp. 485-492
    • Orth, J.M.1
  • 41
    • 0024523008 scopus 로고
    • Determination of Sertoli cell numbers in the developing rat testis by stereological methods
    • Wang ZX, Wreford NG, de Kretser DM. Determination of Sertoli cell numbers in the developing rat testis by stereological methods. Int J Androl 1989;12:58-64. (Pubitemid 19063330)
    • (1989) International Journal of Andrology , vol.12 , Issue.1 , pp. 58-64
    • Wang, Z.X.1    Wreford, N.G.M.2    De Kretser, D.M.3
  • 42
    • 0020594215 scopus 로고
    • Three-dimensional reconstruction of a rat stage V Sertoli cell: II. Morphometry of Sertoli-Sertoli and Sertoli-germ-cell relationships
    • Weber JE, Russell LD, Wong V et al. Three-dimensional reconstruction of a rat stave V Sertoli cell. II. Morphometry of Sertoli-Sertoli and Sertoli-germ-cell relationships. Am J Anaet 1983;167:163-179. (Pubitemid 13069014)
    • (1983) American Journal of Anatomy , vol.167 , Issue.2 , pp. 163-179
    • Weber, J.E.1    Russell, L.D.2    Wong, V.3    Peterson, R.N.4
  • 43
    • 0028814944 scopus 로고
    • Apoptosis of male germ cells, a generalized or a cell type-specific phenomenon?
    • Bartke A. Apoptosis of male germ cells, a generalized or a cell type-specific phenomenon? Endocrinology 1995;136:3-4.
    • (1995) Endocrinology , vol.136 , pp. 3-4
    • Bartke, A.1
  • 44
    • 75449141332 scopus 로고
    • The cycle of the seminiferous epithelium in man
    • Clermont Y. The cycle of the seminiferous epithelium in man. Am J Anat 1963;112:35-51.
    • (1963) Am J Anat , vol.112 , pp. 35-51
    • Clermont, Y.1
  • 45
    • 0033022705 scopus 로고    scopus 로고
    • Hormonal and genetic control of germ cell apoptosis in the testis
    • DOI 10.1530/ror.0.0040038
    • Sinha Hikim AP, Swerdloff RS. Hormonal and genetic control of germ cell apoptosis in the testis. Rev Reprod 1999;4:38-47. (Pubitemid 29078543)
    • (1999) Reviews of Reproduction , vol.4 , Issue.1 , pp. 38-47
    • Hikim, A.P.S.1    Swerdloff, R.S.2
  • 46
    • 9444242676 scopus 로고    scopus 로고
    • Tumor necrosis factor-alpha (TNF-α) promotes cell survival during spermatogenesis, and this effect can be blocked by infliximab, a TNF-α antagonist
    • DOI 10.1530/eje.0.1510629
    • Suominen JS, Wang Y, Kaipia A et al. Tumor necrosis factor-α (TNFct) promotes cell survival during spermatogenesis, and this effect can be blocked by infliximab, a TNF-ct antagonist. Eur J Endocrinol 2004;151:629-640. (Pubitemid 39562519)
    • (2004) European Journal of Endocrinology , vol.151 , Issue.5 , pp. 629-640
    • Suominen, J.S.1    Wang, Y.2    Kaipia, A.3    Toppari, J.4
  • 47
    • 0026094199 scopus 로고
    • Clonal development of interconnected germ cells in the rat and its relationship to the segmental and subsegmental organization of spermatogenesis
    • Ren HP, Russell LD. Clonal development of interconnected germ cells in the rat and its relationship to the segmental and subsegmental organization of spermatogenesis. Am J Anat 1991;192:121-128.
    • (1991) Am J Anat , vol.192 , pp. 121-128
    • Ren, H.P.1    Russell, L.D.2
  • 48
    • 0001005601 scopus 로고
    • Intercellular bridges
    • Fawcett DW. Intercellular bridges. Exp Cell Res 1961;8:174-187.
    • (1961) Exp Cell Res , vol.8 , pp. 174-187
    • Fawcett, D.W.1
  • 51
    • 0031309902 scopus 로고    scopus 로고
    • The discoidin domain receptor tyrosine kinases are activated by collagen
    • Vogel W, Gish GD, Alves F et al. The discoidin domain receptor tyrosine kinases are activated by collagen. Mol Cell 1997;1:13-23. (Pubitemid 127376389)
    • (1997) Molecular Cell , vol.1 , Issue.1 , pp. 13-23
    • Vogel, W.1    Gish, G.D.2    Alves, F.3    Pawson, T.4
  • 52
    • 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. (Pubitemid 8248819)
    • (1977) Tissue and Cell , vol.9 , Issue.3 , pp. 475-498
    • Russell, L.1
  • 54
    • 0037306844 scopus 로고    scopus 로고
    • Is the cadherin/catenin complex a functional unit of cell-cell actin-based adherens junctions in the rat testis?
