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Volumn 139, Issue 5, 1998, Pages 2314-2321

Elevated expression of lanosterol 14α-demethylase (CYP51) and the synthesis of oocyte meiosis-activating sterois in postmeiotic germ cells of male rats

Author keywords

[No Author keywords available]

Indexed keywords

CREATINE KINASE; CYTOCHROME P450; DIHYDROLANOSTEROL; LACTATE DEHYDROGENASE; LANOSTEROL; MESSENGER RNA; SQUALENE SYNTHASE; STEROL; STEROL 14ALPHA DEMETHYLASE; UNCLASSIFIED DRUG;

EID: 0031763463     PISSN: 00137227     EISSN: None     Source Type: Journal    
DOI: 10.1210/endo.139.5.5984     Document Type: Article
Times cited : (52)

References (51)
  • 1
    • 0021717363 scopus 로고
    • Cytochrome P-450-dependent oxidation of lanosterol in cholesterol biosynthesis
    • Trzaskos JM, Bowen WD, Shafiee A, Fischer RT, Gaylor JL 1984 Cytochrome P-450-dependent oxidation of lanosterol in cholesterol biosynthesis. J Biol Chem 259:13402-13412
    • (1984) J Biol Chem , vol.259 , pp. 13402-13412
    • Trzaskos, J.M.1    Bowen, W.D.2    Shafiee, A.3    Fischer, R.T.4    Gaylor, J.L.5
  • 2
    • 0011837288 scopus 로고
    • Plant sterol biosynthesis: Recent advances in the understanding of oxidative demethylations at C4 and C14
    • Taton M, Salmon F, Pascal S, Rahier A 1994 Plant sterol biosynthesis: recent advances in the understanding of oxidative demethylations at C4 and C14. Plant Physiol Biochem 32:751-760
    • (1994) Plant Physiol Biochem , vol.32 , pp. 751-760
    • Taton, M.1    Salmon, F.2    Pascal, S.3    Rahier, A.4
  • 3
    • 0017893275 scopus 로고
    • Interaction of lanosterol to cytochrome P-450 purified from yeast microsomes: Evidence for contribution of cytochrome P-450 to lanosterol metabolism
    • Aoyama Y, Yoshida Y 1978 Interaction of lanosterol to cytochrome P-450 purified from yeast microsomes: evidence for contribution of cytochrome P-450 to lanosterol metabolism. Biochem Biophys Res Commun 82:33-38
    • (1978) Biochem Biophys Res Commun , vol.82 , pp. 33-38
    • Aoyama, Y.1    Yoshida, Y.2
  • 5
    • 0023498489 scopus 로고
    • Primary structure of the P450 lanosterol demethylase gene from Saccharomyces cerevisiae
    • Kalb VF, Woods CW, Turi TG, Dey CR, Sutter TR, Loper JC 1987 Primary structure of the P450 lanosterol demethylase gene from Saccharomyces cerevisiae. DNA 6:529-537
    • (1987) DNA , vol.6 , pp. 529-537
    • Kalb, V.F.1    Woods, C.W.2    Turi, T.G.3    Dey, C.R.4    Sutter, T.R.5    Loper, J.C.6
  • 6
    • 0024114790 scopus 로고
    • Primary structure of the cytochrome P450 lanosterol 14α-demethylase gene from Candida tropicalis
    • Chen C, Kalb VF, Turi TG, Loper JC 1988 Primary structure of the cytochrome P450 lanosterol 14α-demethylase gene from Candida tropicalis. DNA 7:617-626
    • (1988) DNA , vol.7 , pp. 617-626
    • Chen, C.1    Kalb, V.F.2    Turi, T.G.3    Loper, J.C.4
  • 7
    • 0024595561 scopus 로고
    • Nucleotide sequence of cytochrome P450LIA1 (lanosterol 14α-demethylase) from Candida albicans
    • Lai MH, Kirsch DR 1989 Nucleotide sequence of cytochrome P450LIA1 (lanosterol 14α-demethylase) from Candida albicans. Nucleic Acids Res 17:804
    • (1989) Nucleic Acids Res , vol.17 , pp. 804
    • Lai, M.H.1    Kirsch, D.R.2
  • 8
    • 0028302301 scopus 로고
    • Rapid detection and identification of Candida albicans and Torulopsis (Candida) glabrata in clinical specimens by species-specific nested PCR amplification of a cytochrome P-450 lanosterol-14α-demethylase (LIA1) gene fragment
