메뉴 건너뛰기




Volumn 137, Issue 6, 1996, Pages 2464-2472

Developmental Regulation of Unique Adenosine 3′,5′-Monophosphate-Specific Phosphodiesterase Variants during Rat Spermatogenesis

Author keywords

[No Author keywords available]

Indexed keywords

CYCLIC AMP PHOSPHODIESTERASE; ISOENZYME; MESSENGER RNA;

EID: 0029890071     PISSN: 00137227     EISSN: None     Source Type: Journal    
DOI: 10.1210/endo.137.6.8641200     Document Type: Article
Times cited : (41)

References (49)
  • 1
    • 0026270156 scopus 로고
    • Structure and regulation of G protein-coupled receptors: The beta 2-adrenergic receptor as a model
    • Collins S, Lohse MJ, O'Dowd B, Caron MG, Lefkowitz RJ 1991 Structure and regulation of G protein-coupled receptors: the beta 2-adrenergic receptor as a model. Vitam Horm 46:1-39
    • (1991) Vitam Horm , vol.46 , pp. 1-39
    • Collins, S.1    Lohse, M.J.2    O'Dowd, B.3    Caron, M.G.4    Lefkowitz, R.J.5
  • 4
    • 0039792871 scopus 로고
    • AMP-dependent protein kinases
    • Boyer PD (ed) Academic Press, Orlando
    • Beebe SJ, Corbin JD 1995 cAMP-dependent protein kinases. In: Boyer PD (ed) The Enzymes. Academic Press, Orlando, pp 43-75
    • (1995) The Enzymes , pp. 43-75
    • Beebe, S.J.1    Corbin, J.D.2
  • 5
    • 0024253227 scopus 로고
    • Multiple isozymes of cyclic nucleotide phosphodiesterase
    • Beavo JA 1988 Multiple isozymes of cyclic nucleotide phosphodiesterase. Adv Second Messenger Phosphoprotein Res 22:1-38
    • (1988) Adv Second Messenger Phosphoprotein Res , vol.22 , pp. 1-38
    • Beavo, J.A.1
  • 8
    • 0027524769 scopus 로고
    • Induction of CREM activator proteins in spermatids: Downstream targets and implications for haploid germ cell differentiation
    • Delmas V, van der Hoorn F, Mellstrom B, Jegou B, Sassone-Corsi P 1993 Induction of CREM activator proteins in spermatids: downstream targets and implications for haploid germ cell differentiation. Mol Endocrinol 7:1502-1514
    • (1993) Mol Endocrinol , vol.7 , pp. 1502-1514
    • Delmas, V.1    Van Der Hoorn, F.2    Mellstrom, B.3    Jegou, B.4    Sassone-Corsi, P.5
  • 9
    • 0027531329 scopus 로고
    • Sperm-specific expression of angiotensin-converting enzyme (ACE) is mediated by a 91-base-pair promoter containing a CRE-like element
    • Howard T, Balogh R, Overbeek P, Bernstein KE 1993 Sperm-specific expression of angiotensin-converting enzyme (ACE) is mediated by a 91-base-pair promoter containing a CRE-like element. Mol Cell Biol 13:18-27
    • (1993) Mol Cell Biol , vol.13 , pp. 18-27
    • Howard, T.1    Balogh, R.2    Overbeek, P.3    Bernstein, K.E.4
  • 10
    • 0029097303 scopus 로고
    • An intron facilitates activation of the calspermin gene by the testis-specific transcription factor CREMτ
    • Sun Z, Means AR 1995 An intron facilitates activation of the calspermin gene by the testis-specific transcription factor CREMτ. J Biol Chem 270:20962-20967
    • (1995) J Biol Chem , vol.270 , pp. 20962-20967
    • Sun, Z.1    Means, A.R.2
  • 11
    • 0027945544 scopus 로고
    • Identification of a functional cyclic adenosine 3′,5′-monophosphate response element in the 5′-flanking region of the gene for transition protein 1 (TP1), a basic chromosomal protein of mammalian spermatids
