메뉴 건너뛰기




Volumn 56, Issue 6, 1997, Pages 1450-1457

A tyrosine-phosphorylated 55-kilodalton motility-associated bovine sperm protein is regulated by cyclic adenosine 3',5'-monophosphates and calcium

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM; CYCLIC AMP; CYCLIC AMP DEPENDENT PROTEIN KINASE; DIETHYLAMINOETHYL CELLULOSE; ISOBUTYLMETHYLXANTHINE; TYROSINE;

EID: 0030923852     PISSN: 00063363     EISSN: None     Source Type: Journal    
DOI: 10.1095/biolreprod56.6.1450     Document Type: Article
Times cited : (82)

References (48)
  • 1
    • 0022199668 scopus 로고
    • Plasma membrane calcium flux, protein kinase C activation and smooth muscle contraction
    • Forder J, Scriabine A, Rasmussen H. Plasma membrane calcium flux, protein kinase C activation and smooth muscle contraction. J Pharmacol Exp Ther 1985; 235:267-273.
    • (1985) J Pharmacol Exp Ther , vol.235 , pp. 267-273
    • Forder, J.1    Scriabine, A.2    Rasmussen, H.3
  • 2
    • 0028908633 scopus 로고
    • Characterization of two second messenger pathways and their interactions in eliciting the human sperm acrosome reaction
    • Doherty CM, Tarchala SM, Radwanska E, De Jonge CJ. Characterization of two second messenger pathways and their interactions in eliciting the human sperm acrosome reaction. J Androl 1995; 16:36-46.
    • (1995) J Androl , vol.16 , pp. 36-46
    • Doherty, C.M.1    Tarchala, S.M.2    Radwanska, E.3    De Jonge, C.J.4
  • 3
    • 0023952125 scopus 로고
    • Identification, characterization, and functional correlation of calmodulin-dependent protein phosphatase in sperm
    • Tash JS, Krinks M, Patel J, Means RL, Klee CB, Means AR. Identification, characterization, and functional correlation of calmodulin-dependent protein phosphatase in sperm. J Cell Biol 1988; 106:1625-1633.
    • (1988) J Cell Biol , vol.106 , pp. 1625-1633
    • Tash, J.S.1    Krinks, M.2    Patel, J.3    Means, R.L.4    Klee, C.B.5    Means, A.R.6
  • 4
    • 0023071398 scopus 로고
    • 2+ regulation of sperm axonemal motility
    • Means AR, Conn PM (eds.), Orlando, FL: Academic Press, Inc.
    • 2+ regulation of sperm axonemal motility. In: Means AR, Conn PM (eds.), Methods in Enzymology, Vol 139. Orlando, FL: Academic Press, Inc.; 1987: 808-823.
    • (1987) Methods in Enzymology , vol.139 , pp. 808-823
    • Tash, J.S.1    Means, A.R.2
  • 5
    • 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. 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 1984; 118:636-642.
    • (1984) Biochem Biophys Res Commun , vol.118 , pp. 636-642
    • Wasco, W.M.1    Orr, G.A.2
  • 6
    • 0023258569 scopus 로고
    • Calmodulin-mediated adenylate cyclase from mammalian sperm
    • Gross MK, Toscano DG, Toscano WAJR. Calmodulin-mediated adenylate cyclase from mammalian sperm. J Biol Chem 1987; 262: 8672-8676.
    • (1987) J Biol Chem , vol.262 , pp. 8672-8676
    • Gross, M.K.1    Toscano, D.G.2    Toscano, W.A.J.R.3
  • 7
    • 0020075383 scopus 로고
    • Evidence that cAMP-dependent protein kinase and a protein factor are involved in reactivation of triton x-100 models of sea urchin and starfish spermatozoa
    • Ishiguro K, Murofushi H, Sakai H. Evidence that cAMP-dependent protein kinase and a protein factor are involved in reactivation of triton x-100 models of sea urchin and starfish spermatozoa. J Cell Biol 1982; 92:777-782.