    • DOI 10.1095/biolreprod.102.005793
    • Lee NP, Mruk D, Lee WM et al. Is the cadherin/catenin complex a functional unit of cell-cell actin-based adherens junctions in the rat testis? Biol Reprod 2003;68:489-508. (Pubitemid 36139314)
    • (2003) Biology of Reproduction , vol.68 , Issue.2 , pp. 489-508
    • Lee, N.P.Y.1    Mruk, D.2    Lee, W.M.3    Cheng, C.Y.4
  • 56
    • 23844511497 scopus 로고    scopus 로고
    • Blood-testis barrier dynamics are regulated by an engagement/ disengagement mechanism between tight and adherens junctions via peripheral adaptors
    • DOI 10.1073/pnas.0503855102
    • Yan HH, Cheng CY. Blood-testis barrier dynamics are regulated by an engagement/disengagement mechanism between tight and adherens junctions via peripheral adaptors. Proc Natl Acad Sci USA 2005;102:11722-11727. (Pubitemid 41170793)
    • (2005) Proceedings of the National Academy of Sciences of the United States of America , vol.102 , Issue.33 , pp. 11722-11727
    • Van Helen, H.N.1    Cheng, C.Y.2
  • 57
    • 33745214011 scopus 로고    scopus 로고
    • Laminin α3 forms a complex with β3 and γ3 chains that serves as the ligand for α6β1-integrin at the apical ectoplasmic specialization in adult rat testes
    • Yan HH, Cheng CY. Laminin α3 forms a complex with β3 and γ3 chains that serves as the ligand for α6β1-integrin at the apical ectoplasmic specialization in adult rat testes. J Biol Chem 2006;281:17286-17303.
    • (2006) J Biol Chem , vol.281 , pp. 17286-17303
    • Yan, H.H.1    Cheng, C.Y.2
  • 58
    • 1842509188 scopus 로고    scopus 로고
    • Laminin: The crux of basement membrane assembly
    • DOI 10.1083/jcb.200401058
    • Sasaki T, Fassler R, Hohenester E. Laminin: The crux of basement membrane assembly. J Cell Biol 2004;164:959-963. (Pubitemid 38429121)
    • (2004) Journal of Cell Biology , vol.164 , Issue.7 , pp. 959-963
    • Sasaki, T.1    Fassler, R.2    Hohenester, E.3
  • 59
    • 11144249434 scopus 로고    scopus 로고
    • Protein kinases and adherens junction dynamics in the seminiferous epithelium of the rat testis
    • DOI 10.1002/jcp.20119
    • Lee NP, Cheng CY. Protein kinases and adherens junction dynamics in the seminiferous epithelium of the rat testis. J Cell Physiol 2005;202:344-360. (Pubitemid 40041305)
    • (2005) Journal of Cellular Physiology , vol.202 , Issue.2 , pp. 344-360
    • Lee, N.P.Y.1    Cheng, C.Y.2
  • 60
    • 14244268279 scopus 로고    scopus 로고
    • Regulation of ectoplasmic specialization dynamics in the seminiferous epithelium by focal adhesion-associated proteins in testosterone-suppressed rat testes
    • DOI 10.1210/en.2004-1275
    • Wong CH, Xia W, Lee NP et al. Regulation of ectoplasmic specialization dynamics in the seminiferous epithelium by focal adhesion-associated proteins in testosterone-suppressed rat testes. Endocrinology 2005;146:1192-1204. (Pubitemid 40289308)
    • (2005) Endocrinology , vol.146 , Issue.3 , pp. 1192-1204
    • Wong, C.-H.1    Xia, W.2    Lee, N.P.Y.3    Mruk, D.D.4    Lee, W.M.5    Cheng, C.Y.6
  • 61
    • 0026492397 scopus 로고
    • Distribution of β1 integrin subunit in rat seminiferous epithelium
    • Palombi F, Salanova M, Tarone G et al. Distribution of β1 integrin subunit in rat seminiferous epithelium. Biol Reprod 1992;47:1173-1182.
    • (1992) Biol Reprod , vol.47 , pp. 1173-1182
    • Palombi, F.1    Salanova, M.2    Tarone, G.3
  • 62
    • 0031009709 scopus 로고    scopus 로고
    • Localization of integrin β1, α1, α5 and α9 subunits in the rat testis
    • Giebel J, Loster K, Rune GM. Localization of integrin β1, α1, a5 and a9 subunits in the rat testis. Int J Androl 1997;20:3-9. (Pubitemid 27280934)
    • (1997) International Journal of Andrology , vol.20 , Issue.1 , pp. 3-9
    • Giebel, J.1    Loster, K.2    Rune, G.M.3
  • 63
    • 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 et al. Integrin receptor α6β1 is localized at specific sites of cell-to-cell contact in rat seminiferous epithelium. Biol Reprod 1995;52:79-87.
    • (1995) Biol Reprod , vol.52 , pp. 79-87
    • Salanova, M.1    Stefanini, M.2    De Curtis, I.3
  • 64
    • 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. Rat seminiferous epithelium contains a unique junction (ectoplasmic specialization) with signaling properties both of cell/cell and cell/matrix junctions. Biol Reprod 2001;64:396-407. (Pubitemid 32044651)
    • (2001) Biology of Reproduction , vol.64 , Issue.1 , pp. 396-407
    • Mulholland, D.J.1    Dedhar, S.2    Vogl, A.W.3
  • 65
    • 0028175560 scopus 로고
    • Differential distribution of the α6 subunit of integrins in the development and sexual differentiation of the mouse testis
    • Frojdman K, Pelliniemi LJ. Differential distribution of the α6 subunit of integrins in the development and sexual differentiation of the mouse testis. Differentiation 1994;57:21-29.
