메뉴 건너뛰기




Volumn 88, Issue 4 SUPPL., 2007, Pages 1049-1057

Male fertility and protein C inhibitor/plasminogen activator inhibitor-3 (PCI): localization of PCI in mouse testis and failure of single plasminogen activator knockout to restore spermatogenesis in PCI-deficient mice

Author keywords

mice; PCI; rescue of infertility; tPA; urokinase

Indexed keywords

PLASMINOGEN ACTIVATOR INHIBITOR 3; TISSUE PLASMINOGEN ACTIVATOR; UROKINASE;

EID: 34848885727     PISSN: 00150282     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.fertnstert.2006.11.193     Document Type: Article
Times cited : (22)

References (48)
  • 1
    • 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 G.A., Bird P.I., Carrell R.W., Church F.C., Coughlin P.B., Gettins P.G., 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 276 (2001) 33293-33296
    • (2001) J Biol Chem , vol.276 , pp. 33293-33296
    • Silverman, G.A.1    Bird, P.I.2    Carrell, R.W.3    Church, F.C.4    Coughlin, P.B.5    Gettins, P.G.6
  • 2
    • 0019166796 scopus 로고
    • Deficiency of protein C inhibitor in combined factor V/VIII deficiency disease
    • Marlar R.A., and Griffin J.H. Deficiency of protein C inhibitor in combined factor V/VIII deficiency disease. J Clin Invest 66 (1980) 1186-1189
    • (1980) J Clin Invest , vol.66 , pp. 1186-1189
    • Marlar, R.A.1    Griffin, J.H.2
  • 3
    • 0020674167 scopus 로고
    • Protein C inhibitor. Purification from human plasma and characterization
    • Suzuki K., Nishioka J., and Hashimoto S. Protein C inhibitor. Purification from human plasma and characterization. J Biol Chem 258 (1983) 163-168
    • (1983) J Biol Chem , vol.258 , pp. 163-168
    • Suzuki, K.1    Nishioka, J.2    Hashimoto, S.3
  • 4
    • 0024425610 scopus 로고
    • Purification and characterization of plasma protein C inhibitor
    • Espana F., Berrettini M., and Griffin J.H. Purification and characterization of plasma protein C inhibitor. Thromb Res 55 (1989) 369-384
    • (1989) Thromb Res , vol.55 , pp. 369-384
    • Espana, F.1    Berrettini, M.2    Griffin, J.H.3
  • 6
    • 0028845757 scopus 로고
    • Protein C inhibitor is a potent inhibitor of the thrombin-thrombomodulin complex
    • Rezaie A.R., Cooper S.T., Church F.C., and Esmon C.T. Protein C inhibitor is a potent inhibitor of the thrombin-thrombomodulin complex. J Biol Chem 270 (1995) 25336-25339
    • (1995) J Biol Chem , vol.270 , pp. 25336-25339
    • Rezaie, A.R.1    Cooper, S.T.2    Church, F.C.3    Esmon, C.T.4
  • 7
    • 0024392128 scopus 로고
    • Complex formation between urokinase and plasma protein C inhibitor in vitro and in vivo
    • Geiger M., Huber K., Wojta J., Stingl L., Espana F., Griffin J.H., et al. Complex formation between urokinase and plasma protein C inhibitor in vitro and in vivo. Blood 74 (1989) 722-728
    • (1989) Blood , vol.74 , pp. 722-728
    • Geiger, M.1    Huber, K.2    Wojta, J.3    Stingl, L.4    Espana, F.5    Griffin, J.H.6
  • 8
    • 0027762119 scopus 로고
    • Evidence for the regulation of urokinase and tissue type plasminogen activators by the serpin, protein C inhibitor, in semen and blood plasma
    • Espana F., Estelles A., Fernandez P.J., Gilabert J., Sanchez-Cuenca J., and Griffin J.H. Evidence for the regulation of urokinase and tissue type plasminogen activators by the serpin, protein C inhibitor, in semen and blood plasma. Thromb Haemost 70 (1993) 989-994
    • (1993) Thromb Haemost , vol.70 , pp. 989-994
    • Espana, F.1    Estelles, A.2    Fernandez, P.J.3    Gilabert, J.4    Sanchez-Cuenca, J.5    Griffin, J.H.6
  • 9
    • 0028232540 scopus 로고
    • Rapid inhibition of the sperm protease acrosin by protein C inhibitor
