메뉴 건너뛰기




Volumn 636, Issue , 2008, Pages 133-153

Proteases and their cognate inhibitors of the serine and metalloprotease subclasses, in testicular physiology

Author keywords

[No Author keywords available]

Indexed keywords

PEPTIDE HYDROLASE; SERINE PROTEINASE INHIBITOR;

EID: 73949136343     PISSN: 00652598     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-0-387-09597-4_8     Document Type: Article
Times cited : (11)

References (183)
  • 1
    • 0019119141 scopus 로고
    • Sertoli-germ cell interrelations: A review
    • Russell LD. Sertoli-germ cell interrelations: A review. Gamete Res 1980;3:79-202.
    • (1980) Gamete Res , vol.3 , pp. 79-202
    • Russell, L.D.1
  • 2
    • 0002034792 scopus 로고
    • Paracrine mechanisms in testicular control
    • de Kretser DM, ed, San Diego: Academic Press
    • Jegou B, Sharpe RM. Paracrine mechanisms in testicular control. In: de Kretser DM, ed. Molecular Biology of the Male Reproductive System. San Diego: Academic Press, 1993:271-310.
    • (1993) Molecular Biology of the Male Reproductive System , pp. 271-310
    • Jegou, B.1    Sharpe, R.M.2
  • 4
    • 0032130527 scopus 로고    scopus 로고
    • The central role of Sertoli cells in spermatogenesis
    • Griswold MD. The central role of Sertoli cells seminiferous epithelium. Semin Cell Dev Biol 1998;9:411-416. (Pubitemid 128350667)
    • (1998) Seminars in Cell and Developmental Biology , vol.9 , Issue.4 , pp. 411-416
    • Griswold, M.D.1
  • 6
    • 0033118412 scopus 로고    scopus 로고
    • Mammalian sex determination: A molecular drama
    • Swain A, Lovell-Badge R. Mammalian sex determination: A molecular drama. Genes Dev 1999;13:755-767. (Pubitemid 29169835)
    • (1999) Genes and Development , vol.13 , Issue.7 , pp. 755-767
    • Swain, A.1    Lovell-Badge, R.2
  • 8
    • 0036366240 scopus 로고    scopus 로고
    • The battle of the sexes: Opposing pathways in sex determination
    • Chadwick D, Goode J, eds, London: Novartis Foundation
    • Yao HH, Tilmann C, Zhao GO et al. The battle of the sexes: Opposing pathways in sex determination. In: Chadwick D, Goode J, eds. Symposium on the Genetics and Biology of Sex Determination. London: Novartis Foundation, 2002:187-198.
    • (2002) Symposium on the Genetics and Biology of Sex Determination , pp. 187-198
    • Yao, H.H.1    Tilmann, C.2    Zhao, G.O.3
  • 9
    • 3042762359 scopus 로고    scopus 로고
    • One tissue, two fates: Molecular genetic events that underlie testis versus ovary development
    • DOI 10.1038/nrg1381
    • Brennan J, Capel B. One tissue, two fates: Molecular genetic events that underlie testis versus ovary development. Nat Rev Genet 2004;5(7):509-521. (Pubitemid 38868507)
    • (2004) Nature Reviews Genetics , vol.5 , Issue.7 , pp. 509-521
    • Brennan, J.1    Capel, B.2
  • 10
    • 20644451615 scopus 로고    scopus 로고
    • Sex determination: A tale of two Sox genes
    • DOI 10.1016/j.tig.2005.05.006, PII S0168952505001368
    • Koopman P. Sex determination: A tale of two Sox genes. Trends Genet 2005;21(7):367-370. (Pubitemid 40835718)
    • (2005) Trends in Genetics , vol.21 , Issue.7 , pp. 367-370
    • Koopman, P.1
  • 13
    • 0038339998 scopus 로고    scopus 로고
    • Differential expression of tissue inhibitor of metalloproteinases type 1 (TIMP-1) during mouse gonad development
    • DOI 10.1002/dvdy.10321
    • Guyot R, Magre S, Leduque P et al. Differential expression of tissue inhibitor of metalloproteinases type 1(TIMP-1) during mouse gonad development. Dev Dyn 2003;227 (3):357-366. (Pubitemid 36828756)
    • (2003) Developmental Dynamics , vol.227 , Issue.3 , pp. 357-366
    • Guyot, R.1    Magre, S.2    Leduque, P.3    Le Magueresse-Battistoni, B.4
  • 14
    • 0000888012 scopus 로고
    • Proteases and antiproteases in the seminiferous tubules
    • Russell LD, Griswold MD, eds, Clearwater: Cache River Press
    • Fritz IB, Tung PS, Ailenberg M. Proteases and antiproteases in the seminiferous tubules. In: Russell LD, Griswold MD, eds. The Sertoli Cell. Clearwater: Cache River Press, 1993:217-235.
    • (1993) The Sertoli Cell , pp. 217-235
    • Fritz, I.B.1    Tung, P.S.2    Ailenberg, M.3
  • 15
    • 27144550666 scopus 로고    scopus 로고
    • Proteases and protease inhibitors
    • Skinner MK, Griswold MD, eds, London: Elsevier Academic Press
    • Charron M, Wright WW. Proteases and protease inhibitors. In: Skinner MK, Griswold MD, eds. Sertoli Cell Biology. London: Elsevier Academic Press, 2005:121-152.
    • (2005) Sertoli Cell Biology , pp. 121-152
    • Charron, M.1    Wright, W.W.2
  • 16
    • 33645918999 scopus 로고    scopus 로고
    • The blood-testis barrier: Its biology, regulation, and physiological role in spermatogenesis
    • DOI 10.1016/S0070-2153(05)71008-5, PII S0070215305710085
    • Wong CH, Cheng CY. The blood-testis barrier: Its biology, regulation, and physiological role in spermatogenesis. Curr Top Dev Biol 2005;71:263-296. (Pubitemid 43588888)
    • (2005) Current Topics in Developmental Biology , vol.71 , pp. 263-296
    • Wong, C.1    Cheng, C.Y.2
  • 18
    • 0033848986 scopus 로고    scopus 로고
    • Matrix metalloproteinases: Effectors of development and normal physiology
    • Vu TH, Werb Z. Matrix metalloproteinases: Effectors of development and normal physiology. Genes Dev 2000;14(17):2123-2133.
    • (2000) Genes Dev , vol.14 , Issue.17 , pp. 2123-2133
    • Vu, T.H.1    Werb, Z.2
  • 20
    • 0347445722 scopus 로고    scopus 로고
    • A genomic analysis of rat proteases and protease inhibitors
    • DOI 10.1101/gr.1946304
    • Puente XS, Lopez-Otin C. A genomic analysis of rat proteases and protease inhibitors. Genome Res 2004;4(4):609-622. (Pubitemid 38500232)
    • (2004) Genome Research , vol.14 , Issue.4 , pp. 609-622
    • Puente, X.S.1    Lopez-Otin, C.2
  • 21
    • 0041352075 scopus 로고    scopus 로고
    • The matrix metalloproteinase system: Changes, regulation, and impact throughout the ovarian and uterine reproductive cycle
    • DOI 10.1210/er.2002-0005
    • Curry T E J, Osteen KG. The matrix metalloproteinase system: Changes, regulation, and impact throughout the ovarian and uterine reproductive cycle. Endocr Rev 2003;24(4):428-465. (Pubitemid 37056240)
    • (2003) Endocrine Reviews , vol.24 , Issue.4 , pp. 428-465
    • Curry Jr., T.E.1    Osteen, K.G.2
  • 22
    • 15244344671 scopus 로고    scopus 로고
    • EMMPRIN/CD147, an MMP modulator in cancer, development and tissue repair
    • DOI 10.1016/j.biochi.2004.09.023
    • Gabison EE, Hoang-Xuan T, Mauviel A et al. EMMPRIN/CD147, an MMP modulator in cancer, development and tissue repair. Biochimie 2005;87(3-4):361-368. (Pubitemid 40387615)
    • (2005) Biochimie , vol.87 , Issue.3-4 SPEC. ISS. , pp. 361-368
    • Gabison, E.E.1    Hoang-Xuan, T.2    Mauviel, A.3    Menashi, S.4
  • 23
    • 0034141195 scopus 로고    scopus 로고
    • The ADAM gene family: Surface proteins with adhesion and protease activity
    • DOI 10.1016/S0168-9525(99)01926-5, PII S0168952599019265
    • Primakoff P, Myles DG. The ADAM gene family: Surface proteins with adhesion and protease activity. Trends Genet 2000;6(2):83-87. (Pubitemid 30084721)
    • (2000) Trends in Genetics , vol.16 , Issue.2 , pp. 83-87
    • Primakoff, P.1    Myles, D.G.2
  • 24
    • 4143112912 scopus 로고    scopus 로고
    • A disintegrin-like and metalloprotease (reprolysin type) with thrombospondin type 1 motifs: The ADAMTS family
    • DOI 10.1016/j.biocel.2004.01.014, PII S1357272504000226
    • Apte SS. A disintegrin-like and metalloprotease (reprolysin type) with thrombospondin type 1 motifs: The ADAMTS family. Int J Biochem Cell Biol 2004;36(6):981-985. (Pubitemid 38501549)
    • (2004) International Journal of Biochemistry and Cell Biology , vol.36 , Issue.6 , pp. 981-985
    • Apte, S.S.1
  • 25
    • 14244250200 scopus 로고    scopus 로고
    • The ADAMTS metalloproteinases
    • Porter S, Clark IM, Kevorkian L et al. The ADAMTS metalloproteinases. Biochem J 2005;386(Pt 1):15-27.
    • (2005) Biochem J , vol.386 , Issue.1 PART , pp. 15-27
    • Porter, S.1    Clark, I.M.2    Kevorkian, L.3
  • 26
    • 0023057157 scopus 로고
    • A growth-responsive gene (16C8) in normal mouse fibroblasts homologous to a human collagenase inhibitor with erythroid-potentiating activity: Evidence for inducible and constitutive transcripts
    • Edwards DR, Waterhouse P, Holman ML et al. A growth-responsive gene (16C8) in normal mouse fibroblasts homologous to a human collagenase inhibitor with erythroid-potentiating activity: Evidence for inducible and constitutive transcripts. Nucleic Acids Res 1986;14(22):8863-8878.