    • Burgener-Kairuz P, Zuber JP, Jaunin P, Buchman TG, Bille J, Rossier M 1994 Rapid detection and identification of Candida albicans and Torulopsis (Candida) glabrata in clinical specimens by species-specific nested PCR amplification of a cytochrome P-450 lanosterol-14α-demethylase (LIA1) gene fragment. J Clin Microbiol 32:1902-1907
    • (1994) J Clin Microbiol , vol.32 , pp. 1902-1907
    • Burgener-Kairuz, P.1    Zuber, J.P.2    Jaunin, P.3    Buchman, T.G.4    Bille, J.5    Rossier, M.6
  • 10
    • 0031079568 scopus 로고    scopus 로고
    • Cloning and expression in Escherichia coli of the obtusifoliol 14α-demethylase of Sorghum bicolor (L.) Moench, a cytochrome P450 orthologous to the sterol 14α-demethylases (CYP51) from fungi and mammals
    • Bak S, Kahn RA, Olsen C-E, Halkier BA 1997 Cloning and expression in Escherichia coli of the obtusifoliol 14α-demethylase of Sorghum bicolor (L.) Moench, a cytochrome P450 orthologous to the sterol 14α-demethylases (CYP51) from fungi and mammals. Plant J 11:191-201
    • (1997) Plant J , vol.11 , pp. 191-201
    • Bak, S.1    Kahn, R.A.2    Olsen, C.-E.3    Halkier, B.A.4
  • 12
    • 0028021959 scopus 로고
    • Occurrence of a P450 showing high homology to yeast lanosterol 14α-demethylase (P45014DM) in the rat liver
    • Aoyama Y, Funae Y, Noshiro M, Horiuchi, T Yoshida Y 1994 Occurrence of a P450 showing high homology to yeast lanosterol 14α-demethylase (P45014DM) in the rat liver. Biochem Biophys Res Commun 201:1320-1326
    • (1994) Biochem Biophys Res Commun , vol.201 , pp. 1320-1326
    • Aoyama, Y.1    Funae, Y.2    Noshiro, M.3    Horiuchi, T.4    Yoshida, Y.5
  • 14
    • 0029974620 scopus 로고    scopus 로고
    • The ubiquitously expressed human CYP51 encodes lanosterol 14α-demethylase, a cytochrome P450 whose expression is regulated by oxysterols
    • Strömstedt M, Rozman D, Waterman MR 1996 The ubiquitously expressed human CYP51 encodes lanosterol 14α-demethylase, a cytochrome P450 whose expression is regulated by oxysterols. Arch Biochem Biophys 329:73-81
    • (1996) Arch Biochem Biophys , vol.329 , pp. 73-81
    • Strömstedt, M.1    Rozman, D.2    Waterman, M.R.3
  • 16
    • 0030587538 scopus 로고    scopus 로고
    • The three human cytochrome P450 lanosterol 14α-demethylase (CYP51) genes reside on chromosomes 3, 7 and 13: Structure of the two retrotransposed pseudogenes, association with a LINE-1 element and evolution of the human CYP51 family
    • Rozman D, Strömstedt M, Waterman MR 1996 The three human cytochrome P450 lanosterol 14α-demethylase (CYP51) genes reside on chromosomes 3, 7 and 13: structure of the two retrotransposed pseudogenes, association with a LINE-1 element and evolution of the human CYP51 family. Arch Biochem Biophys 333:466-474
    • (1996) Arch Biochem Biophys , vol.333 , pp. 466-474
    • Rozman, D.1    Strömstedt, M.2    Waterman, M.R.3
  • 17
    • 0030589679 scopus 로고    scopus 로고
    • Structure and mapping of the human lanosterol 14α-demethylase gene (CYP51) encoding the cytochrome P450 involved in cholesterol biosynthesis; comparison of exon/intron organization with other mammalian and fungal CYP genes
    • Rozman D, Strömstedt M, Tsui L-C, Scherer SW, Waterman MR 1996 Structure and mapping of the human lanosterol 14α-demethylase gene (CYP51) encoding the cytochrome P450 involved in cholesterol biosynthesis; comparison of exon/intron organization with other mammalian and fungal CYP genes. Genomics 38:371-381
    • (1996) Genomics , vol.38 , pp. 371-381
    • Rozman, D.1    Strömstedt, M.2    Tsui, L.-C.3    Scherer, S.W.4    Waterman, M.R.5
  • 19
    • 0022293979 scopus 로고
    • Processed pseudogenes: Characteristics and evolution
    • Vanin EF 1985 Processed pseudogenes: characteristics and evolution. Annu Rev Genet 19:253-272
    • (1985) Annu Rev Genet , vol.19 , pp. 253-272