    • (1994) Differentiation , vol.57 , pp. 21-29
    • Frojdman, K.1    Pelliniemi, L.J.2
  • 66
    • 0036178447 scopus 로고    scopus 로고
    • Signal transduction by cell adhesion receptors and the cytoskeleton: Functions of integrins, cadherins, selectins, and immunoglobulin-superfamily members
    • DOI 10.1146/annurev.pharmtox.42.090401.151133
    • Juliano RL. Signal transduction by cell adhesion receptors and the cytoskeleton: Functions of integrins, cadherins, selectins, and immunoglobulin-superfamily members. Annu Rev Pharmacol Toxicol 2002;42:283-323. (Pubitemid 34160528)
    • (2002) Annual Review of Pharmacology and Toxicology , vol.42 , pp. 283-323
    • Juliano, R.L.1
  • 67
    • 0026093621 scopus 로고
    • Receptors for laminin on mammalian cells
    • Mecham RP. Receptors for laminin on mammalian cells. FASEB J 1991;5:2538-2546. (Pubitemid 21905803)
    • (1991) FASEB Journal , vol.5 , Issue.11 , pp. 2538-2546
    • Mecham, R.P.1
  • 70
  • 71
    • 2342472716 scopus 로고    scopus 로고
    • Focal adhesion and actin dynamics: A place where kinases and proteases meet to promote invasion
    • DOI 10.1016/j.tcb.2004.03.011, PII S0962892404000856
    • Carragher NO, Frame MC. Focal adhesion and actin dynamics: A place where kinases and proteases meet to promote invasion. Trends Cell Biol 2004;14:241-249. (Pubitemid 38591328)
    • (2004) Trends in Cell Biology , vol.14 , Issue.5 , pp. 241-249
    • Carragher, N.O.1    Frame, M.C.2
  • 72
    • 33645515261 scopus 로고    scopus 로고
    • Integrin trafficking and the control of cell migration
    • Caswell PT, Norman JC. Integrin trafficking and the control of cell migration. Traffic 2006;7:14-21.
    • (2006) Traffic , vol.7 , pp. 14-21
    • Caswell, P.T.1    Norman, J.C.2
  • 73
    • 0033519298 scopus 로고    scopus 로고
    • 3 chain: A novel, nonbasement membrane-associated, laminin chain
    • 3 chain: A novel, nonbasement membrane-associated, laminin chain. J Cell Biol 1999;145:605-618.
    • (1999) J Cell Biol , vol.145 , pp. 605-618
    • Koch, M.1    Olson, P.F.2    Albus, A.3
  • 76
    • 0035027440 scopus 로고    scopus 로고
    • Reversible inhibition of spermatogenesis in rats using a new male contraceptive, 1-(2,4-dichlorobenzyl)-indazole-3-carbohydrazide
    • Grima J, Silvestrini B, Cheng CY. Reversible inhibition of spermatogenesis in rats using a new male contraceptive, 1-(2, 4-dichlorobenzyl)-indazole-3-carbohydrazide. Biol Reprod 2001;64:1500-1508. (Pubitemid 32373073)
    • (2001) Biology of Reproduction , vol.64 , Issue.5 , pp. 1500-1508
    • Grima, J.1    Silvestrini, B.2    Yan Cheng, C.3
  • 77
    • 33750735046 scopus 로고    scopus 로고
    • A male contraceptive targeting germ cell adhesion
    • DOI 10.1038/nm1420, PII NM1420
    • Mruk DD, Wong CH, Silvestrini B et al. A male contraceptive targeting germ cell adhesion. Nat Med 2006;12:1323-1328. (Pubitemid 44706936)
    • (2006) Nature Medicine , vol.12 , Issue.11 , pp. 1323-1328
    • Mruk, D.D.1    Wong, C.-H.2    Silvestrini, B.3    Cheng, C.Y.4
  • 78
    • 0034614939 scopus 로고    scopus 로고
    • Role of cell surface metalloprotease MT1-MMP in epithelial cell migration over laminin-5
    • Koshikawa N, Giannelli G, Cirulli V et al. Role of cell surface metalloprotease MT1-MMP in epithelial cell migration over laminin-5. J Cell Biol 2000;148:615-624.