    • (1986) Nucleic Acids Res , vol.14 , Issue.22 , pp. 8863-8878
    • Edwards, D.R.1    Waterhouse, P.2    Holman, M.L.3
  • 27
    • 0036728623 scopus 로고    scopus 로고
    • MMPs and TIMPs-An historic perspective
    • Woessner J F J. MMPs and TIMPs-An historic perspective. Mol Biotechnol 2002;22(1):33-49.
    • (2002) Mol Biotechnol , vol.22 , Issue.1 , pp. 33-49
    • Woessner, J.F.J.1
  • 29
    • 14844284571 scopus 로고    scopus 로고
    • TIMP-2: An endogenous inhibitor of angiogenesis
    • DOI 10.1016/j.molmed.2005.01.007
    • Stetler-Stevenson WG, Seo DW. TIMP-2: An endogenous inhibitor of angiogenesis. Trends Mol Med 2005;11(3):97-103. (Pubitemid 40348986)
    • (2005) Trends in Molecular Medicine , vol.11 , Issue.3 , pp. 97-103
    • Stetler-Stevenson, W.G.1    Seo, D.-W.2
  • 30
    • 0035175984 scopus 로고    scopus 로고
    • Tissue inhibitors of metalloproteinases and programmed cell death: Conundrums, controversies and potential implications
    • DOI 10.1023/A:1012493808790
    • Mannello F, Gazzanelli G. Tissue inhibitors of metalloproteinases and programmed cell death: Conundrums, controversies and potential implications. Apoptosis 2001;6(6):479-482. (Pubitemid 33078759)
    • (2001) Apoptosis , vol.6 , Issue.6 , pp. 479-482
    • Mannello, F.1    Gazzanelli, G.2
  • 31
    • 0028097367 scopus 로고
    • Mutations in the tissue inhibitor of metalloproteinases-3 (TIMP3) in patients with Sorsby's fundus dystrophy
    • DOI 10.1038/ng1294-352
    • Weber BH, Vogt G, Pruett RC et al. Mutations in the tissue inhibitor of metalloproteinases-3(TIMP-3) in patients with Sorsby's fundus dystrophy. Nat Genet 1994;8 (4):352-356. (Pubitemid 24375600)
    • (1994) Nature Genetics , vol.8 , Issue.4 , pp. 352-356
    • Weber, B.H.F.1    Vogt, G.2    Pruett, R.C.3    Stohr, H.4    Felbor, U.5
  • 33
    • 0032531051 scopus 로고    scopus 로고
    • Development and disease in proteinase-deficient mice: Role of the plasminogen, matrix metalloproteinase and coagulation system
    • DOI 10.1016/S0049-3848(98)00122-4, PII S0049384898001224
    • Carmeliet P, Collen D. Development and disease in proteinase-deficient mice: Role of the plasminogen, matrix metalloproteinase and coagulation system. Thromb Res 1998;91(6):255-285. (Pubitemid 28454725)
    • (1998) Thrombosis Research , vol.91 , Issue.6 , pp. 255-285
    • Carmeliet, P.1    Collen, D.2
  • 36
    • 0037155014 scopus 로고    scopus 로고
    • Matrix remodeling in the ovary: Regulation and functional role of the plasminogen activator and matrix metalloproteinase systems
    • DOI 10.1016/S0303-7207(01)00711-0, PII S0303720701007110
    • Ny T, Wahlberg P, Brandstrom IJ. Matrix remodeling in the ovary: Regulation and functional role of the plasminogen activator and matrix metalloproteinase systems. Mol Cell Endocrinol 2002;187(1-2):29-38. (Pubitemid 34441038)
    • (2002) Molecular and Cellular Endocrinology , vol.187 , Issue.1-2 , pp. 29-38
    • Ny, T.1    Wahlberg, P.2    Brandstrom, I.J.M.3
  • 37
    • 0029089176 scopus 로고
    • Cellular receptors in the regulation of plasmin generation
    • Hajjar KA. Cellular receptors in the regulation of plasmin generation. Thromb Haemost 1995;74(1):294-301.
    • (1995) Thromb Haemost , vol.74 , Issue.1 , pp. 294-301
    • Hajjar, K.A.1
  • 38
    • 0036479735 scopus 로고    scopus 로고
    • Annexin II: A plasminogen-plasminogen activator coreceptor
    • Kim J, Hajjar KA. Annexin II: A plasminogen-plasminogen activator coreceptor. Front Biosci 2002;7:d341-d348.
    • (2002) Front Biosci , vol.7
    • Kim, J.1    Hajjar, K.A.2
  • 39
    • 0026516219 scopus 로고
    • Identification and characterization of the murine cell surface receptor for the urokinase-type plasminogen activator
    • Solberg H, Lober D, Eriksen J et al. Identification and characterization of the murine cell surface receptor for the urokinase-type plasminogen activator. Eur J Biochem 1992;205(2):451-458.
    • (1992) Eur J Biochem , vol.205 , Issue.2 , pp. 451-458
    • Solberg, H.1    Lober, D.2    Eriksen, J.3
  • 40
    • 0036906177 scopus 로고    scopus 로고
    • UPAR: A versatile signalling orchestrator
    • DOI 10.1038/nrm977
    • Blasi F, Carmeliet P. uPAR: A versatile signalling orchestrator. Nat Rev Mol Cell Biol 2002;3(12):932-943. (Pubitemid 35477371)
    • (2002) Nature Reviews Molecular Cell Biology , vol.3 , Issue.12 , pp. 932-943
    • Blasi, F.1    Carmeliet, P.2
  • 42
    • 0035846933 scopus 로고    scopus 로고
    • Type II transmembrane serine proteases. Insights into an emerging class of cell surface proteolytic enzymes
    • DOI 10.1074/jbc.R000020200
    • Hooper JD, Clements JA, Quigley JP et al. Type II transmembrane serine proteases. Insights into an emerging class of cell surface proteolytic enzymes. J Biol Chem 2001;276(2):857-860. (Pubitemid 32096501)
    • (2001) Journal of Biological Chemistry , vol.276 , Issue.2 , pp. 857-860
    • Hooper, J.D.1    Clements, J.A.2    Quigley, J.P.3    Antalis, T.M.4
  • 43
    • 0036320526 scopus 로고    scopus 로고
    • Human tissue kallikreins: A family of new cancer biomarkers
    • Diamandis EP, Yousef GM. Human tissue kallikreins: A family of new cancer biomarkers. Clin Chem 2002;48(8):1198-1205. (Pubitemid 34809825)
    • (2002) Clinical Chemistry , vol.48 , Issue.8 , pp. 1198-1205
    • Diamandis, E.P.1    Yousef, G.M.2
  • 44
    • 1542346405 scopus 로고    scopus 로고
    • An update on human and mouse glandular kallikreins
    • DOI 10.1016/j.clinbiochem.2003.12.013, PII S0009912003002637
    • Diamandis EP, Yousef GM, Olsson AY. An update on human and mouse glandular kallikreins. Clin Biochem 2004;37(4):258-260. (Pubitemid 38314878)
    • (2004) Clinical Biochemistry , vol.37 , Issue.4 , pp. 258-260
    • Diamandis, E.P.1    Yousef, G.M.2    Olsson, A.Y.3
  • 45
    • 0028206262 scopus 로고
    • The serpin superfamily of proteinase inhibitors: Structure, function, and regulation
    • Potempa J, Korzus E, Travis J. The serpin superfamily of proteinase inhibitors: Structure, function, and regulation. J Biol Chem 1994;269(23):15957-15960. (Pubitemid 24209273)
    • (1994) Journal of Biological Chemistry , vol.269 , Issue.23 , pp. 15957-15960
    • Potempa, J.1    Korzus, E.2    Travis, J.3
  • 46
    • 0035823595 scopus 로고    scopus 로고
    • The serpins are an expanding superfamily of structurally similar but functionally diverse proteins. Evolution, mechanism of inhibition, novel functions, and a revised nomenclature
    • Silverman GA, Bird PI, Carrell RW et al. The serpins are an expanding superfamily of structurally similar but functionally diverse proteins. Evolution, mechanism of inhibition, novel functions, and a revised nomenclature. J Biol Chem 2001;276(36):33293-33296.
    • (2001) J Biol Chem , vol.276 , Issue.36 , pp. 33293-33296
    • Silverman, G.A.1    Bird, P.I.2    Carrell, R.W.3
  • 47
    • 0036882395 scopus 로고    scopus 로고
    • Serpin structure, mechanism, and function
    • Gettins PG. Serpin structure, mechanism, and function. Chem Rev 2002;102(12):4751-4804.
    • (2002) Chem Rev , vol.102 , Issue.12 , pp. 4751-4804
    • Gettins, P.G.1
  • 48
    • 26244432935 scopus 로고    scopus 로고
    • Control of the coagulation system by serpins: Getting by with a little help from glycosaminoglycans
    • DOI 10.1111/j.1742-4658.2005.04880.x
    • Pike RN, Buckle AM, Le Bonniec BF et al. Control of the coagulation system by serpins. Getting by with a little help from glycosaminoglycans. FEBS J 2005;272(19):4842-4851. (Pubitemid 41415108)
    • (2005) FEBS Journal , vol.272 , Issue.19 , pp. 4842-4851
    • Pike, R.N.1    Buckle, A.M.2    Le Bonniec, B.F.3    Church, F.C.4
  • 50
    • 1842737700 scopus 로고    scopus 로고
    • Expression analysis of the entire MMP and TIMP gene families during mouse tissue development
    • DOI 10.1016/S0014-5793(04)00281-9, PII S0014579304002819
    • Nuttall RK, Sampieri CL, Pennington CJ et al. Expression analysis of the entire MMP and TIMP gene families during mouse tissue development. FEBS Lett 2004;563(1-3):129-134. (Pubitemid 38471586)
    • (2004) FEBS Letters , vol.563 , Issue.1-3 , pp. 129-134
    • Nuttall, R.K.1    Sampieri, C.L.2    Pennington, C.J.3    Gill, S.E.4    Schultz, G.A.5    Edwards, D.R.6
  • 51
    • 0028052249 scopus 로고
    • Follicle-stimulating hormone increases the expression of tissue inhibitors of metalloproteinases TIMP-1 and TIMP-2 and induces TIMP-1 AP-1 site binding complex (es) in prepubertal rat Sertoli cells
    • Ulisse S, Farina AR, Piersanti D et al. Follicle-stimulating hormone increases the expression of tissue inhibitors of metalloproteinases TIMP-1 and TIMP-2 and induces TIMP-1 AP-1 site binding complex (es) in prepubertal rat Sertoli cells. Endocrinology 1994;135(6):2479-2487.