    • (1982) J Cell Biol , vol.92 , pp. 777-782
    • Ishiguro, K.1    Murofushi, H.2    Sakai, H.3
  • 8
    • 0021184785 scopus 로고
    • Flagellar motility requires the cAMP-dependent phosphorylation of a heat-stable np-40-soluble 56-kDa protein, axokinin
    • Tash JS, Kakar SS, Means AR. Flagellar motility requires the cAMP-dependent phosphorylation of a heat-stable np-40-soluble 56-kDa protein, axokinin. Cell 1984; 38:551-559.
    • (1984) Cell , vol.38 , pp. 551-559
    • Tash, J.S.1    Kakar, S.S.2    Means, A.R.3
  • 9
    • 0024329482 scopus 로고
    • Protein phosphorylation: The second messenger signal transducer of flagellar motility
    • Tash JS. Protein phosphorylation: the second messenger signal transducer of flagellar motility. Cell Motil Cytoskeleton 1989; 14:332-339.
    • (1989) Cell Motil Cytoskeleton , vol.14 , pp. 332-339
    • Tash, J.S.1
  • 10
    • 0021332562 scopus 로고
    • Effects of cyclic AMP on the motility of mature and immature hamster epididymal spermatozoa studied by reactivation of the demembranated cells
    • Yeung CH. Effects of cyclic AMP on the motility of mature and immature hamster epididymal spermatozoa studied by reactivation of the demembranated cells. Gamete Res 1984; 9:99-114.
    • (1984) Gamete Res , vol.9 , pp. 99-114
    • Yeung, C.H.1
  • 11
    • 0021791297 scopus 로고
    • Phosphorylation of a 15K axonemal protein is the trigger initiating trout sperm motility
    • Morisawa M, Hayashi H. Phosphorylation of a 15K axonemal protein is the trigger initiating trout sperm motility. Biomed Res 1985; 6:181-184.
    • (1985) Biomed Res , vol.6 , pp. 181-184
    • Morisawa, M.1    Hayashi, H.2
  • 12
    • 0023646056 scopus 로고
    • Involvement of tyrosine protein kinase in the initiation of flagellar movement in rainbow trout spermatozoa
    • Hayashi H, Yamamoto K, Yonekawa H, Morisawa M. Involvement of tyrosine protein kinase in the initiation of flagellar movement in rainbow trout spermatozoa. J Biol Chem 1987; 262:16692-16698.
    • (1987) J Biol Chem , vol.262 , pp. 16692-16698
    • Hayashi, H.1    Yamamoto, K.2    Yonekawa, H.3    Morisawa, M.4
  • 13
    • 0022536347 scopus 로고
    • Axokinin phosphorylation by cAMP-dependent protein kinase is sufficient for activation of sperm flagellar motility
    • Tash JS, Hidaka H, Means AR. Axokinin phosphorylation by cAMP-dependent protein kinase is sufficient for activation of sperm flagellar motility. J Cell Biol 1986; 103:649-655.
    • (1986) J Cell Biol , vol.103 , pp. 649-655
    • Tash, J.S.1    Hidaka, H.2    Means, A.R.3
  • 14
    • 0023682033 scopus 로고
    • Major 56,000-dalton, soluble phosphoprotein present in bovine sperm is the regulatory subunit of a type Ii cAMP-dependent protein kinase
    • Paupard MC, Macleod J, Wasco W, Orr GA. Major 56,000-dalton, soluble phosphoprotein present in bovine sperm is the regulatory subunit of a type Ii cAMP-dependent protein kinase. J Cell Biochem 1988; 37:161-175.
    • (1988) J Cell Biochem , vol.37 , pp. 161-175
    • Paupard, M.C.1    Macleod, J.2    Wasco, W.3    Orr, G.A.4
  • 15
    • 0028605927 scopus 로고
    • Regulation of sperm motility: Emerging evidence for a major role for protein phosphatases
    • Tash JS, Bracho GE. Regulation of sperm motility: emerging evidence for a major role for protein phosphatases. J Androl 1994; 15:505-509.