    • Kistler MK, Sassone-Corsi P, Kistler WS 1994 Identification of a functional cyclic adenosine 3′,5′-monophosphate response element in the 5′-flanking region of the gene for transition protein 1 (TP1), a basic chromosomal protein of mammalian spermatids. Biol Reprod 51:1322-1329
    • (1994) Biol Reprod , vol.51 , pp. 1322-1329
    • Kistler, M.K.1    Sassone-Corsi, P.2    Kistler, W.S.3
  • 12
    • 0017624192 scopus 로고
    • 2+-sensitive, soluble adenylate cyclase in rat testis. Differentiation from other testicular nucleotide cyclases
    • 2+-sensitive, soluble adenylate cyclase in rat testis. Differentiation from other testicular nucleotide cyclases. Biochim Biophys Acta 481:227-235
    • (1977) Biochim Biophys Acta , vol.481 , pp. 227-235
    • Braun, T.1    Frank, H.2    Dods, R.3    Sepsenwol, S.4
  • 13
    • 0017892960 scopus 로고
    • Physical and functional properties of adenylate cyclase from mature rat testis
    • Neer EJ 1978 Physical and functional properties of adenylate cyclase from mature rat testis. J Biol Chem 253:5808-5812
    • (1978) J Biol Chem , vol.253 , pp. 5808-5812
    • Neer, E.J.1
  • 14
    • 0019159814 scopus 로고
    • Particulate and soluble adenylate cyclase activities of mouse male germ cells
    • Adamo S, Conti M, Geremia R, Monesi V 1980 Particulate and soluble adenylate cyclase activities of mouse male germ cells. Biochem Biophys Res Commun 97:607-613
    • (1980) Biochem Biophys Res Commun , vol.97 , pp. 607-613
    • Adamo, S.1    Conti, M.2    Geremia, R.3    Monesi, V.4
  • 16
    • 0021349138 scopus 로고
    • Characterization of a calmodulin-dependent high-affinity cyclic AMP and cyclic GMP phosphodiesterase from male mouse germ cells
    • Geremia R, Rossi P, Mocini D, Pezzotti R, Conti M 1984 Characterization of a calmodulin-dependent high-affinity cyclic AMP and cyclic GMP phosphodiesterase from male mouse germ cells. Biochem J 217:693-700
    • (1984) Biochem J , vol.217 , pp. 693-700
    • Geremia, R.1    Rossi, P.2    Mocini, D.3    Pezzotti, R.4    Conti, M.5
  • 17
    • 0026513416 scopus 로고
    • Unique adenosine 3′,5′ cyclic monophosphate phosphodiesterase messenger ribonucleic acids in rat spermatogenic cells: Evidence for differential gene expression during spermatogenesis
    • Welch JE, Swinnen JV, O'Brien DA, Eddy EM, Conti M 1992 Unique adenosine 3′,5′ cyclic monophosphate phosphodiesterase messenger ribonucleic acids in rat spermatogenic cells: evidence for differential gene expression during spermatogenesis. Biol Reprod 46:1027-1033
    • (1992) Biol Reprod , vol.46 , pp. 1027-1033
    • Welch, J.E.1    Swinnen, J.V.2    O'Brien, D.A.3    Eddy, E.M.4    Conti, M.5
  • 18
    • 0028911420 scopus 로고
    • Stage and cell-specific expression of the adenosine 3′,5′ monophosphate-phosphodiesterase genes in the rat seminiferous epithelium
    • Morena AR, Boitani C, de Grossi S, Stefanini M, Conti M 1995 Stage and cell-specific expression of the adenosine 3′,5′ monophosphate-phosphodiesterase genes in the rat seminiferous epithelium. Endocrinology 136:687-695
    • (1995) Endocrinology , vol.136 , pp. 687-695
    • Morena, A.R.1    Boitani, C.2    De Grossi, S.3    Stefanini, M.4    Conti, M.5
  • 19
    • 0028136159 scopus 로고