    • (2000) J Cell Biol , vol.148 , pp. 615-624
    • Koshikawa, N.1    Giannelli, G.2    Cirulli, V.3
  • 79
    • 0038713422 scopus 로고    scopus 로고
    • Membrane type-1-matrix metalloproteinase expressed by prostate carcinoma cells cleaves human laminin-5 β3 chain and induces cell migration
    • Udayakumar TS, Chen ML, Bair EL et al. Membrane type-1-matrix metalloproteinase expressed by prostate carcinoma cells cleaves human laminin-5 beta3 chain and induces cell migration. Cancer Res 2003;63:2292-2299. (Pubitemid 36538639)
    • (2003) Cancer Research , vol.63 , Issue.9 , pp. 2292-2299
    • Udayakumar, T.S.1    Chen, M.L.2    Bair, E.L.3    Von Bredow, D.C.4    Cress, A.E.5    Nagle, R.B.6    Bowden, G.T.7
  • 80
  • 82
    • 1242281830 scopus 로고    scopus 로고
    • Interactions of Proteases, Protease Inhibitors, and the β1 Integrin/Laminin γ3 Protein Complex in the Regulation of Ectoplasmic Specialization Dynamics in the Rat Testis
    • DOI 10.1095/biolreprod.103.023606
    • Siu MK, Cheng CY. Interactions of proteases, protease inhibitors, and the β1 integrin/laminin γ3 protein complex in the regulation of ectoplasmic specialization dynamics in the rat testis. Biol Reprod 2004;70:945-964. (Pubitemid 38387703)
    • (2004) Biology of Reproduction , vol.70 , Issue.4 , pp. 945-964
    • Siu, M.K.Y.1    Cheng, C.Y.2
  • 83
    • 0032932582 scopus 로고    scopus 로고
    • Adhesion and signaling proteins spatiotemporally associated with spermiation in the rat
    • Wine RN, Chapin RE. Adhesion and signaling proteins spatiotemporally associated with spermiation in the rat. J Androl 1999;20:198-213. (Pubitemid 29203350)
    • (1999) Journal of Andrology , vol.20 , Issue.2 , pp. 198-213
    • Wine, R.N.1    Chapin, R.E.2
  • 85
    • 0036473058 scopus 로고    scopus 로고
    • Gelsolin - Evidence for a role in turnover of junction-related actin filaments in Sertoli cells
    • Guttman JA, Janmey P, Vogl AW. Gelsolin-evidence for a role in turnover of junction-related actin filaments in Sertoli cells. J Cell Sci 2002;115:499-505. (Pubitemid 34182977)
    • (2002) Journal of Cell Science , vol.115 , Issue.3 , pp. 499-505
    • Guttman, J.A.1    Janmey, P.2    Vogl, A.W.3
  • 86
    • 0036136374 scopus 로고    scopus 로고
    • Fyn tyrosine kinase in sertoli cells is involved in mouse spermatogenesis
    • Maekawa M, Toyama Y, Yasuda M et al. Fyn tyrosine kinase in Sertoli cells is involved in mouse spermatogenesis. Biol Reprod 2002;66:211-221. (Pubitemid 34020606)
    • (2002) Biology of Reproduction , vol.66 , Issue.1 , pp. 211-221
    • Maekawa, M.1    Toyama, Y.2    Yasuda, M.3    Yagi, T.4    Yuasa, S.5
  • 87
    • 29044447052 scopus 로고    scopus 로고
    • Mechanisms of focal adhesion kinase regulation
    • Cohen LA, Guan JL. Mechanisms of focal adhesion kinase regulation. Curr Cancer Drug Targets 2005;5:629-643. (Pubitemid 41789601)
    • (2005) Current Cancer Drug Targets , vol.5 , Issue.8 , pp. 629-643
    • Cohen, L.A.1    Guan, J.-L.2
  • 89
    • 0037509990 scopus 로고    scopus 로고
    • Focal adhesion kinase: The first ten years
    • DOI 10.1242/jcs.00373
    • Parsons JT. Focal adhesion kinase: The first ten years. J Cell Sci 2003;116:1409-1416. (Pubitemid 36527488)
    • (2003) Journal of Cell Science , vol.116 , Issue.8 , pp. 1409-1416
    • Parsons, J.T.1
  • 91
    • 0036251947 scopus 로고    scopus 로고
    • Signaling adaptor protein v-Crk activates Rho and regulates cell motility in 3Y1 rat fibroblast cell line
    • Tsuda M, Tanaka S, Sawa H et al. Signaling adaptor protein v-Crk activates Rho and regulates cell motility in 3Y1 rat fibroblast cell line. Cell Growth Differ 2002;13:131-139. (Pubitemid 34507103)
    • (2002) Cell Growth and Differentiation , vol.13 , Issue.3 , pp. 131-139
    • Tsuda, M.1    Tanaka, S.2    Sawa, H.3    Hanafusa, H.4    Nagashima, K.5
  • 93
  • 94
    • 0035920134 scopus 로고    scopus 로고
    • Laminin-10/11 and fibronectin differentially regulated integrin-dependent Rho and Rac activation via p130-CrkII-DOCK180 pathway
    • Gu J, Sumida Y, Sanzen N et al. Laminin-10/11 and fibronectin differentially regulated integrin-dependent Rho and Rac activation via p130-CrkII-DOCK180 pathway. J Biol Chem 2001;276:27090-27097.