    • Vanin, E.F.1
  • 20
    • 0025120211 scopus 로고
    • Regulation of the mevalonate pathway
    • Goldstein JL, Brown MS 1990 Regulation of the mevalonate pathway. Nature 343:425-430
    • (1990) Nature , vol.343 , pp. 425-430
    • Goldstein, J.L.1    Brown, M.S.2
  • 22
    • 0025316621 scopus 로고
    • Subunits of cyclic adenosine 3′,5′-monophosphate-dependent protein kinase show differential and distinct expression patterns during germ cell differentiation: Alternative polyadenylation in germ cells gives rise to unique smaller sized mRNA species
    • Øyen O, Mykleburst F, Scott JD, Gadd GG, McKnight GS, Hansson V, Jahnsen T 1990 Subunits of cyclic adenosine 3′,5′-monophosphate-dependent protein kinase show differential and distinct expression patterns during germ cell differentiation: alternative polyadenylation in germ cells gives rise to unique smaller sized mRNA species. Biol Reprod 43:46-54
    • (1990) Biol Reprod , vol.43 , pp. 46-54
    • Øyen, O.1    Mykleburst, F.2    Scott, J.D.3    Gadd, G.G.4    McKnight, G.S.5    Hansson, V.6    Jahnsen, T.7
  • 23
    • 0023447556 scopus 로고
    • Cellular localization and age-dependent changes in mRNA for cyclic adenosine 3′,5′-monophosphate-dependent protein kinases in rat testis
    • Øyen O, Froysa A, Sandberg M, Eskild W, Joseph D, Hansson V, Jahnsen T 1987 Cellular localization and age-dependent changes in mRNA for cyclic adenosine 3′,5′-monophosphate-dependent protein kinases in rat testis. Biol Reprod 37:947-956
    • (1987) Biol Reprod , vol.37 , pp. 947-956
    • Øyen, O.1    Froysa, A.2    Sandberg, M.3    Eskild, W.4    Joseph, D.5    Hansson, V.6    Jahnsen, T.7
  • 26
    • 0026808513 scopus 로고
    • Molecular cloning, expression, and characterization of the cDNA for the rat hepatic squalene synthase
    • McKenzie TL, Jiang G, Straubhaar JR, Conrad DG, Schechter I 1992 Molecular cloning, expression, and characterization of the cDNA for the rat hepatic squalene synthase. J Biol Chem 267:21368-21374
    • (1992) J Biol Chem , vol.267 , pp. 21368-21374
    • McKenzie, T.L.1    Jiang, G.2    Straubhaar, J.R.3    Conrad, D.G.4    Schechter, I.5
  • 28
    • 0029064861 scopus 로고
    • Cholesterol side-chain cleavage cytochrome P450 gene expression in the primitive gut of the mouse embryo does not require steroidogenic factor 1
    • Keeney DS, Ikeda Y, Waterman MR, Parker KL 1995 Cholesterol side-chain cleavage cytochrome P450 gene expression in the primitive gut of the mouse embryo does not require steroidogenic factor 1. Mol Endocrinol 9:1091-1098
    • (1995) Mol Endocrinol , vol.9 , pp. 1091-1098
    • Keeney, D.S.1    Ikeda, Y.2    Waterman, M.R.3    Parker, K.L.4
  • 29
    • 0015605558 scopus 로고
    • Cellular composition of fractions of mouse testis following velocity sedimentation separation
    • Meistrich ML, Bruce WR, Clermont Y 1973 Cellular composition of fractions of mouse testis following velocity sedimentation separation. Exp Cell Res 79:213-227
    • (1973) Exp Cell Res , vol.79 , pp. 213-227
    • Meistrich, M.L.1    Bruce, W.R.2    Clermont, Y.3
  • 30
    • 0009732037 scopus 로고
    • Definition of the stages of the cycle of the seminiferous epithelium in the rat
    • Leblond CP, Clermont Y 1952 Definition of the stages of the cycle of the seminiferous epithelium in the rat. Ann NY Acad Sci 55:548-573
    • (1952) Ann NY Acad Sci , vol.55 , pp. 548-573
    • Leblond, C.P.1    Clermont, Y.2
  • 31
    • 0015450727 scopus 로고
    • Identification and enzyme quantitation of the stages of the seminiferous epithelial wave in the rat
    • Parvinen M, Vanha-Perttula T 1972 Identification and enzyme quantitation of the stages of the seminiferous epithelial wave in the rat. Anat Rev 174:435-450