    • Multiple cyclic nucleotide phosphodiesterases
    • Beavo JA, Conti M, Heaslip RJ 1994 Multiple cyclic nucleotide phosphodiesterases. Mol Pharmacol 46:399-405
    • (1994) Mol Pharmacol , vol.46 , pp. 399-405
    • Beavo, J.A.1    Conti, M.2    Heaslip, R.J.3
  • 20
    • 0022412504 scopus 로고
    • Cyclic nucleotide phosphodiesterases in somatic and germ cells of mouse seminiferous tubules
    • Rossi P, Pezzotti R, Conti M, Geremia R 1985 Cyclic nucleotide phosphodiesterases in somatic and germ cells of mouse seminiferous tubules. J Reprod Fertil 74:317-327
    • (1985) J Reprod Fertil , vol.74 , pp. 317-327
    • Rossi, P.1    Pezzotti, R.2    Conti, M.3    Geremia, R.4
  • 21
    • 0022779719 scopus 로고
    • Localization of adenosine receptors in rat testicular cells
    • Monaco L, Conti M 1986 Localization of adenosine receptors in rat testicular cells. Biol Reprod 35:258-266
    • (1986) Biol Reprod , vol.35 , pp. 258-266
    • Monaco, L.1    Conti, M.2
  • 22
    • 0021352272 scopus 로고
    • Characterization and localization of cAMP-dependent protein kinases in rat caudal epididymal sperm
    • Horowitz JA, Toeg H, Orr GA 1984 Characterization and localization of cAMP-dependent protein kinases in rat caudal epididymal sperm. J Biol Chem 259:832-838
    • (1984) J Biol Chem , vol.259 , pp. 832-838
    • Horowitz, J.A.1    Toeg, H.2    Orr, G.A.3
  • 23
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM 1976 A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72:248-254
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 25
    • 0024670166 scopus 로고
    • Cloning and characterization of mammalian homologs of the Drosophila dunce+ gene
    • Davis RL, Takayasu H, Eberwine M, Myres J 1989 Cloning and characterization of mammalian homologs of the Drosophila dunce+ gene. Proc Natl Acad Sci USA 86:3604-3608
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 3604-3608
    • Davis, R.L.1    Takayasu, H.2    Eberwine, M.3    Myres, J.4
  • 26
    • 0026315434 scopus 로고
    • Attenuation of cAMP-mediated responses in MA-10 Leydig tumor cells by genetic manipulation of a cAMP-phosphodiesterase
    • published erratum appears in J Biol Chem 267:2114, 1992.
    • Swinnen JV, D'Souza B, Conti M, Ascoli M 1991 Attenuation of cAMP-mediated responses in MA-10 Leydig tumor cells by genetic manipulation of a cAMP-phosphodiesterase [published erratum appears in J Biol Chem 267:2114, 1992]. J Biol Chem 266:14383-14389
    • (1991) J Biol Chem , vol.266 , pp. 14383-14389
    • Swinnen, J.V.1    D'Souza, B.2    Conti, M.3    Ascoli, M.4
  • 27
    • 0028033778 scopus 로고
    • Differential CNS expression of alternative mRNA isoforms of the mammalian genes encoding cAMP-specific phosphodiesterases
    • Bolger GB, Rodgers L, Riggs M 1994 Differential CNS expression of alternative mRNA isoforms of the mammalian genes encoding cAMP-specific phosphodiesterases. Gene 149:237-244
    • (1994) Gene , vol.149 , pp. 237-244
    • Bolger, G.B.1    Rodgers, L.2    Riggs, M.3
  • 28
    • 0024405251 scopus 로고
    • Molecular cloning of rat homologues of the Drosophila melanogaster dunce cAMP phosphodiesterase: Evidence for a family of genes