    • (1994) Endocrinology , vol.135 , Issue.6 , pp. 2479-2487
    • Ulisse, S.1    Farina, A.R.2    Piersanti, D.3
  • 52
    • 0029000781 scopus 로고
    • Identification of a stimulator of steroid hormone synthesis isolated from testis
    • Boujrad N, Ogwuegbu SO, Garnier M et al. Identification of a stimulator of steroid hormone synthesis isolated from testis. Science 1995;268(5217):1609- 1612.
    • (1995) Science , vol.268 , Issue.5217 , pp. 1609-1612
    • Boujrad, N.1    Ogwuegbu, S.O.2    Garnier, M.3
  • 53
    • 0029868079 scopus 로고    scopus 로고
    • Gelatinase A secretion and its control in peritubular and Sertoli cell cultures: Effects of hormones, second messengers and inducers of cytokine production
    • DOI 10.1016/0303-7207(96)03764-1
    • Hoeben E, Van Haelst I, Swinnen JV et al. Gelatinase A secretion and its control in peritubular and Sertoli cell cultures: Effects of hormones, second messengers and inducers of cytokine production. Mol Cell Endocrinol 1996;118(1-2):37-46. (Pubitemid 26146074)
    • (1996) Molecular and Cellular Endocrinology , vol.118 , Issue.1-2 , pp. 37-46
    • Hoeben, E.1    Van Aelst, I.2    Swinnen, J.V.3    Opdenakker, G.4    Verhoeven, G.5
  • 54
    • 0034065810 scopus 로고    scopus 로고
    • Regulation of tissue inhibitor of metalloproteinases-1 in rat Sertoli cells: Induction by germ cell residual bodies, interleukin-1α, and second messengers
    • Gronning LM, Wang JE, Ree AH et al. Regulation of tissue inhibitor of metalloproteinases-1 in rat Sertoli cells: Induction by germ cell residual bodies, interleukin-1alpha, and second messengers. Biol Reprod 2000;62(4):1040-1046. (Pubitemid 30173819)
    • (2000) Biology of Reproduction , vol.62 , Issue.4 , pp. 1040-1046
    • Gronning, L.M.1    Wang, J.E.2    Ree, A.H.3    Haugen, T.B.4    Tasken, K.5    Tasken, K.A.6
  • 55
    • 0037187323 scopus 로고    scopus 로고
    • Evidence that MMP-2 and TIMP-2 are at play in the FSH-induced changes in Sertoli cells
    • Longin J, Le Magueresse-Battistoni B. Evidence that MMP-2 and TIMP-2 are at play in the FSH-induced changes in Sertoli cells. Mol Cell Endocrinol 2002;189(1-2):25-35.
    • (2002) Mol Cell Endocrinol , vol.189 , Issue.1-2 , pp. 25-35
    • Longin, J.1    Le Magueresse-Battistoni, B.2
  • 56
    • 0036165935 scopus 로고    scopus 로고
    • Matrix metalloproteinases regulate mesonephric cell migration in developing XY gonads which correlates with the inhibition of tissue inhibitor of metalloproteinase-3 by sry
    • DOI 10.1046/j.1440-169x.2002.00618.x
    • Nishino K, Yamanouchi K, Naito K et al. Matrix metalloproteinases regulate mesonephric cell migration in developing XY gonads which correlates with the inhibition of tissue inhibitor of metalloproteinase-3 by Sry. Dev Growth Differ 2002;44(1):35-43. (Pubitemid 34122106)
    • (2002) Development Growth and Differentiation , vol.44 , Issue.1 , pp. 35-43
    • Nishino, K.1    Yamanouchi, K.2    Naito, K.3    Tojo, H.4
  • 58
    • 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-a, 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(1):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
  • 59
    • 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 beta1 integrin/laminin gamma3 protein complex in the regulation of ectoplasmic specialization dynamics in the rat testis. Biol Reprod 2004;70(4):945-964. (Pubitemid 38387703)
    • (2004) Biology of Reproduction , vol.70 , Issue.4 , pp. 945-964
    • Siu, M.K.Y.1    Cheng, C.Y.2
  • 60
    • 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(9):978-992. (Pubitemid 39273071)
    • (2004) BioEssays , vol.26 , Issue.9 , pp. 978-992
    • Siu, M.K.Y.1    Cheng, C.Y.2
  • 61
    • 27644475089 scopus 로고    scopus 로고
    • Fibroblast growth factor (FGF) 2 and FGF9 mediate mesenchymal-epithelial interactions of peritubular and Sertoli cells in the rat testis
    • DOI 10.1677/joe.1.06146
    • El Ramy R, Vérot A, Mazaud S et al. Fibroblast growth factor (FGF) 2 and FGF9 mediate mesenchymal-epithelial interactions of peritubular and Sertoli cells in the rat testis. J Endocrinol 2005;187(1):135-147. (Pubitemid 41556409)
    • (2005) Journal of Endocrinology , vol.187 , Issue.1 , pp. 135-147
    • El Ramy, R.1    Verot, A.2    Mazaud, S.3    Odet, F.4    Magre, S.5    Le Magueresse-Battistoni, B.6
  • 62
    • 27544456723 scopus 로고    scopus 로고
    • Tissue mRNA expression in rat of newly described matrix metalloproteinases
    • Bernal F, Hartung HP, Kieseier BC. Tissue mRNA expression in rat of newly described matrix metalloproteinases. Biol Res 2005;38(2-3):267-271. (Pubitemid 41535627)
    • (2005) Biological Research , vol.38 , Issue.2-3 , pp. 267-271
    • Bernal, F.1    Hartung, H.-P.2    Kieseier, B.C.3
  • 64
    • 0033582513 scopus 로고    scopus 로고
    • Cloning and characterization of human MMP-23, a new matrix metalloproteinase predominantly expressed in reproductive tissues and lacking conserved domains in other family members
    • Velasco G, Pendas AM, Fueyo A et al. Cloning and characterization of human MMP-23, a new matrix metalloproteinase predominantly expressed in reproductive tissues and lacking conserved domains in other family members. J Biol Chem 1999;274(8):4570-4576.
    • (1999) J Biol Chem , vol.274 , Issue.8 , pp. 4570-4576
    • Velasco, G.1    Pendas, A.M.2    Fueyo, A.3
  • 65
    • 0035971090 scopus 로고    scopus 로고
    • Epilysin, a novel human matrix metalloproteinase (MMP-28) expressed in testis and keratinocytes and in response to injury
    • Lohi J, Wilson CL, Roby JD et al. Epilysin, a novel human matrix metalloproteinase (MMP-28) expressed in testis and keratinocytes and in response to injury. J Biol Chem 2001;276(13):10134-10144.
    • (2001) J Biol Chem , vol.276 , Issue.13 , pp. 10134-10144
    • Lohi, J.1    Wilson, C.L.2    Roby, J.D.3
  • 66
    • 0034944729 scopus 로고    scopus 로고
    • Matrix metalloproteinases and tissue inhibitors of metalloproteinases in human fetal testis and ovary
    • Robinson LL, Sznajder NA, Riley SC et al. Matrix metalloproteinases and tissue inhibitors of metalloproteinases in human fetal testis and ovary. Mol Hum Reprod 2001;7(7):641-648. (Pubitemid 32633413)
    • (2001) Molecular Human Reproduction , vol.7 , Issue.7 , pp. 641-648
    • Robinson, L.L.L.1    Sznajder, N.A.2    Riley, S.C.3    Anderson, R.A.4
  • 67
    • 0024591288 scopus 로고
    • Influences of follicle-stimulating hormone, proteases, and antiproteases on permeability of the barrier generated by Sertoli cells in a two-chambered assembly
    • Ailenberg M, Fritz IB. Influences of follicle-stimulating hormone, proteases, and antiproteases on permeability of the barrier generated by Sertoli cells in a two-chambered assembly. Endocrinology 1989;124(3):1399-1407. (Pubitemid 19082713)
    • (1989) Endocrinology , vol.124 , Issue.3 , pp. 1399-1407
    • Ailenberg, M.1    Fritz, I.B.2
  • 68
    • 0025885254 scopus 로고
    • Secretion of latent type IV procollagenase and active type IV collagenase by testicular cells in culture
    • Ailenberg M, Stetler-Stevenson WG, Fritz IB. Secretion of latent type IV procollagenase and active type IV collagenase by testicular cells in culture. Biochem J 1991;279(Pt 1):75-80.