    • Hermans J.M., Jones R., and Stone S.R. Rapid inhibition of the sperm protease acrosin by protein C inhibitor. Biochemistry 33 (1994) 5440-5444
    • (1994) Biochemistry , vol.33 , pp. 5440-5444
    • Hermans, J.M.1    Jones, R.2    Stone, S.R.3
  • 10
    • 0028008178 scopus 로고
    • Inhibition of acrosin by protein C inhibitor and localization of protein C inhibitor to spermatozoa
    • Zheng X., Geiger M., Ecke S., Bielek E., Donner P., Eberspacher U., et al. Inhibition of acrosin by protein C inhibitor and localization of protein C inhibitor to spermatozoa. Am J Physiol 267 (1994) C466-C472
    • (1994) Am J Physiol , vol.267
    • Zheng, X.1    Geiger, M.2    Ecke, S.3    Bielek, E.4    Donner, P.5    Eberspacher, U.6
  • 11
    • 0026656328 scopus 로고
    • Inhibition of tissue kallikrein by protein C inhibitor. Evidence for identity of protein C inhibitor with the kallikrein binding protein
    • Ecke S., Geiger M., Resch I., Jerabek I., Sting L., Maier M., et al. Inhibition of tissue kallikrein by protein C inhibitor. Evidence for identity of protein C inhibitor with the kallikrein binding protein. J Biol Chem 267 (1992) 7048-7052
    • (1992) J Biol Chem , vol.267 , pp. 7048-7052
    • Ecke, S.1    Geiger, M.2    Resch, I.3    Jerabek, I.4    Sting, L.5    Maier, M.6
  • 12
    • 0025983879 scopus 로고
    • Functionally active protein C inhibitor/plasminogen activator inhibitor-3 (PCI/PAI-3) is secreted in seminal vesicles, occurs at high concentrations in human seminal plasma and complexes with prostate-specific antigen
    • Espana F., Gilabert J., Estelles A., Romeu A., Aznar J., and Cabo A. Functionally active protein C inhibitor/plasminogen activator inhibitor-3 (PCI/PAI-3) is secreted in seminal vesicles, occurs at high concentrations in human seminal plasma and complexes with prostate-specific antigen. Thromb Res 64 (1991) 309-320
    • (1991) Thromb Res , vol.64 , pp. 309-320
    • Espana, F.1    Gilabert, J.2    Estelles, A.3    Romeu, A.4    Aznar, J.5    Cabo, A.6
  • 13
    • 0028078676 scopus 로고
    • Complex formation between protein C inhibitor and prostate-specific antigen in vitro and in human semen
    • Christensson A., and Lilja H. Complex formation between protein C inhibitor and prostate-specific antigen in vitro and in human semen. Eur J Biochem 220 (1994) 45-53
    • (1994) Eur J Biochem , vol.220 , pp. 45-53
    • Christensson, A.1    Lilja, H.2
  • 14
    • 0026654795 scopus 로고
    • Protein C inhibitor in human body fluids. Seminal plasma is rich in inhibitor antigen deriving from cells throughout the male reproductive system
    • Laurell M., Christensson A., Abrahamsson P.A., Stenflo J., and Lilja H. Protein C inhibitor in human body fluids. Seminal plasma is rich in inhibitor antigen deriving from cells throughout the male reproductive system. J Clin Invest 89 (1992) 1094-1101
    • (1992) J Clin Invest , vol.89 , pp. 1094-1101
    • Laurell, M.1    Christensson, A.2    Abrahamsson, P.A.3    Stenflo, J.4    Lilja, H.5
  • 15
    • 0034523885 scopus 로고    scopus 로고
    • Disruption of the protein C inhibitor gene results in impaired spermatogenesis and male infertility
    • Uhrin P., Dewerchin M., Hilpert M., Chrenek P., Schofer C., Zechmeister-Machhart M., et al. Disruption of the protein C inhibitor gene results in impaired spermatogenesis and male infertility. J Clin Invest 106 (2000) 1531-1539
    • (2000) J Clin Invest , vol.106 , pp. 1531-1539
    • Uhrin, P.1    Dewerchin, M.2    Hilpert, M.3    Chrenek, P.4    Schofer, C.5    Zechmeister-Machhart, M.6
  • 16
    • 0035047037 scopus 로고    scopus 로고
    • Is cadmium chloride-induced inter-Sertoli tight junction permeability barrier disruption a suitable in vitro model to study the events of junction disassembly during spermatogenesis in the rat testis?