    • (2001) J Biol Chem , vol.276 , pp. 27090-27097
    • Gu, J.1    Sumida, Y.2    Sanzen, N.3
  • 96
    • 19044391626 scopus 로고    scopus 로고
    • TGF-β3 regulates anchoring junction dynamics in the seminiferous epithelium of the rat testis via the Ras/ERK signaling pathway: An in vivo study
    • DOI 10.1016/j.ydbio.2004.12.036, PII S0012160605000345
    • Xia W, Cheng CY. TGF-β3 regulates anchoring junction dynamics in the seminiferous epithelium of the rat testis via the Ras/ERK signaling pathway: An in vivo study. Dev Biol 2005;280:321-343. (Pubitemid 40692135)
    • (2005) Developmental Biology , vol.280 , Issue.2 , pp. 321-343
    • Xia, W.1    Cheng, C.Y.2
  • 97
    • 33947720531 scopus 로고    scopus 로고
    • Coxsackie and adenovirus receptor (CAR) is a product of Sertoli and germ cells in rat testes which is localized at the Sertoli-Sertoli and Sertoli-germ cell interface
    • DOI 10.1016/j.yexcr.2007.01.017, PII S0014482707000468
    • Wang CQ, Mruk DD, Lee WM et al. Coxsackie and adenovirus receptor (CAR) is a product of Sertoli and germ cells in rat testes which is localized at the Sertoli-Sertoli and Sertoli-germ cell interface. Exp Cell Res 2007;313:1373-1392. (Pubitemid 46507447)
    • (2007) Experimental Cell Research , vol.313 , Issue.7 , pp. 1373-1392
    • Wang, C.Q.F.1    Mruk, D.D.2    Lee, W.M.3    Cheng, C.Y.4
  • 98
    • 33646153988 scopus 로고    scopus 로고
    • The coxsackie-and adenovirus receptor (CAR) is an in vivo marker for epithelial tight junctions, with a potential role in regulating permeability and tissue homeostasis
    • Raschperger E, Thyberg J, Pettersson S et al. The coxsackie-and adenovirus receptor (CAR) is an in vivo marker for epithelial tight junctions, with a potential role in regulating permeability and tissue homeostasis. Exp Cell Res 2006;312:1566-1580.
    • (2006) Exp Cell Res , vol.312 , pp. 1566-1580
    • Raschperger, E.1    Thyberg, J.2    Pettersson, S.3
  • 99
    • 33644895026 scopus 로고    scopus 로고
    • Coxsackievirus and adenovirus receptor (CAR) is expressed in male germ cells and forms a complex with the differentiation factor JAM-C in mouse testis
    • Mirza M, Hreinsson J, Strand ML et al. Coxsackievirus and adenovirus receptor (CAR) is expressed in male germ cells and forms a complex with the differentiation factor JAM-C in mouse testis. Exp Cell Res 2006;312:817-830.
    • (2006) Exp Cell Res , vol.312 , pp. 817-830
    • Mirza, M.1    Hreinsson, J.2    Strand, M.L.3
  • 100
    • 4644307425 scopus 로고    scopus 로고
    • Spermatid differentiation requires the assembly of a cell polarity complex downstream of junctional adhesion molecule-C
    • DOI 10.1038/nature02877
    • Gliki G, Ebnet K, Aurrand-Lions M et al. Spermatid differentiation requires the assembly of a cell polarity complex downstream of junctional adhesion molecule-C. Nature 2004;320-324. (Pubitemid 39265668)
    • (2004) Nature , vol.431 , Issue.7006 , pp. 320-324
    • Gliki, G.1    Ebnet, K.2    Aurrand-Lions, M.3    Imhof, B.A.4    Adams, R.H.5
  • 101
    • 33745214011 scopus 로고    scopus 로고
    • Laminin α3 forms a complex with β3 and γ3 chains that serves as the ligand for α6β1-integrin at the apical ectoplasmic specialization in adult rat testes
    • Yan HH, Cheng CY. Laminin α3 forms a complex with β3 and γ3 chains that serves as the ligand for α6β1-integrin at the apical ectoplasmic specialization in adult rat testes. J Biol Chem 2006;281:17286-17303.
    • (2006) J Biol Chem , vol.281 , pp. 17286-17303
    • Yan, H.H.1    Cheng, C.Y.2
  • 102
    • 1842509188 scopus 로고    scopus 로고
    • Laminin: The crux of basement membrane assembly
    • DOI 10.1083/jcb.200401058
    • Sasaki T, Fassler R, Hohenester E. Laminin: The crux of basement membrane assembly. J Cell Biol 2004;164:959-963. (Pubitemid 38429121)
    • (2004) Journal of Cell Biology , vol.164 , Issue.7 , pp. 959-963
    • Sasaki, T.1    Fassler, R.2    Hohenester, E.3
  • 103
    • 11144249434 scopus 로고    scopus 로고
    • Protein kinases and adherens junction dynamics in the seminiferous epithelium of the rat testis
    • DOI 10.1002/jcp.20119
    • Lee NP, Cheng CY. Protein kinases and adherens junction dynamics in the seminiferous epithelium of the rat testis. J Cell Physiol 2005;202:344-360. (Pubitemid 40041305)
    • (2005) Journal of Cellular Physiology , vol.202 , Issue.2 , pp. 344-360
    • Lee, N.P.Y.1    Cheng, C.Y.2
  • 104
    • 14244268279 scopus 로고    scopus 로고
    • Regulation of ectoplasmic specialization dynamics in the seminiferous epithelium by focal adhesion-associated proteins in testosterone-suppressed rat testes
    • DOI 10.1210/en.2004-1275
    • Wong CH, Xia W, Lee NP et al. Regulation of ectoplasmic specialization dynamics in the seminiferous epithelium by focal adhesion-associated proteins in testosterone-suppressed rat testes. Endocrinology 2005;146:1192-1204. (Pubitemid 40289308)
    • (2005) Endocrinology , vol.146 , Issue.3 , pp. 1192-1204
    • Wong, C.-H.1    Xia, W.2    Lee, N.P.Y.3    Mruk, D.D.4    Lee, W.M.5    Cheng, C.Y.6
  • 105
    • 0026492397 scopus 로고
    • Distribution of β1 integrin subunit in rat seminiferous epithelium
    • Palombi F, Salanova M, Tarone G et al. Distribution of β1 integrin subunit in rat seminiferous epithelium. Biol Reprod 1992;47:1173-1182.