    • (1991) Biochem J , vol.279 , Issue.1 PART , pp. 75-80
    • Ailenberg, M.1    Stetler-Stevenson, W.G.2    Fritz, I.B.3
  • 69
    • 0034457254 scopus 로고    scopus 로고
    • Identification of ADAM 31: A protein expressed in Leydig cells and specialized epithelia
    • DOI 10.1210/en.141.6.2033
    • Liu L, Smith JW. Identification of ADAM 31: A protein expressed in Leydig cells and specialized epithelia. Endocrinology 2000;141(6):2033-2042. (Pubitemid 32274353)
    • (2000) Endocrinology , vol.141 , Issue.6 , pp. 2033-2042
    • Liu, L.1    Smith, J.W.2
  • 70
    • 0030885016 scopus 로고    scopus 로고
    • Tissue inhibitor of metalloproteinases-2 is expressed in the interstitial matrix in adult mouse organs and during embryonic development
    • Blavier L, DeClerck YA. Tissue inhibitor of metalloproteinases-2 is expressed in the interstitial matrix in adult mouse organs and during embryonic development. Mol Biol Cell 1997;8(8):1513-1527. (Pubitemid 27385573)
    • (1997) Molecular Biology of the Cell , vol.8 , Issue.8 , pp. 1513-1527
    • Blavier, L.1    DeClerck, Y.A.2
  • 71
    • 18844438907 scopus 로고    scopus 로고
    • Gene expression in rat leydig cells during development from the progenitor to adult stage: A cluster analysis
    • DOI 10.1095/biolreprod.104.037499
    • Ge RS, Dong O, Sottas CM et al. Gene expression in rat Leydig cells during development from the progenitor to adult stage: A cluster analysis. Biol Reprod 2005;72(6):1405-1415. (Pubitemid 40696083)
    • (2005) Biology of Reproduction , vol.72 , Issue.6 , pp. 1405-1415
    • Ge, R.-S.1    Dong, Q.2    Sottas, C.M.3    Chen, H.4    Zirkin, B.R.5    Hardy, M.P.6
  • 72
    • 0020262650 scopus 로고
    • Changes in levels of plasminogen activator activity in normal and germ-cell-depleted testes during development
    • DOI 10.1016/0303-7207(82)90115-0
    • Lacroix M, Smith FE, Fritz IB. Changes in levels of plasminogen activator activity in normal and germ-cell-depleted testes during development. Mol Cell Endocrinol 1982;26(3):259-267. (Pubitemid 13108882)
    • (1982) Molecular and Cellular Endocrinology , vol.26 , Issue.3 , pp. 259-267
    • Lacroix, M.1    Smith, F.E.2    Fritz, I.B.3
  • 73
    • 0022999147 scopus 로고
    • Local synthesis of plasminogen by the seminiferous tubules of the testis
    • DOI 10.1016/0014-5793(86)80810-9
    • Saksela O, Vihko KK. Local synthesis of plasminogen by the seminiferous tubules of the testis. FEBS Lett 1986;204(2):193-197. (Pubitemid 17177102)
    • (1986) FEBS Letters , vol.204 , Issue.2 , pp. 193-197
    • Saksela, O.1    Vihko, K.K.2
  • 74
    • 0024499823 scopus 로고
    • Regulation of urokinase- and tissue-type plasminogen activator gene expression in the rat seminiferous epithelium
    • Vihko KK, Penttila TL, Parvinen M et al. Regulation of urokinase-and tissue-type plasminogen activator gene expression in the rat seminiferous epithelium. Mol Cell Endocrinol 1989;31(1):52-59. (Pubitemid 19045674)
    • (1989) Molecular Endocrinology , vol.3 , Issue.1 , pp. 52-59
    • Vihko, K.K.1    Penttila, T.-L.2    Parvinen, M.3    Belin, D.4
  • 75
    • 0029058394 scopus 로고
    • Hormonal regulation of urokinase-and tissue-type plasminogen activator in rat Sertoli cells
    • Tolli R, Monaco L D B, Di Bonito P et al. Hormonal regulation of urokinase-and tissue-type plasminogen activator in rat Sertoli cells. Biol Reprod 1995;53(1):193-200.
    • (1995) Biol Reprod , vol.53 , Issue.1 , pp. 193-200
    • Tolli, R.1    Monaco, L.D.B.2    Di Bonito, P.3
  • 76
    • 0033888021 scopus 로고    scopus 로고
    • Retinoid modulation of plasminogen activator production in rat Sertoli cells
    • Canipari R, Galdieri M. Retinoid modulation of plasminogen activator production in rat Sertoli cells. Biol Reprod 2000;63(2):544-550. (Pubitemid 30639945)
    • (2000) Biology of Reproduction , vol.63 , Issue.2 , pp. 544-550
    • Canipari, R.1    Galdieri, M.2
  • 77
    • 0023870949 scopus 로고
    • Immunohistochemical localization of urokinase-type plasminogen activator in Sertoli cells and tissue-type plasminogen activator in spermatogenic cells in the rat seminiferous epithelium
    • Vihko KK, Kristensen P, Dano K et al. Immunohistochemical localization of urokinase-type plasminogen activator in Sertoli cells and tissue-type plasminogen activator in spermatogenic cells in the rat seminiferous epithelium. Dev Biol 1988;126(1):150-155. (Pubitemid 18077594)
    • (1988) Developmental Biology , vol.126 , Issue.1 , pp. 150-155
    • Vihko, K.K.1    Kristensen, P.2    Dano, K.3    Parvinen, M.4
  • 78
    • 0042916338 scopus 로고    scopus 로고
    • Identification of developmentally regulated genes in the somatic cells of the mouse testis using serial analysis of gene expression
    • DOI 10.1095/biolreprod.103.016899
    • O'Shaughnessy PJ, Fleming L, Baker PJ et al. Identification of developmentally regulated genes in the somatic cells of the mouse testis using serial analysis of gene expression. Biol Reprod 2003;69(3):797-808. (Pubitemid 37069254)
    • (2003) Biology of Reproduction , vol.69 , Issue.3 , pp. 797-808
    • O'Shaughnessy, P.J.1    Fleming, L.2    Baker, P.J.3    Jackson, G.4    Johnston, H.5
  • 79
    • 1442299093 scopus 로고    scopus 로고
    • Evidence for similar expression of protein c inhibitor and the urokinase-type plasminogen activator system during mouse testis development
    • DOI 10.1210/en.2003-0955
    • Odet F, Guyot R, Leduque P et al. Evidence for similar expression of protein C inhibitor and the urokinase-type plasminogen activator system during mouse testis development. Endocrinology 2004;145:1481-1489. (Pubitemid 38281034)
    • (2004) Endocrinology , vol.145 , Issue.3 , pp. 1481-1489
    • Odet, F.1    Guyot, R.2    Leduque, P.3    Le Magueresse-Battistoni, B.4
  • 80
    • 0023251025 scopus 로고
    • Plasminogen activator and mouse spermatozoa: Urokinase synthesis in the male genital tract and binding of the enzyme to the sperm cell surface
    • DOI 10.1083/jcb.104.5.1281
    • Huarte J, Belin D, Bosco D et al. Plasminogen activator and mouse spermatozoa: Urokinase synthesis in the male genital tract and binding of the enzyme to the sperm cell surface. J Cell Biol 1987;104(5):1281-1289. (Pubitemid 17084487)
    • (1987) Journal of Cell Biology , vol.104 , Issue.5 , pp. 1281-1289
    • Huarte, J.1    Belin, D.2    Bosco, D.3
  • 81
    • 16844377832 scopus 로고    scopus 로고
    • Historical analysis of PAI-I from its discovery to its potential role in cell motility and disease
    • DOI 10.1160/TH05-01-0033
    • Dellas C, Loskutoff DJ. Historical analysis of PAI-1 from its discovery to its potential role in cell motility and disease. Thromb Haemost 2005;93(4):631-640. (Pubitemid 40485397)
    • (2005) Thrombosis and Haemostasis , vol.93 , Issue.4 , pp. 631-640
    • Dellas, C.1    Loskutoff, D.J.2
  • 82
    • 0029655550 scopus 로고    scopus 로고
    • Vitronectin in the cytoplasm of Leydig cells in the rat testis
    • Sawada H, Sugawara I, Kitami A et al. Vitronectin in the cytoplasm of Leydig cells in the rat testis. Biol Reprod 1996;54(1):29-35. (Pubitemid 126506795)
    • (1996) Biology of Reproduction , vol.54 , Issue.1 , pp. 29-35
    • Sawada, H.1    Sugawara, I.2    Kitami, A.3    Hayashi, M.4
  • 83
    • 0029026059 scopus 로고
    • PCR-amplified vitronectin mRNA localizes in situ to spermatocytes and round spermatids in the human testis
    • Nuovo GJ, Preissner KT, Bronson RA. PCR-amplified vitronectin mRNA localizes in situ to spermatocytes and round spermatids in the human testis. Hum Reprod 1995;10(8):2187-2191.