    • Swinnen JV, Joseph DR, Conti M 1989 Molecular cloning of rat homologues of the Drosophila melanogaster dunce cAMP phosphodiesterase: evidence for a family of genes. Proc Natl Acad Sci USA 86:5325-5329
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 5325-5329
    • Swinnen, J.V.1    Joseph, D.R.2    Conti, M.3
  • 29
    • 0016225079 scopus 로고
    • Assay of cyclic nucleotide phosphodiesterases with radioactive substrates
    • Thompson WJ, Brooker G, Appleman MM 1974 Assay of cyclic nucleotide phosphodiesterases with radioactive substrates. Methods Enzymol 38:205-212
    • (1974) Methods Enzymol , vol.38 , pp. 205-212
    • Thompson, W.J.1    Brooker, G.2    Appleman, M.M.3
  • 30
    • 0021920534 scopus 로고
    • GMP phosphodiesterase in rod and cone outer segments of the retina
    • Hurwitz RL, Bunt-Milam AH, Chang ML, Beavo JA 1985 cGMP phosphodiesterase in rod and cone outer segments of the retina. J Biol Chem 260:568-573
    • (1985) J Biol Chem , vol.260 , pp. 568-573
    • Hurwitz, R.L.1    Bunt-Milam, A.H.2    Chang, M.L.3    Beavo, J.A.4
  • 31
    • 0017120229 scopus 로고
    • 4-(3-Cyclopentyloxy-4-methoxyphenyl)-2-pyrrolidone (ZK 62711): A potent inhibitor of adenosine cyclic 3′,5′-monophosphate phosphodiesterases in homogenates and tissue slices from rat brain
    • Schwabe U, Miyake M, Ohga Y, Daly JW 1976 4-(3-Cyclopentyloxy-4-methoxyphenyl)-2-pyrrolidone (ZK 62711): a potent inhibitor of adenosine cyclic 3′,5′-monophosphate phosphodiesterases in homogenates and tissue slices from rat brain. Mol Pharmacol 12:900-910
    • (1976) Mol Pharmacol , vol.12 , pp. 900-910
    • Schwabe, U.1    Miyake, M.2    Ohga, Y.3    Daly, J.W.4
  • 32
    • 0023806075 scopus 로고
    • Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferase
    • Smith DB, Johnson KS 1988 Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferase. Gene 67:31-40
    • (1988) Gene , vol.67 , pp. 31-40
    • Smith, D.B.1    Johnson, K.S.2
  • 33
    • 0029061008 scopus 로고
    • Characterization of a hormone-inducible, high affinity 3′-5′-cyclic monophosphate phosphodiesterase from the rat Sertoli cell
    • Conti M, Iona S, Cuomo M, Swinnen JV, Odeh J, Svoboda ME, Salis A 1995 Characterization of a hormone-inducible, high affinity 3′-5′-cyclic monophosphate phosphodiesterase from the rat Sertoli cell. Biochemistry 34:797-7987
    • (1995) Biochemistry , vol.34 , pp. 797-7987
    • Conti, M.1    Iona, S.2    Cuomo, M.3    Swinnen, J.V.4    Odeh, J.5    Svoboda, M.E.6    Salis, A.7
  • 34
    • 0022973992 scopus 로고
    • Immunological identification of the major platelet low-Km cAMP phosphodiesterase: Probable target for anti-thrombotic agents
    • Macphee CH, Harrison SA, Beavo JA 1986 Immunological identification of the major platelet low-Km cAMP phosphodiesterase: probable target for anti-thrombotic agents. Proc Natl Acad Sci USA 83:6660-6663
    • (1986) Proc Natl Acad Sci USA , vol.83 , pp. 6660-6663
    • Macphee, C.H.1    Harrison, S.A.2    Beavo, J.A.3
  • 35
    • 0027454556 scopus 로고
    • A family of human phosphodiesterases homologous to the dunce learning and memory gene product of Drosophila melanogaster are potential targets for antidepressant drugs