    • (1992) Biol Reprod , vol.47 , pp. 1173-1182
    • Palombi, F.1    Salanova, M.2    Tarone, G.3
  • 106
    • 0031009709 scopus 로고    scopus 로고
    • Localization of integrin β1, α1, α5 and α9 subunits in the rat testis
    • Giebel J, Loster K, Rune GM. Localization of integrin β1, α1, α5 and α9 subunits in the rat testis. Int J Androl 1997;20:3-9. (Pubitemid 27280934)
    • (1997) International Journal of Andrology , vol.20 , Issue.1 , pp. 3-9
    • Giebel, J.1    Loster, K.2    Rune, G.M.3
  • 107
    • 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 et al. Integrin receptor α6β1 is localized at specific sites of cell-to-cell contact in rat seminiferous epithelium. Biol Reprod 1995;52:79-87.
    • (1995) Biol Reprod , vol.52 , pp. 79-87
    • Salanova, M.1    Stefanini, M.2    De Curtis, I.3
  • 108
    • 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. Rat seminiferous epithelium contains a unique junction (ectoplasmic specialization) with signaling properties both of cell/cell and cell/matrix junctions. Biol Reprod 2001;64:396-407. (Pubitemid 32044651)
    • (2001) Biology of Reproduction , vol.64 , Issue.1 , pp. 396-407
    • Mulholland, D.J.1    Dedhar, S.2    Vogl, A.W.3
  • 109
    • 0028175560 scopus 로고
    • Differential distribution of the α6 subunit of integrins in the development and sexual differentiation of the mouse testis
    • Frojdman K, Pelliniemi LJ. Differential distribution of the α6 subunit of integrins in the development and sexual differentiation of the mouse testis. Differentiation 1994;57:21-29.
    • (1994) Differentiation , vol.57 , pp. 21-29
    • Frojdman, K.1    Pelliniemi, L.J.2
  • 110
    • 0036178447 scopus 로고    scopus 로고
    • Signal transduction by cell adhesion receptors and the cytoskeleton: Functions of integrins, cadherins, selectins, and immunoglobulin-superfamily members
    • DOI 10.1146/annurev.pharmtox.42.090401.151133
    • Juliano RL. Signal transduction by cell adhesion receptors and the cytoskeleton: Functions of integrins, cadherins, selectins, and immunoglobulin-superfamily members. Annu Rev Pharmacol Toxicol 2002;42:283-323. (Pubitemid 34160528)
    • (2002) Annual Review of Pharmacology and Toxicology , vol.42 , pp. 283-323
    • Juliano, R.L.1
  • 111
    • 0026093621 scopus 로고
    • Receptors for laminin on mammalian cells
    • Mecham RP. Receptors for laminin on mammalian cells. FASEB J 1991;5:2538-2546. (Pubitemid 21905803)
    • (1991) FASEB Journal , vol.5 , Issue.11 , pp. 2538-2546
    • Mecham, R.P.1
  • 114
  • 115
    • 2342472716 scopus 로고    scopus 로고
    • Focal adhesion and actin dynamics: A place where kinases and proteases meet to promote invasion
    • DOI 10.1016/j.tcb.2004.03.011, PII S0962892404000856
    • Carragher NO, Frame MC. Focal adhesion and actin dynamics: A place where kinases and proteases meet to promote invasion. Trends Cell Biol 2004;14:241-249. (Pubitemid 38591328)
    • (2004) Trends in Cell Biology , vol.14 , Issue.5 , pp. 241-249
    • Carragher, N.O.1    Frame, M.C.2
  • 116
    • 33645515261 scopus 로고    scopus 로고
    • Integrin trafficking and the control of cell migration
    • Caswell PT, Norman JC. Integrin trafficking and the control of cell migration. Traffic 2006;7:14-21.
    • (2006) Traffic , vol.7 , pp. 14-21
    • Caswell, P.T.1    Norman, J.C.2
  • 117
    • 0033519298 scopus 로고    scopus 로고
    • Characterization and expression of the laminin γ3 chain: A novel, nonbasement membrane-associated, laminin chain
    • Koch M, Olson PF, Albus A et al. Characterization and expression of the laminin γ3 chain: A novel, nonbasement membrane-associated, laminin chain. J Cell Biol 1999;145:605-618.