    • (1995) Hum Reprod , vol.10 , Issue.8 , pp. 2187-2191
    • Nuovo, G.J.1    Preissner, K.T.2    Bronson, R.A.3
  • 84
    • 0023914671 scopus 로고
    • Rat testicular peritubular cells in culture secrete an inhibitor of plasminogen activator activity
    • Hettle JA, Balekjian E, Tung PS et al. Rat testicular peritubular cells in culture secrete an inhibitor of plasminogen activator activity. Biol Reprod 1988;38(2):359-371. (Pubitemid 18097775)
    • (1988) Biology of Reproduction , vol.38 , Issue.2 , pp. 359-371
    • Hettle, J.A.1    Balekjian, E.2    Tung, P.S.3    Fritz, I.B.4
  • 86
    • 0025248246 scopus 로고
    • Modulation of levels of messenger RNA for tissue-type plasminogen activator in rat Sertoli cells, and levels of messenger RNA for plasminogen activator inhibitor in testis peritubular cells
    • DOI 10.1016/0303-7207(90)90060-L
    • Nargolwalla C, McCabe D, Fritz IB. Modulation of levels of messenger RNA for tissue-type plasminogen activator in rat Sertoli cells, and levels of messenger RNA for plasminogen activator inhibitor in testis peritubular cells. Mol Cell Endocrinol 1990;70(1):73-80. (Pubitemid 20097825)
    • (1990) Molecular and Cellular Endocrinology , vol.70 , Issue.1 , pp. 73-80
    • Nargolwalla, C.1    McCabe, D.2    Fritz, I.B.3
  • 87
    • 0029783821 scopus 로고    scopus 로고
    • Plasminogen activator inhibitor-1 regulation in cultured rat peritubular cells by basic fibroblast growth factor and transforming growth factor-α
    • DOI 10.1210/en.137.10.4243
    • Le Magueresse-Battistoni B, Pernod G, Kolodie L et al. Plasminogen activator inhibitor-1 regulation in cultured rat peritubular cells by basic fibroblast growth factor and transforming growth factor-alpha. Endocrinology 1996;137(10):4243-4249. (Pubitemid 26321872)
    • (1996) Endocrinology , vol.137 , Issue.10 , pp. 4243-4249
    • Le Magueresse-Battistoni, B.1    Pernod, G.2    Kolodie, L.3    Benahmed, M.4
  • 88
    • 0031039730 scopus 로고    scopus 로고
    • Tumor necrosis factor-α regulates plasminogen activator inhibitor-1 in rat testicular peritubular cells
    • DOI 10.1210/en.138.3.1097
    • Le Magueresse-Battistoni B, Pernod G, Kolodie L et al. Tumor necrosis factor-alpha regulates plasminogen activator inhibitor-1 in rat testicular peritubular cells. Endocrinology 1997;138(3):1097-1105. (Pubitemid 27089766)
    • (1997) Endocrinology , vol.138 , Issue.3 , pp. 1097-1105
    • Le Magueresse-Battistoni, B.1    Pernod, G.2    Kolodie, L.3    Morera, A.-M.4    Benahmed, M.5
  • 90
    • 23844470846 scopus 로고    scopus 로고
    • Protein C inhibitor expression by adult rat sertoli cells: Effects of testosterone withdrawal and replacement
    • DOI 10.2164/jandrol.05001
    • Anway MD, Show MD, Zirkin BR. Protein C inhibitor expression by adult rat Sertoli cells: Effects of testosterone withdrawal and replacement. J Androl 2005;26(5):578-585. (Pubitemid 41161317)
    • (2005) Journal of Andrology , vol.26 , Issue.5 , pp. 578-585
    • Anway, M.D.1    Show, M.D.2    Zirkin, B.R.3
  • 92
    • 0031829165 scopus 로고    scopus 로고
    • Extrahepatic expression and regulation of protein C in the mouse
    • Yamamoto K, Loskutoff DJ. Extrahepatic expression and regulation of protein C in the mouse. Am J Pathol 1998;153(2):547-555. (Pubitemid 28373665)
    • (1998) American Journal of Pathology , vol.153 , Issue.2 , pp. 547-555
    • Yamamoto, K.1    Loskutoff, D.J.2
  • 93
    • 33747594541 scopus 로고    scopus 로고
    • The mouse testis is the source of various serine proteases and serine proteinase inhibitors (SERPINs): Serine proteases and SERPINs identified in leydig cells are under gonadotropin regulation
    • DOI 10.1210/en.2006-0484
    • Odet F, Vérot A, Le Magueresse-Battistoni B. The mouse testis is the source of various serine proteases and SERine Proteinase INhibitors (SERPINs). Serine proteases and SERPINs identified in Leydig cells are under gonadotropin regulation. Endocrinology 2006;147(9):4374-83. (Pubitemid 44268388)
    • (2006) Endocrinology , vol.147 , Issue.9 , pp. 4374-4383
    • Odet, F.1    Verot, A.2    Le Magueresse-Battistoni, B.3
  • 95
    • 0037053319 scopus 로고    scopus 로고
    • A mouse serine protease TESP5 is selectively included into lipid rafts of sperm membrane presumably as a glycosylphosphatidylinositol-anchored protein
    • DOI 10.1074/jbc.M112470200
    • Honda A, Yamagata K, Sugiura S et al. A mouse serine protease TESP5 is selectively included into lipid rafts of sperm membrane presumably as a glycosylphosphatidylinositol-anchored protein. J Biol Chem 2002;277(19):16976- 16984. (Pubitemid 34967726)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.19 , pp. 16976-16984
    • Honda, A.1    Yamagata, K.2    Sugiura, S.3    Watanabe, K.4    Baba, T.5
  • 96
    • 10044256743 scopus 로고    scopus 로고
    • TESSP-1: A novel serine protease gene expressed in the spermatogonia and spermatocytes of adult mouse testes
    • DOI 10.1002/mrd.20184
    • Takano N, Matsui H, Takahashi T. TESSP-1: A novel serine protease gene expressed in the spermatogonia and spermatocytes of adult mouse testes. Mol Reprod Dev 2005;70(1):1-10. (Pubitemid 39602535)
    • (2005) Molecular Reproduction and Development , vol.70 , Issue.1 , pp. 1-10
    • Takano, N.1    Matsui, H.2    Takahashi, T.3
  • 97
    • 0033118244 scopus 로고    scopus 로고
    • Cloning and structural analysis of leydin, a novel human serine protease expressed by the Leydig cells of the testis
    • DOI 10.1046/j.1432-1327.1999.00266.x
    • Poorafshar M, Hellman L. Cloning and structural analysis of leydin, a novel human serine protease expressed by the Leydig cells of the testis. Eur J Biochem 1999;261(1):244-250. (Pubitemid 29166090)
    • (1999) European Journal of Biochemistry , vol.261 , Issue.1 , pp. 244-250
    • Poorafshar, M.1    Hellman, L.2
  • 98
    • 0033724731 scopus 로고    scopus 로고
    • Cloning and characterization of mouse klk27, a novel tissue kallikrein expressed in testicular Leydig cells and exhibiting chymotrypsin-like specificity
    • Matsui H, Moriyama A, Takahashi T. Cloning and characterization of mouse klk27, a novel tissue kallikrein expressed in testicular Leydig cells and exhibiting chymotrypsin-like specificity. Eur J Biochem 2000;267(23):6858-6865.
    • (2000) Eur J Biochem , vol.267 , Issue.23 , pp. 6858-6865
    • Matsui, H.1    Moriyama, A.2    Takahashi, T.3
  • 99
    • 0034751918 scopus 로고    scopus 로고
    • Mouse testicular leydig cells express Klk21, a tissue kallikrein that cleaves fibronectin and IGF-binding protein-3
    • DOI 10.1210/en.142.11.4918
    • Matsui H, Takahashi T. Mouse testicular Leydig cells express Klk21, a tissue kallikrein that cleaves fibronectin and IGF-binding protein-3. Endocrinology 2001;142:4918-4929. (Pubitemid 33022368)
    • (2001) Endocrinology , vol.142 , Issue.11 , pp. 4918-4929
    • Matsui, H.1    Takahashi, T.2
  • 100
    • 23944479689 scopus 로고    scopus 로고
    • Characterization of mouse glandular kallikrein 24 expressed in testicular Leydig cells
    • DOI 10.1016/j.biocel.2005.05.011, PII S1357272505001615
    • Matsui H, Takano N, Takahashi T. Characterization of mouse glandular kallikrein 24 expressed in testicular Leydig cells. Int J Biochem Cell Biol 2005;37(11):2333-2343. (Pubitemid 41207405)
    • (2005) International Journal of Biochemistry and Cell Biology , vol.37 , Issue.11 , pp. 2333-2343
    • Matsui, H.1    Takano, N.2    Takahashi, T.3
  • 102
    • 0029086070 scopus 로고
    • Thiol ester cleavage-dependent conformational change in human α2-macroglobulin. Influence of attacking nucleophile and of Cys949 modification
    • Gettins PG. Thiol ester cleavage-dependent conformational change in human α2-macroglobulin. Influence of attacking nucleophile and of Cys949 modification. Biochemistry 1995;34(38):12233-12240.
    • (1995) Biochemistry , vol.34 , Issue.38 , pp. 12233-12240
    • Gettins, P.G.1
  • 103
    • 0025743229 scopus 로고
    • Alpha 2-macroglobulin is not an acute-phase protein in the rat testis
    • Stahler MS, Schlegel P, Bardin CW et al. Alpha 2-macroglobulin is not an acute-phase protein in the rat testis. Endocrinology 1991;128(6):2805-2814.
    • (1991) Endocrinology , vol.128 , Issue.6 , pp. 2805-2814
    • Stahler, M.S.1    Schlegel, P.2    Bardin, C.W.3
  • 104
    • 0033783352 scopus 로고    scopus 로고
    • Fibroblast growth factors, their receptors and signalling
    • Powers CJ, McLeskey SW, Wellistein A. Fibroblast growth factors, their receptors and signalling. Endocr Relat Cancer 2000;7(3):165-197.
    • (2000) Endocr Relat Cancer , vol.7 , Issue.3 , pp. 165-197
    • Powers, C.J.1    McLeskey, S.W.2    Wellistein, A.3
  • 105
    • 27944450453 scopus 로고    scopus 로고
    • TGFβ superfamily members in spermatogenesis: Setting the stage for fertility in mouse and Drosophila
    • DOI 10.1007/s00441-005-0008-0
    • Loveland KL, Hime G. TGFbeta superfamily members in spermatogenesis: Setting the stage for fertility in mouse and Drosophila. Cell Tissue Res 2005;322(1):141-146. (Pubitemid 41677665)
    • (2005) Cell and Tissue Research , vol.322 , Issue.1 , pp. 141-146
    • Loveland, K.L.1    Hime, G.2
  • 106
    • 0033305171 scopus 로고    scopus 로고
    • Hepatocyte growth factor and c-MET are expressed in rat prepuberal testis
    • Catizone A, Ricci G, Arista V et al. Hepatocyte growth factor and c-MET are expressed in rat prepuberal testis. Endocrinology 1999;140(7):3106-3113. (Pubitemid 30650625)
    • (1999) Endocrinology , vol.140 , Issue.7 , pp. 3106-3113
    • Catizone, A.1    Ricci, G.2    Arista, V.3    Innocenzi, A.4    Galdieri, M.5
  • 107
    • 0035043068 scopus 로고    scopus 로고
    • Expression and functional role of hepatocyte growth factor receptor (C-MET) during postnatal rat testis development
    • DOI 10.1210/en.142.5.1828
    • Catizone A, Ricci G, Galdieri M. Expression and functional role of hepatocyte growth factor receptor (C-MET) during postnatal rat testis development. Endocrinology 2001;142(5):1828-1834. (Pubitemid 32405939)
    • (2001) Endocrinology , vol.142 , Issue.5 , pp. 1828-1834
    • Catizone, A.1    Ricci, G.2    Galdieri, M.3
  • 108
    • 0037059458 scopus 로고    scopus 로고
    • Vascular origin of a soluble truncated form of the hepatocyte growth factor receptor (c-met)
    • DOI 10.1161/hh0102.102756
    • Wajih N, Walter J, Sane DC. Vascular origin of a soluble truncated form of the hepatocyte growth factor (c-met). Circ Res 2002;90(1):46-52. (Pubitemid 34074607)
    • (2002) Circulation Research , vol.90 , Issue.1 , pp. 46-52
    • Wajih, N.1    Walter, J.2    Sane, D.C.3
  • 109
    • 0029959437 scopus 로고    scopus 로고
    • Matrix metalloproteinase 2 releases active soluble ectodomain of fibroblast growth factor receptor 1
    • Levi E, Fridman R, Hiao HQ et al. Matrix metalloproteinase 2 releases active soluble ectodomain of fibroblast growth factor receptor 1. Proc Natl Acad Sci USA 1996;93(14):1069-7074.