    • (1994) J Androl , vol.15 , pp. 505-509
    • Tash, J.S.1    Bracho, G.E.2
  • 16
    • 0025018348 scopus 로고
    • The phosphorylation of a putative sperm microtubule-associated protein 2 (MAP2) is uniquely sensitive to regulation
    • Carr DW, Acott TS. The phosphorylation of a putative sperm microtubule-associated protein 2 (MAP2) is uniquely sensitive to regulation. Biol Reprod 1990; 43:795-805.
    • (1990) Biol Reprod , vol.43 , pp. 795-805
    • Carr, D.W.1    Acott, T.S.2
  • 17
    • 0018830277 scopus 로고
    • A c-AMP-dependent phosphorylated motility protein in bovine epididymal sperm
    • Brandt H, Hoskins DD. A c-AMP-dependent phosphorylated motility protein in bovine epididymal sperm. J Biol Chem 1980; 255:982-987.
    • (1980) J Biol Chem , vol.255 , pp. 982-987
    • Brandt, H.1    Hoskins, D.D.2
  • 18
    • 0028957362 scopus 로고
    • Capacitation of mouse spermatozoa. I. Correlation between the capacitation state and protein tyrosine phosphorylation
    • Visconti PE, Bailey JL, Moore GD, Pan D, Olds-Clarke P, Kopf GS. Capacitation of mouse spermatozoa. I. Correlation between the capacitation state and protein tyrosine phosphorylation. Development 1995; 121:1129-1137.
    • (1995) Development , vol.121 , pp. 1129-1137
    • Visconti, P.E.1    Bailey, J.L.2    Moore, G.D.3    Pan, D.4    Olds-Clarke, P.5    Kopf, G.S.6
  • 19
    • 0028936801 scopus 로고
    • Capacitation of mouse spermatozoa. II. Protein tyrosine phosphorylation and capacitation are regulated by a cAMP-dependent pathway
    • Visconti PE, Moore GD, Bailey JL. Capacitation of mouse spermatozoa. II. Protein tyrosine phosphorylation and capacitation are regulated by a cAMP-dependent pathway. Development 1995; 121:1139-1150.
    • (1995) Development , vol.121 , pp. 1139-1150
    • Visconti, P.E.1    Moore, G.D.2    Bailey, J.L.3
  • 20
    • 0030047194 scopus 로고    scopus 로고
    • Sperm motility development in the epididymis is associated with decreased glycogen synthase kinase-3 and protein phosphatase 1 activity
    • Vijayaraghavan S, Stephens DT, Trautman K. Sperm motility development in the epididymis is associated with decreased glycogen synthase kinase-3 and protein phosphatase 1 activity. Biol Reprod 1996; 54:709-718.
    • (1996) Biol Reprod , vol.54 , pp. 709-718
    • Vijayaraghavan, S.1    Stephens, D.T.2    Trautman, K.3
  • 22
    • 0024397415 scopus 로고
    • The structure and regulation of protein phosphatases
    • Cohen P. The structure and regulation of protein phosphatases. Annu Rev Biochem 1989; 58:453.
    • (1989) Annu Rev Biochem , vol.58 , pp. 453
    • Cohen, P.1
  • 23
    • 0027475421 scopus 로고
    • Modulation of the glycogen synthase kinase-3 family by tyrosine phosphorylation
    • Hughes K, Nikolakaki E, Plyte S. Totty NF, Woodgett JR. Modulation of the glycogen synthase kinase-3 family by tyrosine phosphorylation. EMBO J 1993; 12:803-808.
    • (1993) EMBO J , vol.12 , pp. 803-808
    • Hughes, K.1    Nikolakaki, E.2    Plyte, S.3    Totty, N.F.4    Woodgett, J.R.5
  • 24
    • 0026680801 scopus 로고
    • Association of the type II cAMP-dependent protein kinase with a human thyroid RII-anchoring protein. Cloning and characterization of the RII-binding domain
    • Carr DW, Hausken ZE, Fraser ID, Stofko-Hahn RE, Scott JD. Association of the type II cAMP-dependent protein kinase with a human thyroid RII-anchoring protein. Cloning and characterization of the RII-binding domain. J Biol Chem 1992;267:13376-13382.