    • (1972) Anat Rev , vol.174 , pp. 435-450
    • Parvinen, M.1    Vanha-Perttula, T.2
  • 32
    • 84987485510 scopus 로고
    • Endogenous steroids in rat seminiferous tubules. Comparison of the stages of the epithelial cycle isolated by transillumination-assisted microdissection
    • Parvinen M, Ruokonen A 1982 Endogenous steroids in rat seminiferous tubules. Comparison of the stages of the epithelial cycle isolated by transillumination-assisted microdissection. J Androl 3:211-220
    • (1982) J Androl , vol.3 , pp. 211-220
    • Parvinen, M.1    Ruokonen, A.2
  • 33
    • 0027503273 scopus 로고
    • Incomplete development of human spermatozoa is associated with increased creatine phosphokinase concentration and abnormal head morphology
    • Huszar G, Vigue L 1993 Incomplete development of human spermatozoa is associated with increased creatine phosphokinase concentration and abnormal head morphology. Mol Reprod Dev 34:292-298
    • (1993) Mol Reprod Dev , vol.34 , pp. 292-298
    • Huszar, G.1    Vigue, L.2
  • 34
    • 3142574556 scopus 로고    scopus 로고
    • Biochemical markers of early and late spermatogenesis: Relationship between the lactate dehydrogenase-X and creatine kinase-M isoform concentrations in human spermatozoa
    • Lalwani S, Sayme N, Vigue L, Corrales M, Huzar G 1996 Biochemical markers of early and late spermatogenesis: relationship between the lactate dehydrogenase-X and creatine kinase-M isoform concentrations in human spermatozoa. Mol Reprod Dev 43:495-502
    • (1996) Mol Reprod Dev , vol.43 , pp. 495-502
    • Lalwani, S.1    Sayme, N.2    Vigue, L.3    Corrales, M.4    Huzar, G.5
  • 35
    • 0024515672 scopus 로고
    • Different activity and synthesys of lactate dehydrogenase isozymes A (muscle), and C (testis) in mouse spermatogenic cells
    • Li S-L, O'Brien DA, Hou EW, Versola J, Rockett DL, Eddy EM 1989 Different activity and synthesys of lactate dehydrogenase isozymes A (muscle), and C (testis) in mouse spermatogenic cells. Biol Reprod 40:173-180
    • (1989) Biol Reprod , vol.40 , pp. 173-180
    • Li, S.-L.1    O'Brien, D.A.2    Hou, E.W.3    Versola, J.4    Rockett, D.L.5    Eddy, E.M.6
  • 36
    • 0029844192 scopus 로고    scopus 로고
    • Cholesterol modification of hedgehog signalling proteins in animal development
    • Porter JA, Zoung KE, Beachy PA 1996 Cholesterol modification of hedgehog signalling proteins in animal development. Science 274:255-259
    • (1996) Science , vol.274 , pp. 255-259
    • Porter, J.A.1    Zoung, K.E.2    Beachy, P.A.3
  • 37
    • 9544223310 scopus 로고    scopus 로고
    • Emopamil-binding protein, a mammalian protein that binds a series of structurally diverse neuroprotective agents, exhibits Δ8-Δ7 sterol isomerase activity
    • Silve S, Dupuy PH, Labit-Leboutellier C, Kaghad M, Chalon P, Raiher A, Taton M, Lupker J, Shire D, Loison G 1996 Emopamil-binding protein, a mammalian protein that binds a series of structurally diverse neuroprotective agents, exhibits Δ8-Δ7 sterol isomerase activity. J Biol Chem 37:22434-22440
    • (1996) J Biol Chem , vol.37 , pp. 22434-22440
    • Silve, S.1    Dupuy, P.H.2    Labit-Leboutellier, C.3    Kaghad, M.4    Chalon, P.5    Raiher, A.6    Taton, M.7    Lupker, J.8    Shire, D.9    Loison, G.10
  • 39
    • 0024687825 scopus 로고
    • Protamine 3′-untranslated sequences regulate temporal translational control and subcellular localization of growth hormone in spermatids of transgenic mice
    • Braun RE, Peschon JJ, Behringer RR, Brinster RL 1989 Protamine 3′-untranslated sequences regulate temporal translational control and subcellular localization of growth hormone in spermatids of transgenic mice. Genes Dev 3:793-802