    • (1996) Proc Natl Acad Sci USA , vol.93 , Issue.14 , pp. 1069-7074
    • Levi, E.1    Fridman, R.2    Hiao, H.Q.3
  • 110
    • 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(1):102-115. (Pubitemid 24058598)
    • (1994) Endocrine Reviews , vol.15 , Issue.1 , pp. 102-115
    • Dym, M.1
  • 111
    • 0016699710 scopus 로고
    • The peritubular tissue in the normal and pathological human testis. An ultrastructural study
    • de Kretser DM, Kerr JB, Paulsen CA. The peritubular tissue in the normal and pathological human testis. An ultrastructural study. Biol Reprod 1975;12(3):317-324.
    • (1975) Biol Reprod , vol.12 , Issue.3 , pp. 317-324
    • De Kretser, D.M.1    Kerr, J.B.2    Paulsen, C.A.3
  • 114
    • 33646873238 scopus 로고    scopus 로고
    • Adhesion molecules for mouse primordial germ cells
    • De Felici M, Scaldaferri ML, Farini D. Adhesion molecules for mouse primordial germ cells. Front Biosci 2005;10:542-551.
    • (2005) Front Biosci , vol.10 , pp. 542-551
    • De Felici, M.1    Scaldaferri, M.L.2    Farini, D.3
  • 117
    • 0024344909 scopus 로고
    • Basement membrane and epithelial features of fetal-type Leydig cells in rat and human testis
    • Kuopio T, Paranko J, Pelliniemi LJ. Basement membrane and epithelial features of fetal-type Leydig cells in rat and human testis. Differentiation 1989;40(3):198-206. (Pubitemid 19198278)
    • (1989) Differentiation , vol.40 , Issue.3 , pp. 198-206
    • Kuopio, T.1    Paranko, J.2    Pelliniemi, L.J.3
  • 118
    • 0025728605 scopus 로고
    • Effect of tunicamycin, an inhibitor of protein glycosylation, on testicular cord organization in fetal mouse gonadal explants in vitro
    • Kanai Y, Hayashi Y, Kawakami H et al. Effect of tunicamycin, an inhibitor of protein glycosylation, on testicular cord organization in fetal mouse gonadal explants in vitro. Anat Rec 1991;230(2):199-208.
    • (1991) Anat Rec , vol.230 , Issue.2 , pp. 199-208
    • Kanai, Y.1    Hayashi, Y.2    Kawakami, H.3
  • 119
    • 0033839508 scopus 로고    scopus 로고
    • Gonadal development in mammals at the cellular and molecular levels
    • Mackay S. Gonadal development in mammals at the cellular and molecular levels. Int Rev Cytol 2000;200:47-99. (Pubitemid 30670197)
    • (2000) International Review of Cytology , vol.200 , pp. 47-99
    • Mackay, S.1
  • 121
    • 0033999286 scopus 로고    scopus 로고
    • The battle of the sexes
    • DOI 10.1016/S0925-4773(99)00327-5, PII S0925477399003275
    • Capel B. The battle of the sexes. Mech Dev 2000;92(1):89-103. (Pubitemid 30125964)
    • (2000) Mechanisms of Development , vol.92 , Issue.1 , pp. 89-103
    • Capel, B.1
  • 122
    • 0023513106 scopus 로고
    • Expression of type I and II collagen during morphogenesis of fetal rat testis and ovary
    • DOI 10.1002/ar.1092190115
    • Paranko J. Expression of type I and III collagen during morphogenesis of fetal rat testis and ovary. Anat Rec 1987;219(1):91-101. (Pubitemid 18011923)
    • (1987) Anatomical Record , vol.219 , Issue.1 , pp. 91-101
    • Paranko, J.1
  • 124
    • 0026776491 scopus 로고
    • Differential expression of acidic cytokeratins 18 and 19 during sexual differentiation of the rat gonad
    • Fridmacher V, Locquet O, Magre S. Differential expression of acidic cytokeratins 18 and 19 during sexual differentiation of the rat gonad. Development 1992;115(2):503-517.
    • (1992) Development , vol.115 , Issue.2 , pp. 503-517
    • Fridmacher, V.1    Locquet, O.2    Magre, S.3
  • 125
    • 0026718476 scopus 로고
    • Intermediate filaments and epithelial differentiation of male rat embryonic gonad
    • Frojdman K, Paranko J, Virtanen I et al. Intermediate filaments and epithelial differentiation of male rat embryonic gonad. Differentiation 1992;50(2):113-123.
    • (1992) Differentiation , vol.50 , Issue.2 , pp. 113-123
    • Frojdman, K.1    Paranko, J.2    Virtanen, I.3
  • 126
    • 0035883926 scopus 로고    scopus 로고
    • Structural and regulatory macromolecules in sex differentiation of gonads
    • DOI 10.1002/jez.1096
    • Pelliniemi LJ, Frojdman K. Structural and regulatory macromolecules in sex differentiation of gonads. J Exp Zool 2001;290(5):523-528. (Pubitemid 32930902)
    • (2001) Journal of Experimental Zoology , vol.290 , Issue.5 , pp. 523-528
    • Pelliniemi, L.J.1    Frojdman, K.2
  • 127
    • 0028298134 scopus 로고
    • Extracellular matrix abnormalities in testis and epididymis of XXSxr ("sex-reversed") mice
    • Griffin JK, Blecher SR. Extracellular matrix abnormalities in testis and epididymis of XXSxr ("sex-reversed") mice. Mol Reprod Dev 1994;38(1):1-7.
    • (1994) Mol Reprod Dev , vol.38 , Issue.1 , pp. 1-7
    • Griffin, J.K.1    Blecher, S.R.2
  • 128
    • 0035114455 scopus 로고    scopus 로고
    • Tescalcin, a novel gene encoding a putative EF-hand Ca (2+)-binding protein, Col9a3, and renin are expressed in the mouse testis during the early stages of gonadal differentiation
    • Perera EM, Martin H, Seeherunvong T et al. Tescalcin, a novel gene encoding a putative EF-hand Ca (2+)-binding protein, Col9a3, and renin are expressed in the mouse testis during the early stages of gonadal differentiation. Endocrinology 2001;142(1):455-163.
    • (2001) Endocrinology , vol.142 , Issue.1 , pp. 455-163
    • Perera, E.M.1    Martin, H.2    Seeherunvong, T.3
  • 129
    • 11144344432 scopus 로고    scopus 로고
    • Basal membrane remodeling during follicle histogenesis in the rat ovary: Contribution of proteinases of the MMP and PA families
    • DOI 10.1016/j.ydbio.2004.10.001, PII S0012160604007134
    • Mazaud S, Guyot R, Guigon CJ et al. Basal membrane remodeling during follicle histogenesis in the rat ovary: Contribution of proteinases of the MMP and PA families. Dev Biol 2005;277(2):403-416. (Pubitemid 40022960)
    • (2005) Developmental Biology , vol.277 , Issue.2 , pp. 403-416
    • Mazaud, S.1    Guyot, R.2    Guigon, C.J.3    Coudouel, N.4    Le Magueresse-Battistoni, B.5    Magre, S.6
  • 131
    • 31544470351 scopus 로고    scopus 로고
    • Expression profiling of purified mouse gonadal somatic cells during the critical time window of sex determination reveals novel candidate genes for human sexual dysgenesis syndromes
    • DOI 10.1093/hmg/ddi463
    • Beverdam A, Koopman P. Expression profiling of purified mouse gonadal somatic cells during the critical time window of sex determination reveals novel candidate genes for human sexual dysgenesis syndromes. Hum Mol Genet 2006;15(3):417-431. (Pubitemid 43159894)
    • (2006) Human Molecular Genetics , vol.15 , Issue.3 , pp. 417-431
    • Beverdam, A.1    Koopman, P.2
  • 132
    • 0030111258 scopus 로고    scopus 로고
    • Sertoli cell signaling by Desert hedgehog regulates the male germline
    • Bitgood MJ, Shen L, McMahon AP. Sertoli cell signaling by Desert hedgehog regulates the male germline. Curr Biol 1996;6(3):298-304.
    • (1996) Curr Biol , vol.6 , Issue.3 , pp. 298-304
    • Bitgood, M.J.1    Shen, L.2    McMahon, A.P.3
  • 133
    • 0033709190 scopus 로고    scopus 로고
    • Desert hedgehog (Dhh) gene is required in the mouse testis for formation of adult-type Leydig cells and normal development of peritubular cells and seminiferous tubules
    • Clark AM, Garland KK, Russell LD. Desert hedgehog (Dhh) gene is required in the mouse testis for formation of adult-type Leydig cells and normal development of peritubular cells and seminiferous tubules. Biol Reprod 2000;63(6):1825-1838.