    • (1992) J Biol Chem , vol.267 , pp. 13376-13382
    • Carr, D.W.1    Hausken, Z.E.2    Fraser, I.D.3    Stofko-Hahn, R.E.4    Scott, J.D.5
  • 25
    • 0028588997 scopus 로고
    • A kinase anchor proteins and the intracellular targeting of signals carried by cyclic AMP
    • Rubin CS. A kinase anchor proteins and the intracellular targeting of signals carried by cyclic AMP. Biochim Biophys Acta 1994; 1224: 467-479.
    • (1994) Biochim Biophys Acta , vol.1224 , pp. 467-479
    • Rubin, C.S.1
  • 26
    • 0026348474 scopus 로고
    • Interaction of the regulatory subunit (RII) of cAMP-dependent protein kinase with RII-anchoring proteins occurs through an amphipathic helix binding motif
    • Carr DW, Stofko-Hahn RE, Fraser ID, Bishop SM, Acott TS. Interaction of the regulatory subunit (RII) of cAMP-dependent protein kinase with RII-anchoring proteins occurs through an amphipathic helix binding motif. J Biol Chem 1991; 266:14188-14192.
    • (1991) J Biol Chem , vol.266 , pp. 14188-14192
    • Carr, D.W.1    Stofko-Hahn, R.E.2    Fraser, I.D.3    Bishop, S.M.4    Acott, T.S.5
  • 27
    • 0026795614 scopus 로고
    • Localization of the cAMP-dependent protein kinase to the postsynaptic densities by A-kinase anchoring proteins. Characterization of AKAP 79
    • Carr DW, Stofko-Hahn RE, Fraser ID, Cone RD, Scott JD. Localization of the cAMP-dependent protein kinase to the postsynaptic densities by A-kinase anchoring proteins. Characterization of AKAP 79. J Biol Chem 1992; 267:16816-16823.
    • (1992) J Biol Chem , vol.267 , pp. 16816-16823
    • Carr, D.W.1    Stofko-Hahn, R.E.2    Fraser, I.D.3    Cone, R.D.4    Scott, J.D.5
  • 28
    • 0023951935 scopus 로고
    • Description, validation, and performance characteristics of a new computer-automated sperm motility analysis system
    • Stephens DT, Hickman R, Hoskins DD. Description, validation, and performance characteristics of a new computer-automated sperm motility analysis system. Biol Reprod 1988; 38:577-586.
    • (1988) Biol Reprod , vol.38 , pp. 577-586
    • Stephens, D.T.1    Hickman, R.2    Hoskins, D.D.3
  • 30
    • 0031040893 scopus 로고    scopus 로고
    • Protein kinase A anchoring inhibitor peptides arrest mammalian sperm motility
    • Vijayaraghavan S, Goueli S, Davey MP, Carr DW. Protein kinase A anchoring inhibitor peptides arrest mammalian sperm motility. J Biol Chem 1997; 272:4747-4752.
    • (1997) J Biol Chem , vol.272 , pp. 4747-4752
    • Vijayaraghavan, S.1    Goueli, S.2    Davey, M.P.3    Carr, D.W.4
  • 31
    • 0018997299 scopus 로고
    • Transient flagellar waveforms during intermittent swimming in sea urchin sperm I. Wave parameters
    • Gibbons IR, Gibbons BH. Transient flagellar waveforms during intermittent swimming in sea urchin sperm I. Wave parameters. J Muscle Res Cell Motil 1980; 1:31-59.
    • (1980) J Muscle Res Cell Motil , vol.1 , pp. 31-59
    • Gibbons, I.R.1    Gibbons, B.H.2
  • 32
    • 0018843689 scopus 로고
    • Calcium-induced quiescence in reactivated sea urchin sperm
    • Gibbons BH, Gibbons IR. Calcium-induced quiescence in reactivated sea urchin sperm. J Cell Biol 1980; 84:13-27.
    • (1980) J Cell Biol , vol.84 , pp. 13-27
    • Gibbons, B.H.1    Gibbons, I.R.2
  • 33
    • 0015802035 scopus 로고
    • The stimulation of bovine epididymal sperm metabolism by cyclic nucleotide phosphodiesterase inhibitors
    • Garbers DL, First NL, Lardy HA. The stimulation of bovine epididymal sperm metabolism by cyclic nucleotide phosphodiesterase inhibitors. Biol Reprod 1973; 8:589-598.