    • Chung N.P., and Cheng C.Y. Is cadmium chloride-induced inter-Sertoli tight junction permeability barrier disruption a suitable in vitro model to study the events of junction disassembly during spermatogenesis in the rat testis?. Endocrinology 142 (2001) 1878-1888
    • (2001) Endocrinology , vol.142 , pp. 1878-1888
    • Chung, N.P.1    Cheng, C.Y.2
  • 17
    • 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 C.C., Chung S.S., Grima J., Zhu L.J., Mruk D., Lee W.M., et al. Changes in the expression of junctional and nonjunctional complex component genes when inter-Sertoli tight junctions are formed in vitro. J Androl 21 (2000) 227-237
    • (2000) J Androl , vol.21 , pp. 227-237
    • Wong, C.C.1    Chung, S.S.2    Grima, J.3    Zhu, L.J.4    Mruk, D.5    Lee, W.M.6
  • 18
    • 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 L.J., Silvestrini B., Lee W.M., and Cheng C.Y. Interactions of proteases and protease inhibitors in Sertoli-germ cell cocultures preceding the formation of specialized Sertoli-germ cell junctions in vitro. J Androl 18 (1997) 612-622
    • (1997) J Androl , vol.18 , pp. 612-622
    • Mruk, D.1    Zhu, L.J.2    Silvestrini, B.3    Lee, W.M.4    Cheng, C.Y.5
  • 19
    • 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 K.K., Kristensen P., Dano K., and Parvinen M. 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 126 (1988) 150-155
    • (1988) Dev Biol , vol.126 , pp. 150-155
    • Vihko, K.K.1    Kristensen, P.2    Dano, K.3    Parvinen, M.4
  • 20
    • 1442299093 scopus 로고    scopus 로고
    • Evidence for similar expression of protein C inhibitor and the urokinase-type plasminogen activator system during mouse testis development
    • Odet F., Guyot R., Leduque P., and Magueresse-Battistoni B. Evidence for similar expression of protein C inhibitor and the urokinase-type plasminogen activator system during mouse testis development. Endocrinology 145 (2004) 1481-1489
    • (2004) Endocrinology , vol.145 , pp. 1481-1489
    • Odet, F.1    Guyot, R.2    Leduque, P.3    Magueresse-Battistoni, B.4
  • 21
    • 0032531051 scopus 로고    scopus 로고
    • Development and disease in proteinase-deficient mice: role of the plasminogen, matrix metalloproteinase and coagulation system
    • Carmeliet P., and Collen D. Development and disease in proteinase-deficient mice: role of the plasminogen, matrix metalloproteinase and coagulation system. Thromb Res 91 (1998) 255-285
    • (1998) Thromb Res , vol.91 , pp. 255-285
    • Carmeliet, P.1    Collen, D.2
  • 22
    • 0028102361 scopus 로고
    • Localization of urokinase- and tissue-type plasminogen activator mRNAs in rat testes
    • Penttila T.L., Kaipia A., Toppari J., Parvinen M., and Mali P. Localization of urokinase- and tissue-type plasminogen activator mRNAs in rat testes. Mol Cell Endocrinol 105 (1994) 55-64
    • (1994) Mol Cell Endocrinol , vol.105 , pp. 55-64
    • Penttila, T.L.1    Kaipia, A.2    Toppari, J.3    Parvinen, M.4    Mali, P.5
  • 23
    • 0030852031 scopus 로고    scopus 로고
    • The receptor for urokinase-type plasminogen activator is expressed during mouse spermatogenesis
    • Zhou H., and Vassalli J.D. The receptor for urokinase-type plasminogen activator is expressed during mouse spermatogenesis. FEBS Lett 413 (1997) 11-15
    • (1997) FEBS Lett , vol.413 , pp. 11-15
    • Zhou, H.1    Vassalli, J.D.2
  • 24
    • 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
    • Huarte J., Belin D., Bosco D., Sappino A.P., and Vassalli J.D. 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 104 (1987) 1281-1289
    • (1987) J Cell Biol , vol.104 , pp. 1281-1289