    • (2000) Biol Reprod , vol.63 , Issue.6 , pp. 1825-1838
    • Clark, A.M.1    Garland, K.K.2    Russell, L.D.3
  • 134
    • 0034758841 scopus 로고    scopus 로고
    • A developmental study of the desert hedgehog-null mouse testis
    • Pierucci-Alves F, Clark AM, Russell LD. A developmental study of the Desert hedgehog-null mouse testis. Biol Reprod 2001;65(5):1392-1402. (Pubitemid 33031496)
    • (2001) Biology of Reproduction , vol.65 , Issue.5 , pp. 1392-1402
    • Pierucci-Alves, F.1    Clark, A.M.2    Russell, L.D.3
  • 135
    • 0036067874 scopus 로고    scopus 로고
    • Disruption of testis cords by cyclopamine or forskolin reveals independent cellular pathways in testis organogenesis
    • DOI 10.1006/dbio.2002.0663
    • Yao HH, Capel B. Disruption of testis cords by cyclopamine or forskolin reveals independent cellular pathways in testis organogenesis. Dev Biol 2002;246(2):356-365. (Pubitemid 34775352)
    • (2002) Developmental Biology , vol.246 , Issue.2 , pp. 356-365
    • Yao, H.H.-C.1    Capel, B.2
  • 136
    • 0027468962 scopus 로고
    • Proteases are implicated in the changes in the Sertoli cell cytoskeleton elicited by follicle-stimulating hormone or by dibutyryl cyclic AMP
    • Tung PS, Burdzy K, Fritz IB. Proteases are implicated in the changes in the Sertoli cell cytoskeleton elicited by follicle-stimulating hormone or by dibutyryl cyclic AMP. J Cell Physiol 1993;155(1):139-148. (Pubitemid 23109066)
    • (1993) Journal of Cellular Physiology , vol.155 , Issue.1 , pp. 139-148
    • Tung, P.S.1    Burdzy, K.2    Fritz, I.B.3
  • 137
    • 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(6):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
  • 138
    • 0025303122 scopus 로고
    • Laminin promotes formation of cord-like structures by Sertoli cells in vitro
    • DOI 10.1016/0012-1606(90)90082-T
    • Hadley MA, Weeks BS, Kleinman HK et al. Laminin promotes formation of cord-like structures by Sertoli cells in vitro. Dev Biol 1990;40(2):318-327. (Pubitemid 20222470)
    • (1990) Developmental Biology , vol.140 , Issue.2 , pp. 318-327
    • Hadley, M.A.1    Weeks, B.S.2    Kleinman, H.K.3    Dym, M.4
  • 139
    • 0027944828 scopus 로고
    • Role of laminin in the morphogenetic cascade during coculture of sertoli cells with peritubular cells
    • DOI 10.1002/jcp.1041610111
    • Tung PS, Fritz IB. Role of laminin in the morphogenetic cascade during coculture of Sertoli cells with peritubular cells. J Cell Physiol 1994;161(1):77-88. (Pubitemid 24315653)
    • (1994) Journal of Cellular Physiology , vol.161 , Issue.1 , pp. 77-88
    • Tung, P.S.1    Fritz, I.B.2
  • 140
    • 0033544026 scopus 로고    scopus 로고
    • An in vitro tubule assay identifies HGF as a morphogen for the formation of seminiferous tubules in the postnatal mouse testis
    • DOI 10.1006/excr.1999.4630
    • van der Wee K, Hofmann MC. An in vitro tubule assay identifies HGF as a morphogen for the formation of seminiferous tubules in the postnatal mouse testis. Exp Cell Res 1999;252(1):175-185. (Pubitemid 29485137)
    • (1999) Experimental Cell Research , vol.252 , Issue.1 , pp. 175-185
    • Van Der Wee, K.1    Hofmann, M.-C.2
  • 141
    • 24044452859 scopus 로고    scopus 로고
    • Laminin α1 chain corrects male infertility caused by absence of laminin α2 chain
    • Hager M, Gawlik K, Nystrom A et al. Laminin {alpha}1 chain corrects male infertility caused by absence of laminin {alpha}2 chain. Am J Pathol 2005;167(3):823-833. (Pubitemid 41216365)
    • (2005) American Journal of Pathology , vol.167 , Issue.3 , pp. 823-833
    • Hager, M.1    Gawlik, K.2    Nystrom, A.3    Sasaki, T.4    Durbeej, M.5
  • 142
    • 0037378623 scopus 로고    scopus 로고
    • Sertoli cell tight junction dynamics: Their regulation during spermatogenesis
    • DOI 10.1095/biolreprod.102.010371
    • Lui WY, Mruk D, Lee WM et al. Sertoli cell tight junction dynamics: Their regulation during spermatogenesis. Biol Reprod 2003;68(4):1087-1097. (Pubitemid 36359095)
    • (2003) Biology of Reproduction , vol.68 , Issue.4 , pp. 1087-1097
    • Lui, W.-Y.1    Mruk, D.2    Lee, W.M.3    Cheng, C.Y.4
  • 143
    • 22544470331 scopus 로고    scopus 로고
    • Cytokines and junction restructuring during spermatogenesis - A lesson to learn from the testis
    • DOI 10.1016/j.cytogfr.2005.05.007, PII S1359610105000675
    • Xia W, Mruk DD, Lee WM et al. Cytokines and junction restructuring during spermatogenesis-A lesson to learn from the testis. Cytokine Growth Factor Rev 2005;16(4-5):469-493. (Pubitemid 41022014)
    • (2005) Cytokine and Growth Factor Reviews , vol.16 , Issue.4-5 , pp. 469-493
    • Xia, W.1    Mruk, D.D.2    Lee, W.M.3    Cheng, C.Y.4
  • 145
    • 0022588214 scopus 로고
    • Regulation of stages VI and VIII of the rat seminiferous epithelial cycle in vitro
    • Toppari J, Vihko KK, Rasanen KG et al. Regulation of stages VI and VIII of the rat seminiferous epithelial cycle in vitro. J Endocrinol 1986;108(3):417-422. (Pubitemid 16160810)
    • (1986) Journal of Endocrinology , vol.108 , Issue.3 , pp. 417-422
    • Toppari, J.1    Vihko, K.K.2    Rasanen, K.G.E.3
  • 146
    • 0028587657 scopus 로고
    • The immunohistochemical localization of alpha 2-macroglobulin in rat testes is consistent with its role in germ cell movement and spermiation
    • Zhu LJ, Cheng CY, Phillips DM et al. The immunohistochemical localization of alpha 2-macroglobulin in rat testes is consistent with its role in germ cell movement and spermiation. J Androl 1994;15:575-582.
    • (1994) J Androl , vol.15 , pp. 575-582
    • Zhu, L.J.1    Cheng, C.Y.2    Phillips, D.M.3
  • 147
    • 0031424610 scopus 로고    scopus 로고
    • Interactions of proteases and protease inhibitors in sertoli-germ cell cocultures preceding the formation of specialized sertoli-germ cell junctions In Vitro
    • Mruk D, Zhu LJ, Silvestrini B et al. Interactions of proteases and protease inhibitors in Sertoli-germ cell cocultures preceding the formation of specialized Sertoli-germ cell junctions in vitro. J Androl 1997;18(6):612-622. (Pubitemid 28098775)
    • (1997) Journal of Andrology , vol.18 , Issue.6 , pp. 612-622
    • Mruk, D.1    Zhu, L.-J.2    Silvestrini, B.3    Lee, W.M.4    Cheng, C.Y.5
  • 148
    • 0028958806 scopus 로고
    • Germ cell-Sertoli cell interactions: Regulation by germ cells of the stage-specific expression of CP-2/cathepsin L mRNA by Sertoli cells
    • Wright WW, Zabludoff SD, Penttila TL et al. Germ cell-Sertoli cell interactions: Regulation by germ cells of the stage-specific expression of CP-2/cathepsin L mRNA by Sertoli cells. Dev Genet 1995;16(2):104-113.
    • (1995) Dev Genet , vol.16 , Issue.2 , pp. 104-113
    • Wright, W.W.1    Zabludoff, S.D.2    Penttila, T.L.3
  • 149
    • 0035017190 scopus 로고    scopus 로고
    • Male germ cells regulate transcription of the cathepsin L gene by rat Sertoli cells
    • DOI 10.1210/en.142.6.2318
    • Zabludoff SD, Charron M, DeCerbo JN et al. Male germ cells regulate transcription of the cathepsin l gene by rat Sertoli cells. Endocrinology 2001;142(6):2318-2327. (Pubitemid 32473086)
    • (2001) Endocrinology , vol.142 , Issue.6 , pp. 2318-2327
    • Zabludoff, S.D.1    Charron, M.2    Decerbo, J.N.3    Simukova, N.4    Wright, W.W.5
  • 150
    • 0031594946 scopus 로고    scopus 로고
    • 2-macroglobulin expression in rat sertoli cells and hepatocytes by germ cells in vitro
    • DOI 10.1095/biolreprod59.1.111
    • Braghiroli L, Silvestrini B, Sorrentino C et al. Regulation of alpha2-macroglobulin expression in rat Sertoli cells and hepatocytes by germ cells in vitro. Biol Reprod 1998;59(1):111-123. (Pubitemid 28304361)
    • (1998) Biology of Reproduction , vol.59 , Issue.1 , pp. 111-123
    • Braghiroli, L.1    Silvestrini, B.2    Sorrentino, C.3    Grima, J.4    Mruk, D.5    Cheng, C.Y.6
  • 151
    • 0033997927 scopus 로고    scopus 로고
    • Changes in the expression of junctional and nonjunctional complex component genes when inter-Sertoli tight junctions are formed in vitro
    • Wong CC, Chung SS, Grima J et al. Changes in the expression of junctional and nonjunctional complex component genes when inter-Sertoli tight junctions are formed in vitro. J Androl 2000;21(2):227-237. (Pubitemid 30123704)
    • (2000) Journal of Andrology , vol.21 , Issue.2 , pp. 227-237
    • Wong, C.C.S.1    Chung, S.S.W.2    Grima, J.3    Zhu, L.-J.4    Mruk, D.5    Lee, W.M.6    Cheng, C.Y.7
  • 152
    • 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 D, 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(5):747-806. (Pubitemid 39362296)
    • (2004) Endocrine Reviews , vol.25 , Issue.5 , pp. 747-806
    • Mruk, D.D.1    Cheng, C.Y.2
  • 153
    • 0001176886 scopus 로고
    • Etudes sur la structure des tubes séminifères et sur la spermatogenèse chez les mammifères
    • 231-280
    • Regaud C. Etudes sur la structure des tubes séminifères et sur la spermatogenèse chez les mammifères. Arch Anat Microscop Morphol Exp 1901;4:101-156, 231-280.