    • (1973) Biol Reprod , vol.8 , pp. 589-598
    • Garbers, D.L.1    First, N.L.2    Lardy, H.A.3
  • 34
    • 0022053915 scopus 로고
    • Evidence for a role for cellular alkalinization in the cyclic adenosine 3′,5′-monophosphate-mediated initiation of motility in bovine caput spermatozoa
    • Vijayaraghavan S, Critchlow LM, Hoskins DD. Evidence for a role for cellular alkalinization in the cyclic adenosine 3′,5′-monophosphate-mediated initiation of motility in bovine caput spermatozoa. Biol Reprod 1985; 32:489-500.
    • (1985) Biol Reprod , vol.32 , pp. 489-500
    • Vijayaraghavan, S.1    Critchlow, L.M.2    Hoskins, D.D.3
  • 35
    • 0022654972 scopus 로고
    • Regulation of bovine sperm motility and cyclic adenosine 3′,5′-monophosphate by adenosine and its analogues
    • Vijayaraghavan S, Hoskins DD. Regulation of bovine sperm motility and cyclic adenosine 3′,5′-monophosphate by adenosine and its analogues. Biol Reprod 1986; 34:468-477.
    • (1986) Biol Reprod , vol.34 , pp. 468-477
    • Vijayaraghavan, S.1    Hoskins, D.D.2
  • 36
    • 0000759707 scopus 로고
    • The mammalian spermatozoon: Morphology, biochemistry and physiology
    • Lamming GE (ed.), Edinburgh: Churchill Livingstone
    • Bedford JM, Hoskins DD. The mammalian spermatozoon: morphology, biochemistry and physiology. In: Lamming GE (ed.), Marshall's Physiology of Reproduction. Edinburgh: Churchill Livingstone; 1990: 379.
    • (1990) Marshall's Physiology of Reproduction , pp. 379
    • Bedford, J.M.1    Hoskins, D.D.2
  • 37
    • 0016830715 scopus 로고
    • Induction of motility in immature bovine spermatozoa by cyclic AMP phosphodiesterase inhibitors and seminal plasma
    • Hoskins D, Hall M, Munsterman D. Induction of motility in immature bovine spermatozoa by cyclic AMP phosphodiesterase inhibitors and seminal plasma. Biol Reprod 1975; 13:168-176.
    • (1975) Biol Reprod , vol.13 , pp. 168-176
    • Hoskins, D.1    Hall, M.2    Munsterman, D.3
  • 38
    • 0026793456 scopus 로고
    • Growth factor signaling by receptor tyrosine kinases
    • Schlessinger J, Ullrich A. Growth factor signaling by receptor tyrosine kinases. Neuron 1992; 9:383-391.
    • (1992) Neuron , vol.9 , pp. 383-391
    • Schlessinger, J.1    Ullrich, A.2
  • 39
    • 0028872649 scopus 로고
    • Specificity of receptor tyrosine kinase signalling: Transient versus sustained extracellular signal-regulated kinase activation
    • Marshall CJ. Specificity of receptor tyrosine kinase signalling: transient versus sustained extracellular signal-regulated kinase activation. Cell 1995; 80:179-185.
    • (1995) Cell , vol.80 , pp. 179-185
    • Marshall, C.J.1
  • 40
    • 0024356430 scopus 로고
    • 95 kd Sperm proteins bind ZP3 and serve as tyrosine kinase substrates in response to zona binding
    • Leyton L, Saling P. 95 kd Sperm proteins bind ZP3 and serve as tyrosine kinase substrates in response to zona binding. Cell 1989; 57: 1123-1130.
    • (1989) Cell , vol.57 , pp. 1123-1130
    • Leyton, L.1    Saling, P.2
  • 41
    • 0024424850 scopus 로고
    • Mechanisms of signal transduction in mouse spermatozoa
    • Kopf GS. Mechanisms of signal transduction in mouse spermatozoa. Ann NY Acad Sci 1989; 564:289-302.