    • Bolger G, Michaeli T, Martins T, St.John T, Steiner B, Rodgers L, Riggs M, Wigler M, Ferguson K 1993 A family of human phosphodiesterases homologous to the dunce learning and memory gene product of Drosophila melanogaster are potential targets for antidepressant drugs. Mol Cell Biol 13:6558-6571
    • (1993) Mol Cell Biol , vol.13 , pp. 6558-6571
    • Bolger, G.1    Michaeli, T.2    Martins, T.3    St. John, T.4    Steiner, B.5    Rodgers, L.6    Riggs, M.7    Wigler, M.8    Ferguson, K.9
  • 37
    • 70449159934 scopus 로고
    • Quantitative study of the cell population of the seminiferous tubules in immature rats
    • Clermont Y, Perey B 1957 Quantitative study of the cell population of the seminiferous tubules in immature rats. Am J Anat 100:241-268
    • (1957) Am J Anat , vol.100 , pp. 241-268
    • Clermont, Y.1    Perey, B.2
  • 38
    • 0026753496 scopus 로고
    • Characterization of the structure of a low Km, rolipram-sensitive cAMP phosphodiesterase. Mapping of the catalytic domain
    • Jin SL, Swinnen JV, Conti M 1992 Characterization of the structure of a low Km, rolipram-sensitive cAMP phosphodiesterase. Mapping of the catalytic domain. J Biol Chem 267:18929-18939
    • (1992) J Biol Chem , vol.267 , pp. 18929-18939
    • Jin, S.L.1    Swinnen, J.V.2    Conti, M.3
  • 39
    • 0020506624 scopus 로고
    • Regulation of cyclic adenosine 3′:5′-monophosphate phosphodiesterases: Altered pattern in transformed myoblasts
    • Seth PK, Rogers J, Narindrasorasak S, Sanwal BD 1983 Regulation of cyclic adenosine 3′:5′-monophosphate phosphodiesterases: altered pattern in transformed myoblasts. J Cell Physiol 116:336-344
    • (1983) J Cell Physiol , vol.116 , pp. 336-344
    • Seth, P.K.1    Rogers, J.2    Narindrasorasak, S.3    Sanwal, B.D.4
  • 40
    • 0019964794 scopus 로고
    • Regulation of cyclic adenosine 3′:5′-monophosphate phosphodiesterases. Interrelationship of the various forms in rat skeletal myoblasts and adult muscle
    • Narindrasorasak S, Tan LU, Seth PK, Sanwal BD 1982 Regulation of cyclic adenosine 3′:5′-monophosphate phosphodiesterases. Interrelationship of the various forms in rat skeletal myoblasts and adult muscle. J Biol Chem 257:4618-4626
    • (1982) J Biol Chem , vol.257 , pp. 4618-4626
    • Narindrasorasak, S.1    Tan, L.U.2    Seth, P.K.3    Sanwal, B.D.4
  • 41
    • 0019972206 scopus 로고
    • Cyclic nucleotide phosphodiesterase in developing rat testis. Identification of somatic and germ-cell forms
    • Geremia R, Rossi P, Pezzotti R, Conti M 1982 Cyclic nucleotide phosphodiesterase in developing rat testis. Identification of somatic and germ-cell forms. Mol Cell Endocrinol 28:37-53
    • (1982) Mol Cell Endocrinol , vol.28 , pp. 37-53
    • Geremia, R.1    Rossi, P.2    Pezzotti, R.3    Conti, M.4
  • 42
    • 0021347846 scopus 로고
    • Function of calmodulin in mammalian sperm: Presence of a calmodulin-dependent cyclic nucleotide phosphodiesterase associated with demembranated rat caudal epididymal sperm
    • Wasco WM, Orr GA 1984 Function of calmodulin in mammalian sperm: presence of a calmodulin-dependent cyclic nucleotide phosphodiesterase associated with demembranated rat caudal epididymal sperm. Biochem Biophys Res Commun 118:636-642
    • (1984) Biochem Biophys Res Commun , vol.118 , pp. 636-642
    • Wasco, W.M.1    Orr, G.A.2
  • 43
    • 0024584508 scopus 로고