    • (1901) Arch Anat Microscop Morphol Exp , vol.4 , pp. 101-156
    • Regaud, C.1
  • 154
    • 0040606278 scopus 로고
    • Kinetics of spermatogenesis in mammals
    • Roosen-Runge EC. Kinetics of spermatogenesis in mammals. Ann NY Acad Sci 1952;55(4):574-584.
    • (1952) Ann NY Acad Sci , vol.55 , Issue.4 , pp. 574-584
    • Roosen-Runge, E.C.1
  • 156
    • 0025894111 scopus 로고
    • Study in vitro of the phagocytic function of Sertoli cells in the rat
    • Pineau C, Le Magueresse B, Courtens JL et al. Study in vitro of the phagocytic function of Sertoli cells in the rat. Cell Tissue Res 1991;264(3):589-598.
    • (1991) Cell Tissue Res , vol.264 , Issue.3 , pp. 589-598
    • Pineau, C.1    Le Magueresse, B.2    Courtens, J.L.3
  • 157
    • 0026740931 scopus 로고
    • Lipopolysaccharide, latex beads and residual bodies are potent activators of Sertoli cell interleukin-1 alpha production
    • Gerard N, Syed V, Jegou B. Lipopolysaccharide, latex beads and residual bodies are potent activators of Sertoli cell interleukin-1 alpha production. Biochem Biophys Res Commun 1992;185(1):154-161.
    • (1992) Biochem Biophys Res Commun , vol.185 , Issue.1 , pp. 154-161
    • Gerard, N.1    Syed, V.2    Jegou, B.3
  • 158
    • 0029060690 scopus 로고
    • Residual bodies activate Sertoli cell interleukin-1α (IL-1α) release, which triggers IL-6 production by an autocrine mechanism, through the lipoxygenase pathway
    • Syed V, Stephan JP, Gerard N et al. Residual bodies activate Sertoli cell interleukin-1α (IL-1α) release, which triggers IL-6 production by an autocrine mechanism, through the lipoxygenase pathway. Endocrinology 1995;136(7):3070-3078.
    • (1995) Endocrinology , vol.136 , Issue.7 , pp. 3070-3078
    • Syed, V.1    Stephan, J.P.2    Gerard, N.3
  • 159
    • 0026589413 scopus 로고
    • Testosterone and spermatogenesis. Identification of stage-specific, androgen-regulated proteins secreted by adult rat seminiferous tubules
    • Sharpe RM, Maddocks S, Millar M et al. Testosterone and spermatogenesis. Identification of stage-specific, androgen-regulated proteins secreted by adult rat seminiferous tubules. J Androl 1992;13(2):172-184.
    • (1992) J Androl , vol.13 , Issue.2 , pp. 172-184
    • Sharpe, R.M.1    Maddocks, S.2    Millar, M.3
  • 160
    • 0029787431 scopus 로고    scopus 로고
    • Testosterone withdrawal promotes stage-specific detachment of round spermatids from the rat seminiferous epithelium
    • O'Donnell L, McLachlan RI, Wreford NG et al. Testosterone withdrawal promotes stage-specific detachment of round spermatids from the rat seminiferous epithelium. Biol Reprod 1996;55(4):895-901. (Pubitemid 26304769)
    • (1996) Biology of Reproduction , vol.55 , Issue.4 , pp. 895-901
    • O'Donnell, L.1    McLachlan, R.I.2    Wreford, N.G.3    De Kretser, D.M.4    Robertson, D.M.5
  • 161
    • 0032130798 scopus 로고    scopus 로고
    • Spermatogenesis: Its regulation by testosterone and FSH
    • Zirkin BR. Spermatogenesis: Its regulation by testosterone and FSH. Semin Cell Dev Biol 1998;9(4):417-421. (Pubitemid 128350668)
    • (1998) Seminars in Cell and Developmental Biology , vol.9 , Issue.4 , pp. 417-421
    • Zirkin, B.R.1
  • 162
    • 4544233717 scopus 로고    scopus 로고
    • Intratesticular androgen levels, androgen receptor localization, and androgen receptor expression in adult rat sertoli cells
    • DOI 10.1095/biolreprod.104.029249
    • Hill CM, Anway MD, Zirkin BR et al. Intratesticular androgen levels, androgen receptor localization, and androgen receptor expression in adult rat Sertoli cells. Biol Reprod 2004;71(4):1348-1358. (Pubitemid 39249822)
    • (2004) Biology of Reproduction , vol.71 , Issue.4 , pp. 1348-1358
    • Hill, C.M.1    Anway, M.D.2    Zirkin, B.R.3    Brown, T.R.4
  • 163
    • 0025239553 scopus 로고
    • Androgens inhibit plasminogen activator activity secreted by Sertoli cells in culture in a two-chambered assembly
    • Ailenberg M, McCabe D, Fritz IB. Androgens inhibit plasminogen activator activity secreted by Sertoli cells in culture in a two-chambered assembly. Endocrinology 1990;126(3):1561-1568. (Pubitemid 20095764)
    • (1990) Endocrinology , vol.126 , Issue.3 , pp. 1561-1568
    • Ailenberg, M.1    McGabe, D.2    Fritz, I.B.3
  • 167
    • 0141527550 scopus 로고    scopus 로고
    • Changes in the expression of claudins and transepithelial electrical resistance of mouse Sertoli cells by Leydig cell coculture
    • DOI 10.1046/j.1365-2605.2003.00423.x
    • Gye MC. Changes in the expression of claudins and transepithelial electrical resistance of mouse Sertoli cells by Leydig cell coculture. Int J Androl 2003;26:271-278. (Pubitemid 37211268)
    • (2003) International Journal of Andrology , vol.26 , Issue.5 , pp. 271-278
    • Gye, M.C.1
  • 169
    • 0035958937 scopus 로고    scopus 로고
    • Claudin promotes activation of pro-matrix metalloproteinase-2 mediated by membrane-type matrix metalloproteinases
    • Miyamori H, Takino T, Kobayashi Y et al. Claudin promotes activation of pro-matrix metalloproteinase-2 mediated by membrane-type matrix metalloproteinases. J Biol Chem 2001;276(30):28204-28211.
    • (2001) J Biol Chem , vol.276 , Issue.30 , pp. 28204-28211
    • Miyamori, H.1    Takino, T.2    Kobayashi, Y.3
  • 171
    • 23244457920 scopus 로고    scopus 로고
    • Type IV collagen induces down-regulation of steroidogenic response to gonadotropins in adult rat leydig cells involving mitogen-activated protein kinase
    • DOI 10.1002/mrd.20259
    • Diaz ES, Pellizzari E, Casanova M et al. Type IV collagen induces downregulation of steroidogenic response to gonadotropins in adult rat Leydig cells involving mitogen-activated protein kinase. Mol Reprod Dev 2005;72(2):208-215. (Pubitemid 41099410)
    • (2005) Molecular Reproduction and Development , vol.72 , Issue.2 , pp. 208-215
    • Diaz, E.S.1    Pellizzari, E.2    Casanova, M.3    Cigorraga, S.B.4    Denduchis, B.5
  • 172
    • 2142646426 scopus 로고    scopus 로고
    • TGF-β signaling and the fibrotic response
    • Leask A, Abraham DJ. TGF-β signaling and the fibrotic response. FASEB J 2004;18(7):816-827.
    • (2004) FASEB J , vol.18 , Issue.7 , pp. 816-827
    • Leask, A.1    Abraham, D.J.2
  • 174
    • 0030853418 scopus 로고    scopus 로고
    • Gonadal peptides as mediators of development and functional control of the testis: An integrated system with hormones and local environment
    • DOI 10.1210/er.18.4.541
    • Gnessi L, Fabbri A, Spera G. Gonadal peptides as mediators of development and functional control of the testis: An integrated system with hormones and local environment. Endocr Rev 1997;18(4):541-609. (Pubitemid 27349556)
    • (1997) Endocrine Reviews , vol.18 , Issue.4 , pp. 541-609
    • Gnessi, L.1    Fabbri, A.2    Spera, G.3
  • 176
    • 0031879947 scopus 로고    scopus 로고
    • Pattern of messenger ribonucleic acid expression of tissue inhibitors of metalloproteinases (TIMPs) during testicular maturation in male mice lacking a functional TIMP-1 gene
    • DOI 10.1095/biolreprod59.2.364
    • Nothnick WB, Soloway PD, Curry T E J. Pattern of messenger ribonucleic acid expression of tissue inhibitors of metalloproteinases (TIMPs) during testicular maturation in male mice lacking a functional TIMP-1 gene. Biol Reprod 1998;59(2):364-370. (Pubitemid 28354878)
    • (1998) Biology of Reproduction , vol.59 , Issue.2 , pp. 364-370
    • Nothnick, W.B.1    Soloway, P.D.2    Curry Jr., T.E.3
  • 177
    • 0037307043 scopus 로고    scopus 로고
    • Mice that express enzymatically inactive cathepsin L exhibit abnormal spermatogenesis
    • DOI 10.1095/biolreprod.102.006726
    • Wright WW, Smith L, Kerr C et al. Mice that express enzymatically inactive cathepsin L exhibit abnormal spermatogenesis. Biol Reprod 2003;68:680-687. (Pubitemid 36139337)
    • (2003) Biology of Reproduction , vol.68 , Issue.2 , pp. 680-687
    • Wright, W.W.1    Smith, L.2    Kerr, C.3    Charron, M.4
  • 183
    • 0031930620 scopus 로고    scopus 로고
    • Overexpression of the matrix metalloproteinase matrilysin results in premature mammary gland differentiation and male infertility
    • Rudolph-Owen LA, Cannon P, Matrisian LM. Overexpression of the matrix metalloproteinase matrilysin results in premature mammary gland differentiation and male infertility. Mol Biol Cell 1998;9:421-435. (Pubitemid 28084135)
    • (1998) Molecular Biology of the Cell , vol.9 , Issue.2 , pp. 421-435
    • Rudolph-Owen, L.A.1    Cannon, P.2    Matrisian, L.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.