    • (1989) Ann NY Acad Sci , vol.564 , pp. 289-302
    • Kopf, G.S.1
  • 42
    • 0027080725 scopus 로고
    • Regulation of mouse gamete interaction by a sperm tyrosine kinase
    • Leyton L, LeGuen P, Bunch D, Saling PM. Regulation of mouse gamete interaction by a sperm tyrosine kinase. Proc Natl Acad Sci USA 1992; 89:11692-11695.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 11692-11695
    • Leyton, L.1    LeGuen, P.2    Bunch, D.3    Saling, P.M.4
  • 43
    • 0028111490 scopus 로고
    • p95, the major phosphotyrosine-containing protein in mouse spermatozoa, is a hexokinase with unique properties
    • Kalab P, Visconti PE, Leclerc P, Kopf GS. p95, the major phosphotyrosine-containing protein in mouse spermatozoa, is a hexokinase with unique properties. J Biol Chem 1994; 269:3810-3817.
    • (1994) J Biol Chem , vol.269 , pp. 3810-3817
    • Kalab, P.1    Visconti, P.E.2    Leclerc, P.3    Kopf, G.S.4
  • 44
    • 4243714048 scopus 로고    scopus 로고
    • Regulation of sperm motility and tyrosine phosphorylation by PKA anchoring inhibitor peptides
    • abstract 721
    • Vijayaraghavan S, Goueli SA, Davey MP, Carr DW. Regulation of sperm motility and tyrosine phosphorylation by PKA anchoring inhibitor peptides. J Cell Biol 1996; 7 (suppl.):124a (abstract 721).
    • (1996) J Cell Biol , vol.7 , Issue.SUPPL.
    • Vijayaraghavan, S.1    Goueli, S.A.2    Davey, M.P.3    Carr, D.W.4
  • 45
    • 0024003066 scopus 로고
    • Calmodulin-stimulated cyclic nucleotide phosphodiesterases in plasma membranes of bovine epididymal spermatozoa
    • Chaudhry PS, Casillas ER. Calmodulin-stimulated cyclic nucleotide phosphodiesterases in plasma membranes of bovine epididymal spermatozoa. Arch Biochem Biophys 1988; 262:439-444.
    • (1988) Arch Biochem Biophys , vol.262 , pp. 439-444
    • Chaudhry, P.S.1    Casillas, E.R.2
  • 46
    • 0015983925 scopus 로고
    • Cyclic adenosine 3′,5′-monophosphate and protein kinase levels in developing bovine spermatozoa
    • Hoskins DD, Stephens DT, Hall ML. Cyclic adenosine 3′,5′-monophosphate and protein kinase levels in developing bovine spermatozoa. J Reprod Fertil 1974; 37:131-133.
    • (1974) J Reprod Fertil , vol.37 , pp. 131-133
    • Hoskins, D.D.1    Stephens, D.T.2    Hall, M.L.3
  • 47
    • 0025217162 scopus 로고
    • Changes in the mitochondrial calcium influx and efflux properties are responsible for the decline in sperm calcium during epididymal maturation
    • Vijayaraghavan S, Hoskins DD. Changes in the mitochondrial calcium influx and efflux properties are responsible for the decline in sperm calcium during epididymal maturation. Mol Reprod Dev 1990; 25: 186-194.
    • (1990) Mol Reprod Dev , vol.25 , pp. 186-194
    • Vijayaraghavan, S.1    Hoskins, D.D.2
  • 48
    • 0024654917 scopus 로고
    • Calcium uptake by bovine epididymal spermatozoa is regulated by the redox state of the mitochondrial pyridine nucleotides
    • Vijayaraghavan S, Bhattacharyya A, Hoskins DD. Calcium uptake by bovine epididymal spermatozoa is regulated by the redox state of the mitochondrial pyridine nucleotides. Biol Reprod 1989; 40:744-751.
    • (1989) Biol Reprod , vol.40 , pp. 744-751
    • Vijayaraghavan, S.1    Bhattacharyya, A.2    Hoskins, D.D.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.