    • Huarte, J.1    Belin, D.2    Bosco, D.3    Sappino, A.P.4    Vassalli, J.D.5
  • 26
    • 0025760576 scopus 로고
    • Human seminal fibrinolytic activity: specific determinations of tissue plasminogen activator and urokinase
    • Van Dreden P., Gonzales J., and Poirot C. Human seminal fibrinolytic activity: specific determinations of tissue plasminogen activator and urokinase. Andrologia 23 (1991) 29-33
    • (1991) Andrologia , vol.23 , pp. 29-33
    • Van Dreden, P.1    Gonzales, J.2    Poirot, C.3
  • 27
    • 0032973947 scopus 로고    scopus 로고
    • Functionally inactive protein C inhibitor in seminal plasma may be associated with infertility
    • He S., Lin Y.L., and Liu Y.X. Functionally inactive protein C inhibitor in seminal plasma may be associated with infertility. Mol Hum Reprod 5 (1999) 513-519
    • (1999) Mol Hum Reprod , vol.5 , pp. 513-519
    • He, S.1    Lin, Y.L.2    Liu, Y.X.3
  • 28
    • 0028295979 scopus 로고
    • Physiological consequences of loss of plasminogen activator gene function in mice
    • Carmeliet P., Schoonjans L., Kieckens L., Ream B., Degen J., Bronson R., et al. Physiological consequences of loss of plasminogen activator gene function in mice. Nature 368 (1994) 419-424
    • (1994) Nature , vol.368 , pp. 419-424
    • Carmeliet, P.1    Schoonjans, L.2    Kieckens, L.3    Ream, B.4    Degen, J.5    Bronson, R.6
  • 29
    • 20244375372 scopus 로고    scopus 로고
    • Characterization of transgenic mice that secrete functional human protein C inhibitor into the circulation
    • Wagenaar G.T., van Vuuren A.J., Girma M., Tiekstra M.J., Kwast L., Koster J.G., et al. Characterization of transgenic mice that secrete functional human protein C inhibitor into the circulation. Thromb Haemost 83 (2000) 93-101
    • (2000) Thromb Haemost , vol.83 , pp. 93-101
    • Wagenaar, G.T.1    van Vuuren, A.J.2    Girma, M.3    Tiekstra, M.J.4    Kwast, L.5    Koster, J.G.6
  • 30
    • 0001333357 scopus 로고
    • Calendar of gametogenic development in the prepuberal male mouse
    • Nebel B.R., Marose A.P., and Hacket E.M. Calendar of gametogenic development in the prepuberal male mouse. Science 134 (1961) 832-833
    • (1961) Science , vol.134 , pp. 832-833
    • Nebel, B.R.1    Marose, A.P.2    Hacket, E.M.3
  • 31
    • 23844470846 scopus 로고    scopus 로고
    • Protein C inhibitor expression by adult rat sertoli cells: effects of testosterone withdrawal and replacement
    • Anway M.D., Show M.D., and Zirkin B.R. Protein C inhibitor expression by adult rat sertoli cells: effects of testosterone withdrawal and replacement. J Androl 26 (2005) 578-585
    • (2005) J Androl , vol.26 , pp. 578-585
    • Anway, M.D.1    Show, M.D.2    Zirkin, B.R.3
  • 32
    • 3142769033 scopus 로고    scopus 로고
    • The murine testicular transcriptome: characterizing gene expression in the testis during the progression of spermatogenesis
    • Shima J.E., McLean D.J., McCarrey J.R., and Griswold M.D. The murine testicular transcriptome: characterizing gene expression in the testis during the progression of spermatogenesis. Biol Reprod 71 (2004) 319-330
    • (2004) Biol Reprod , vol.71 , pp. 319-330
    • Shima, J.E.1    McLean, D.J.2    McCarrey, J.R.3    Griswold, M.D.4
  • 33
    • 4644328373 scopus 로고    scopus 로고
    • Dynamic cross-talk between cells and the extracellular matrix in the testis
    • Siu M.K., and Cheng C.Y. Dynamic cross-talk between cells and the extracellular matrix in the testis. Bioessays 26 (2004) 978-992
    • (2004) Bioessays , vol.26 , pp. 978-992
    • Siu, M.K.1    Cheng, C.Y.2
  • 34