    • Biochemical and immunological characterization of the flagellar-associated regulatory subunit of a type II cyclic adenosine 5′-monophosphate-dependent protein kinase
    • Horowitz JA, Voulalas P, Wasco W, MacLeod J, Paupard MC, Orr GA 1989 Biochemical and immunological characterization of the flagellar-associated regulatory subunit of a type II cyclic adenosine 5′-monophosphate-dependent protein kinase. Arch Biochem Biophys 270:411-418
    • (1989) Arch Biochem Biophys , vol.270 , pp. 411-418
    • Horowitz, J.A.1    Voulalas, P.2    Wasco, W.3    MacLeod, J.4    Paupard, M.C.5    Orr, G.A.6
  • 44
    • 0023841019 scopus 로고
    • Interaction of the regulatory subunit of a type II cAMP-dependent protein kinase with mammalian sperm flagellum
    • Horowitz JA, Wasco W, Leiser M, Orr GA 1988 Interaction of the regulatory subunit of a type II cAMP-dependent protein kinase with mammalian sperm flagellum. J Biol Chem 263:2098-2104
    • (1988) J Biol Chem , vol.263 , pp. 2098-2104
    • Horowitz, J.A.1    Wasco, W.2    Leiser, M.3    Orr, G.A.4
  • 45
    • 0028111091 scopus 로고
    • Association of the regulatory subunit of a type II cAMP-dependent protein kinase and its binding proteins with the fibrous sheath of rat sperm flagellum
    • Macleod L, Mei X, Erlichman J, Orr GA 1994 Association of the regulatory subunit of a type II cAMP-dependent protein kinase and its binding proteins with the fibrous sheath of rat sperm flagellum. Eur J Biochem 225:107-114
    • (1994) Eur J Biochem , vol.225 , pp. 107-114
    • Macleod, L.1    Mei, X.2    Erlichman, J.3    Orr, G.A.4
  • 46
    • 0028023326 scopus 로고
    • The major fibrous sheath polypeptide of mouse sperm: Structural and functional similarities to the A-kinase anchoring proteins
    • Carrera A, Gerton GL, Moss SB 1994 The major fibrous sheath polypeptide of mouse sperm: structural and functional similarities to the A-kinase anchoring proteins. Dev Biol 165:272-284
    • (1994) Dev Biol , vol.165 , pp. 272-284
    • Carrera, A.1    Gerton, G.L.2    Moss, S.B.3
  • 47
    • 85033736859 scopus 로고
    • Epididymal physiology and sperm maturation
    • Hubinat M, l'Hermite M, Scwers J (eds) I. Sperm Action. Kager, Basel
    • Hamilton DW, Olson GE, Beeuwkes R 1971 Epididymal physiology and sperm maturation. In: Hubinat M, l'Hermite M, Scwers J (eds) Progress in Reproductive Biology. I. Sperm Action. Kager, Basel, pp 62-73
    • (1971) Progress in Reproductive Biology , pp. 62-73
    • Hamilton, D.W.1    Olson, G.E.2    Beeuwkes, R.3
  • 48
    • 0020623097 scopus 로고
    • Cyclic adenosine 3′,5′ monophosphate, calcium and protein phosphorylation in flagellar motility
    • Tash JS, Means AR 1983 Cyclic adenosine 3′,5′ monophosphate, calcium and protein phosphorylation in flagellar motility. Biol Reprod 28:75-104
    • (1983) Biol Reprod , vol.28 , pp. 75-104
    • Tash, J.S.1    Means, A.R.2
  • 49
    • 0025999955 scopus 로고
    • Cyclic nucleotide phosphodiesterases: Pharmacology, biochemistry and function
    • Thompson WJ 1991 Cyclic nucleotide phosphodiesterases: pharmacology, biochemistry and function. Pharmacol Ther 51:13-33
    • (1991) Pharmacol Ther , vol.51 , pp. 13-33
    • Thompson, W.J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.