    • (1999) J Cell Biol , vol.145 , pp. 605-618
    • Koch, M.1    Olson, P.F.2    Albus, A.3
  • 120
    • 0035027440 scopus 로고    scopus 로고
    • Reversible inhibition of spermatogenesis in rats using a new male contraceptive, 1-(2,4-dichlorobenzyl)-indazole-3-carbohydrazide
    • Grima J, Silvestrini B, Cheng CY. Reversible inhibition of spermatogenesis in rats using a new male contraceptive, 1-(2, 4-dichlorobenzyl)-indazole-3-carbohydrazide. Biol Reprod 2001;64:1500-1508. (Pubitemid 32373073)
    • (2001) Biology of Reproduction , vol.64 , Issue.5 , pp. 1500-1508
    • Grima, J.1    Silvestrini, B.2    Yan Cheng, C.3
  • 121
    • 33750735046 scopus 로고    scopus 로고
    • A male contraceptive targeting germ cell adhesion
    • DOI 10.1038/nm1420, PII NM1420
    • Mruk DD, Wong CH, Silvestrini B et al. A male contraceptive targeting germ cell adhesion. Nat Med 2006;12:1323-1328. (Pubitemid 44706936)
    • (2006) Nature Medicine , vol.12 , Issue.11 , pp. 1323-1328
    • Mruk, D.D.1    Wong, C.-H.2    Silvestrini, B.3    Cheng, C.Y.4
  • 122
    • 0034614939 scopus 로고    scopus 로고
    • Role of cell surface metalloprotease MT1-MMP in epithelial cell migration over laminin-5
    • Koshikawa N, Giannelli G, Cirulli V et al. Role of cell surface metalloprotease MT1-MMP in epithelial cell migration over laminin-5. J Cell Biol 2000;148:615-624.
    • (2000) J Cell Biol , vol.148 , pp. 615-624
    • Koshikawa, N.1    Giannelli, G.2    Cirulli, V.3
  • 123
    • 0038713422 scopus 로고    scopus 로고
    • Membrane type-1-matrix metalloproteinase expressed by prostate carcinoma cells cleaves human laminin-5 β3 chain and induces cell migration
    • Udayakumar TS, Chen ML, Bair EL et al. Membrane type-1-matrix metalloproteinase expressed by prostate carcinoma cells cleaves human laminin-5 beta3 chain and induces cell migration. Cancer Res 2003;63:2292-2299. (Pubitemid 36538639)
    • (2003) Cancer Research , vol.63 , Issue.9 , pp. 2292-2299
    • Udayakumar, T.S.1    Chen, M.L.2    Bair, E.L.3    Von Bredow, D.C.4    Cress, A.E.5    Nagle, R.B.6    Bowden, G.T.7
  • 124
  • 126
    • 1242281830 scopus 로고    scopus 로고
    • Interactions of Proteases, Protease Inhibitors, and the β1 Integrin/Laminin γ3 Protein Complex in the Regulation of Ectoplasmic Specialization Dynamics in the Rat Testis
    • DOI 10.1095/biolreprod.103.023606
    • Siu MK, Cheng CY. Interactions of proteases, protease inhibitors, and the β1 integrin/laminin γ3 protein complex in the regulation of ectoplasmic specialization dynamics in the rat testis. Biol Reprod 2004;70:945-964. (Pubitemid 38387703)
    • (2004) Biology of Reproduction , vol.70 , Issue.4 , pp. 945-964
    • Siu, M.K.Y.1    Cheng, C.Y.2
  • 127
    • 0032932582 scopus 로고    scopus 로고
    • Adhesion and signaling proteins spatiotemporally associated with spermiation in the rat
    • Wine RN, Chapin RE. Adhesion and signaling proteins spatiotemporally associated with spermiation in the rat. J Androl 1999;20:198-213. (Pubitemid 29203350)
    • (1999) Journal of Andrology , vol.20 , Issue.2 , pp. 198-213
    • Wine, R.N.1    Chapin, R.E.2
  • 129
    • 0036473058 scopus 로고    scopus 로고
    • Gelsolin - Evidence for a role in turnover of junction-related actin filaments in Sertoli cells
    • Guttman JA, Janmey P, Vogl AW. Gelsolin-Evidence for a role in turnover of junction-related actin filaments in Sertoli cells. J Cell Sci 2002;115:499-505. (Pubitemid 34182977)
    • (2002) Journal of Cell Science , vol.115 , Issue.3 , pp. 499-505
    • Guttman, J.A.1    Janmey, P.2    Vogl, A.W.3
  • 130
    • 0036136374 scopus 로고    scopus 로고
    • Fyn tyrosine kinase in sertoli cells is involved in mouse spermatogenesis
    • Maekawa M, Toyama Y, Yasuda M et al. Fyn tyrosine kinase in Sertoli cells is involved in mouse spermatogenesis. Biol Reprod 2002;66:211-221. (Pubitemid 34020606)
    • (2002) Biology of Reproduction , vol.66 , Issue.1 , pp. 211-221
    • Maekawa, M.1    Toyama, Y.2    Yasuda, M.3    Yagi, T.4    Yuasa, S.5
  • 131
    • 29044447052 scopus 로고    scopus 로고
    • Mechanisms of focal adhesion kinase regulation