    • (1989) Genes Dev , vol.3 , pp. 793-802
    • Braun, R.E.1    Peschon, J.J.2    Behringer, R.R.3    Brinster, R.L.4
  • 40
    • 0025806761 scopus 로고
    • Cytoplasmic protein binding to highly conserved sequences in the 3′-untranslated region of the mouse protamine 2 mRNA, a translationally regulated transcript of male germ cells
    • Kwon YK, Hecht NB 1991 Cytoplasmic protein binding to highly conserved sequences in the 3′-untranslated region of the mouse protamine 2 mRNA, a translationally regulated transcript of male germ cells. Proc Natl Acad Sci USA 88:3584-3588
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 3584-3588
    • Kwon, Y.K.1    Hecht, N.B.2
  • 41
    • 0025320076 scopus 로고
    • Testis-specific transcription initiation sites of rat farnesyl pyrophosphate synthetase mRNA
    • Teruya JH, Kutsunai DHS, Edwards PA, Clarke CF 1990 Testis-specific transcription initiation sites of rat farnesyl pyrophosphate synthetase mRNA. Mo Cell Biol 10:2315-2326
    • (1990) Mo Cell Biol , vol.10 , pp. 2315-2326
    • Teruya, J.H.1    Kutsunai, D.H.S.2    Edwards, P.A.3    Clarke, C.F.4
  • 42
    • 0028988016 scopus 로고
    • 3′-end cleavage and polyadenilation of mRNA precursors
    • Wahle E 1995 3′-end cleavage and polyadenilation of mRNA precursors. Biochim Biophys Acta 1261:183-194
    • (1995) Biochim Biophys Acta , vol.1261 , pp. 183-194
    • Wahle, E.1
  • 43
    • 0024448762 scopus 로고
    • Analysis of expression of multiple genes encoding calmodulin during spermatogenesis
    • Slaughter GR, Means AR 1989 Analysis of expression of multiple genes encoding calmodulin during spermatogenesis. Mol Endocrinol 3:1569-1578
    • (1989) Mol Endocrinol , vol.3 , pp. 1569-1578
    • Slaughter, G.R.1    Means, A.R.2
  • 46
    • 0024549994 scopus 로고
    • Human testis cDNA for the regulatory subunit RIIα of cAMP-dependent protein kinase encodes an alternate aminoterminal region
    • Øyen O, Myklebust F, Scott JD, Hansson V, Jahnsen T 1989 Human testis cDNA for the regulatory subunit RIIα of cAMP-dependent protein kinase encodes an alternate aminoterminal region. FEBS Lett 246:57-64
    • (1989) FEBS Lett , vol.246 , pp. 57-64
    • Øyen, O.1    Myklebust, F.2    Scott, J.D.3    Hansson, V.4    Jahnsen, T.5
  • 48
    • 0027410096 scopus 로고
    • Pituitary hormone FSH directs the CREM functional swithc during spermatogenesis
    • Foulkes NS, Schlotter F, Pévet P, Sassone-Corsi P 1993 Pituitary hormone FSH directs the CREM functional swithc during spermatogenesis. Nature 362:264-267
    • (1993) Nature , vol.362 , pp. 264-267
    • Foulkes, N.S.1    Schlotter, F.2    Pévet, P.3    Sassone-Corsi, P.4
  • 49
    • 0023058975 scopus 로고
    • A conserved AU sequence from the 3′ untranslated region of GM-CSF mRNA mediates selective mRNA degradation
    • Shaw G, Kamen R 1986 A conserved AU sequence from the 3′ untranslated region of GM-CSF mRNA mediates selective mRNA degradation. Cell 46:659-667
    • (1986) Cell , vol.46 , pp. 659-667
    • Shaw, G.1    Kamen, R.2
  • 50
    • 0018142760 scopus 로고
    • Regulation of initiation of meiosis in fetal gonads
    • Byskov A-G 1978 Regulation of initiation of meiosis in fetal gonads. Int J Androl [Supp] 2:29-37
    • (1978) Int J Androl [Supp] , vol.2 , pp. 29-37
    • Byskov, A.-G.1
  • 51
    • 0020427752 scopus 로고
    • Is the spermatogenic cycle regulated by MIS and MPS?
    • Parvinen M 1982 Is the spermatogenic cycle regulated by MIS and MPS? Ann NY Acad Sci 383:483-484
    • (1982) Ann NY Acad Sci , vol.383 , pp. 483-484
    • Parvinen, M.1


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