    • 0029610066 scopus 로고
    • Ovulation efficiency is reduced in mice that lack plasminogen activator gene function: functional redundancy among physiological plasminogen activators
    • Leonardsson G., Peng X.R., Liu K., Nordstrom L., Carmeliet P., Mulligan R., et al. Ovulation efficiency is reduced in mice that lack plasminogen activator gene function: functional redundancy among physiological plasminogen activators. Proc Natl Acad Sci U S A 92 (1995) 12446-12450
    • (1995) Proc Natl Acad Sci U S A , vol.92 , pp. 12446-12450
    • Leonardsson, G.1    Peng, X.R.2    Liu, K.3    Nordstrom, L.4    Carmeliet, P.5    Mulligan, R.6
  • 35
    • 0033118244 scopus 로고    scopus 로고
    • Cloning and structural analysis of leydin, a novel human serine protease expressed by the Leydig cells of the testis
    • Poorafshar M., and Hellman L. Cloning and structural analysis of leydin, a novel human serine protease expressed by the Leydig cells of the testis. Eur J Biochem 261 (1999) 244-250
    • (1999) Eur J Biochem , vol.261 , pp. 244-250
    • Poorafshar, M.1    Hellman, L.2
  • 36
    • 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
    • Honda A., Yamagata K., Sugiura S., Watanabe K., and Baba T. A mouse serine protease TESP5 is selectively included into lipid rafts of sperm membrane presumably as a glycosylphosphatidylinositol-anchored protein. J Biol Chem 277 (2002) 16976-16984
    • (2002) J Biol Chem , vol.277 , pp. 16976-16984
    • Honda, A.1    Yamagata, K.2    Sugiura, S.3    Watanabe, K.4    Baba, T.5
  • 37
    • 0033168561 scopus 로고    scopus 로고
    • Testisin, a new human serine proteinase expressed by premeiotic testicular germ cells and lost in testicular germ cell tumors
    • Hooper J.D., Nicol D.L., Dickinson J.L., Eyre H.J., Scarman A.L., Normyle J.F., et al. Testisin, a new human serine proteinase expressed by premeiotic testicular germ cells and lost in testicular germ cell tumors. Cancer Res 59 (1999) 3199-3205
    • (1999) Cancer Res , vol.59 , pp. 3199-3205
    • Hooper, J.D.1    Nicol, D.L.2    Dickinson, J.L.3    Eyre, H.J.4    Scarman, A.L.5    Normyle, J.F.6
  • 38
    • 0035078575 scopus 로고    scopus 로고
    • Organization and chromosomal localization of the murine Testisin gene encoding a serine protease temporally expressed during spermatogenesis
    • Scarman A.L., Hooper J.D., Boucaut K.J., Sit M.L., Webb G.C., Normyle J.F., et al. Organization and chromosomal localization of the murine Testisin gene encoding a serine protease temporally expressed during spermatogenesis. Eur J Biochem 268 (2001) 1250-1258
    • (2001) Eur J Biochem , vol.268 , pp. 1250-1258
    • Scarman, A.L.1    Hooper, J.D.2    Boucaut, K.J.3    Sit, M.L.4    Webb, G.C.5    Normyle, J.F.6
  • 39
    • 0032576956 scopus 로고    scopus 로고
    • Two novel testicular serine proteases, TESP1 and TESP2, are present in the mouse sperm acrosome
    • Kohno N., Yamagata K., Yamada S., Kashiwabara S., Sakai Y., and Baba T. Two novel testicular serine proteases, TESP1 and TESP2, are present in the mouse sperm acrosome. Biochem Biophys Res Commun 245 (1998) 658-665
    • (1998) Biochem Biophys Res Commun , vol.245 , pp. 658-665
    • Kohno, N.1    Yamagata, K.2    Yamada, S.3    Kashiwabara, S.4    Sakai, Y.5    Baba, T.6
  • 40
    • 0033593530 scopus 로고    scopus 로고
    • Mammalian fertilization: molecular aspects of gamete adhesion, exocytosis, and fusion
    • Wassarman P.M. Mammalian fertilization: molecular aspects of gamete adhesion, exocytosis, and fusion. Cell 96 (1999) 175-183
    • (1999) Cell , vol.96 , pp. 175-183
    • Wassarman, P.M.1
  • 41