    • Cohen LA, Guan JL. Mechanisms of focal adhesion kinase regulation. Curr Cancer Drug Targets 2005;5:629-643. (Pubitemid 41789601)
    • (2005) Current Cancer Drug Targets , vol.5 , Issue.8 , pp. 629-643
    • Cohen, L.A.1    Guan, J.-L.2
  • 133
    • 0037509990 scopus 로고    scopus 로고
    • Focal adhesion kinase: The first ten years
    • DOI 10.1242/jcs.00373
    • Parsons JT. Focal adhesion kinase: The first ten years. J Cell Sci 2003;116:1409-1416. (Pubitemid 36527488)
    • (2003) Journal of Cell Science , vol.116 , Issue.8 , pp. 1409-1416
    • Parsons, J.T.1
  • 135
    • 0036251947 scopus 로고    scopus 로고
    • Signaling adaptor protein v-Crk activates Rho and regulates cell motility in 3Y1 rat fibroblast cell line
    • Tsuda M, Tanaka S, Sawa H et al. Signaling adaptor protein v-Crk activates Rho and regulates cell motility in 3Y1 rat fibroblast cell line. Cell Growth Differ 2002;13:131-139. (Pubitemid 34507103)
    • (2002) Cell Growth and Differentiation , vol.13 , Issue.3 , pp. 131-139
    • Tsuda, M.1    Tanaka, S.2    Sawa, H.3    Hanafusa, H.4    Nagashima, K.5
  • 137
  • 140
    • 19044391626 scopus 로고    scopus 로고
    • TGF-β3 regulates anchoring junction dynamics in the seminiferous epithelium of the rat testis via the Ras/ERK signaling pathway: An in vivo study
    • DOI 10.1016/j.ydbio.2004.12.036, PII S0012160605000345
    • Xia W, Cheng CY. TGF-β3 regulates anchoring junction dynamics in the seminiferous epithelium of the rat testis via the Ras/ERK signaling pathway: An in vivo study. Dev Biol 2005;280:321-343. (Pubitemid 40692135)
    • (2005) Developmental Biology , vol.280 , Issue.2 , pp. 321-343
    • Xia, W.1    Cheng, C.Y.2
  • 141
    • 33947720531 scopus 로고    scopus 로고
    • Coxsackie and adenovirus receptor (CAR) is a product of Sertoli and germ cells in rat testes which is localized at the Sertoli-Sertoli and Sertoli-germ cell interface
    • DOI 10.1016/j.yexcr.2007.01.017, PII S0014482707000468
    • Wang CQ, Mruk DD, Lee WM et al. Coxsackie and adenovirus receptor (CAR) is a product of Sertoli and germ cells in rat testes which is localized at the Sertoli-Sertoli and Sertoli-germ cell interface. Exp Cell Res 2007;313:1373-1392. (Pubitemid 46507447)
    • (2007) Experimental Cell Research , vol.313 , Issue.7 , pp. 1373-1392
    • Wang, C.Q.F.1    Mruk, D.D.2    Lee, W.M.3    Cheng, C.Y.4
  • 142
    • 33646153988 scopus 로고    scopus 로고
    • The coxsackie-and adenovirus receptor (CAR) is an in vivo marker for epithelial tight junctions, with a potential role in regulating permeability and tissue homeostasis
    • Raschperger E, Thyberg J, Pettersson S et al. The coxsackie-and adenovirus receptor (CAR) is an in vivo marker for epithelial tight junctions, with a potential role in regulating permeability and tissue homeostasis. Exp Cell Res 2006;312:1566-1580.
    • (2006) Exp Cell Res , vol.312 , pp. 1566-1580
    • Raschperger, E.1    Thyberg, J.2    Pettersson, S.3
  • 143
    • 33644895026 scopus 로고    scopus 로고
    • Coxsackievirus and adenovirus receptor (CAR) is expressed in male germ cells and forms a complex with the differentiation factor JAM-C in mouse testis
    • Mirza M, Hreinsson J, Strand ML et al. Coxsackievirus and adenovirus receptor (CAR) is expressed in male germ cells and forms a complex with the differentiation factor JAM-C in mouse testis. Exp Cell Res 2006;312:817-830.
    • (2006) Exp Cell Res , vol.312 , pp. 817-830
    • Mirza, M.1    Hreinsson, J.2    Strand, M.L.3
  • 144
    • 4644307425 scopus 로고    scopus 로고
    • Spermatid differentiation requires the assembly of a cell polarity complex downstream of junctional adhesion molecule-C
    • DOI 10.1038/nature02877
    • Gliki G, Ebnet K, Aurrand-Lions M et al. Spermatid differentiation requires the assembly of a cell polarity complex downstream of junctional adhesion molecule-C. Nature 2004;320-324. (Pubitemid 39265668)
    • (2004) Nature , vol.431 , Issue.7006 , pp. 320-324
    • Gliki, G.1    Ebnet, K.2    Aurrand-Lions, M.3    Imhof, B.A.4    Adams, R.H.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.