    • 0032883785 scopus 로고    scopus 로고
    • A homologue of pancreatic trypsin is localized in the acrosome of mammalian sperm and is released during acrosome reaction
    • Ohmura K., Kohno N., Kobayashi Y., Yamagata K., Sato S., Kashiwabara S., et al. A homologue of pancreatic trypsin is localized in the acrosome of mammalian sperm and is released during acrosome reaction. J Biol Chem 274 (1999) 29426-29432
    • (1999) J Biol Chem , vol.274 , pp. 29426-29432
    • Ohmura, K.1    Kohno, N.2    Kobayashi, Y.3    Yamagata, K.4    Sato, S.5    Kashiwabara, S.6
  • 42
    • 8744227027 scopus 로고    scopus 로고
    • Mouse DESC1 is located within a cluster of seven DESC1-like genes and encodes a type II transmembrane serine protease that forms serpin inhibitory complexes
    • Hobson J.P., Netzel-Arnett S., Szabo R., Rehault S.M., Church F.C., et al. Mouse DESC1 is located within a cluster of seven DESC1-like genes and encodes a type II transmembrane serine protease that forms serpin inhibitory complexes. J Biol Chem 279 (2004) 46981-46994
    • (2004) J Biol Chem , vol.279 , pp. 46981-46994
    • Hobson, J.P.1    Netzel-Arnett, S.2    Szabo, R.3    Rehault, S.M.4    Church, F.C.5
  • 43
    • 23944450595 scopus 로고    scopus 로고
    • Matriptase-3 is a novel phylogenetically preserved membrane-anchored serine protease with broad serpin reactivity
    • Szabo R., Netzel-Arnett S., Hobson J.P., Antalis T.M., and Bugge T.H. Matriptase-3 is a novel phylogenetically preserved membrane-anchored serine protease with broad serpin reactivity. Biochem J 390 (2005) 231-242
    • (2005) Biochem J , vol.390 , pp. 231-242
    • Szabo, R.1    Netzel-Arnett, S.2    Hobson, J.P.3    Antalis, T.M.4    Bugge, T.H.5
  • 44
    • 0027415898 scopus 로고
    • Human sperm-egg binding is inhibited by peptides corresponding to core region of an acrosomal serine protease inhibitor
    • Moore A., Penfold L.M., Johnson J.L., Latchman D.S., and Moore H.D. Human sperm-egg binding is inhibited by peptides corresponding to core region of an acrosomal serine protease inhibitor. Mol Reprod Dev 34 (1993) 280-291
    • (1993) Mol Reprod Dev , vol.34 , pp. 280-291
    • Moore, A.1    Penfold, L.M.2    Johnson, J.L.3    Latchman, D.S.4    Moore, H.D.5
  • 45
    • 0027420389 scopus 로고
    • The cytoplasmic droplet of rat epididymal spermatozoa contains saccular elements with Golgi characteristics
    • Oko R., Hermo L., Chan P.T., Fazel A., and Bergeron J.J. The cytoplasmic droplet of rat epididymal spermatozoa contains saccular elements with Golgi characteristics. J Cell Biol 123 (1993) 809-821
    • (1993) J Cell Biol , vol.123 , pp. 809-821
    • Oko, R.1    Hermo, L.2    Chan, P.T.3    Fazel, A.4    Bergeron, J.J.5
  • 47
    • 0037405925 scopus 로고    scopus 로고
    • Acquisition of volume regulatory response of sperm upon maturation in the epididymis and the role of the cytoplasmic droplet
    • Cooper T.G., and Yeung C.H. Acquisition of volume regulatory response of sperm upon maturation in the epididymis and the role of the cytoplasmic droplet. Microsc Res Tech 61 (2003) 28-38
    • (2003) Microsc Res Tech , vol.61 , pp. 28-38
    • Cooper, T.G.1    Yeung, C.H.2
  • 48
    • 0035919207 scopus 로고    scopus 로고
    • Origin, differentiation and regulation of fetal and adult Leydig cells
    • Habert R., Lejeune H., and Saez J.M. Origin, differentiation and regulation of fetal and adult Leydig cells. Mol Cell Endocrinol 179 (2001) 47-74
    • (2001) Mol Cell Endocrinol , vol.179 , pp. 47-74
    • Habert, R.1    Lejeune, H.2    Saez, J.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.