메뉴 건너뛰기




Volumn 137, Issue 4, 2004, Pages 509-520

Identification of 36 kDa phosphoprotein in fibrous sheath of hamster spermatozoa

Author keywords

Fibrous sheath; Flagellum; Hamster; LC MS MS; Peptide mass finger printing; Phosphorylation; Pyruvate dehydrogenase; Spermatozoa

Indexed keywords

AMINO ACID; CYCLIC AMP; PHOSPHOPROTEIN; PYRUVATE DEHYDROGENASE; SERINE;

EID: 1842664370     PISSN: 10964959     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cbpc.2004.02.006     Document Type: Article
Times cited : (23)

References (50)
  • 1
    • 0033962261 scopus 로고    scopus 로고
    • Effect of ornidazole on fertility of male rats: Inhibition of a glycolysis-related motility pattern and zona binding required for fertilization in vitro
    • Bone W., Jones N.G., Kamp G., Yeung C.H., Cooper T.G. Effect of ornidazole on fertility of male rats: inhibition of a glycolysis-related motility pattern and zona binding required for fertilization in vitro. J. Reprod. Fertil. 118:2000;127-135.
    • (2000) J. Reprod. Fertil. , vol.118 , pp. 127-135
    • Bone, W.1    Jones, N.G.2    Kamp, G.3    Yeung, C.H.4    Cooper, T.G.5
  • 2
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:1976;248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 3
    • 0029185567 scopus 로고
    • Isolation of the dense fibers of mammalian sperm flagella
    • Brito M., Burzio L.O. Isolation of the dense fibers of mammalian sperm flagella. Method Cell Biol. 47:1995a;385-389.
    • (1995) Method Cell Biol. , vol.47 , pp. 385-389
    • Brito, M.1    Burzio, L.O.2
  • 4
    • 0029173944 scopus 로고
    • Isolation of the fibrous sheath of mammalian sperm flagella
    • Brito M., Burzio L.O. Isolation of the fibrous sheath of mammalian sperm flagella. Method Cell Biol. 47:1995b;391-395.
    • (1995) Method Cell Biol. , vol.47 , pp. 391-395
    • Brito, M.1    Burzio, L.O.2
  • 5
    • 0026744628 scopus 로고
    • Cauda epididymal sperm interactions with seminal vesicle fluid
    • Curry P.T., Atherton R.W. Cauda epididymal sperm interactions with seminal vesicle fluid. Mol. Reprod. Dev. 33:1992;67-73.
    • (1992) Mol. Reprod. Dev. , vol.33 , pp. 67-73
    • Curry, P.T.1    Atherton, R.W.2
  • 6
    • 0032724850 scopus 로고    scopus 로고
    • Characterization of the regulatory region of the human testis-specific form of the pyruvate dehydrogenase α-subunit (PDHA-2) gene
    • Datta U., Wexler I.D., Kerr D.S., Raz I., Patel M.S. Characterization of the regulatory region of the human testis-specific form of the pyruvate dehydrogenase α-subunit (PDHA-2) gene. Biochim. Biophys. Acta. 1447:1999;236-243.
    • (1999) Biochim. Biophys. Acta , vol.1447 , pp. 236-243
    • Datta, U.1    Wexler, I.D.2    Kerr, D.S.3    Raz, I.4    Patel, M.S.5
  • 7
    • 0002494818 scopus 로고
    • The spermatozoon
    • E. Knobil, Neill J.D. New York: Raven Press
    • Eddy E.M., O'Brien D.A. The spermatozoon. Knobil E., Neill J.D. The Physiology of Reproduction. 1:1994;29-77 Raven Press, New York.
    • (1994) The Physiology of Reproduction , vol.1 , pp. 29-77
    • Eddy, E.M.1    O'Brien, D.A.2
  • 8
    • 0027114115 scopus 로고
    • Isolation and characterization of the mouse pyruvate dehydrogenase E1α genes
    • Fitzgerald J., Hutchison W.M., Dahl H-H.M. Isolation and characterization of the mouse pyruvate dehydrogenase E1α genes. Biochim. Biophys. Acta. 1131:1992;83-90.
    • (1992) Biochim. Biophys. Acta , vol.1131 , pp. 83-90
    • Fitzgerald, J.1    Hutchison, W.M.2    Dahl, H.-H.M.3
  • 9
    • 0027930457 scopus 로고
    • Differential expression of two testis-specific transcripts of the mouse pdha-2 gene during spermatogenesis
    • Fitzgerald J., Dahl H-H.M., Iannello R.C. Differential expression of two testis-specific transcripts of the mouse pdha-2 gene during spermatogenesis. DNA Cell Biol. 13:1994;531-537.
    • (1994) DNA Cell Biol. , vol.13 , pp. 531-537
    • Fitzgerald, J.1    Dahl, H.-H.M.2    Iannello, R.C.3
  • 10
    • 0002533183 scopus 로고    scopus 로고
    • Serine phosphorylation of flagellar proteins associated with the motility activation of hamster spermatozoa
    • Fujinoki M., Ohtake H., Okuno M. Serine phosphorylation of flagellar proteins associated with the motility activation of hamster spermatozoa. Biomed. Res. 22:2001a;45-58.
    • (2001) Biomed. Res. , vol.22 , pp. 45-58
    • Fujinoki, M.1    Ohtake, H.2    Okuno, M.3
  • 11
    • 0013251793 scopus 로고    scopus 로고
    • Tyrosine phosphorylation and dephosphorylation associated with motility of hamster spermatozoa
    • Fujinoki M., Ohtake H., Okuno M. Tyrosine phosphorylation and dephosphorylation associated with motility of hamster spermatozoa. Biomed. Res. 22:2001b;147-155.
    • (2001) Biomed. Res. , vol.22 , pp. 147-155
    • Fujinoki, M.1    Ohtake, H.2    Okuno, M.3
  • 12
    • 0036890994 scopus 로고    scopus 로고
    • Tropomyosin isoforms present in the sea anemone, Anthopleura japonica (Anthozoa, Cnidaria)
    • Fujinoki M., Tomiyama T., Ishimoda-Takagi T. Tropomyosin isoforms present in the sea anemone, Anthopleura japonica (Anthozoa, Cnidaria). J. Exp. Zool. 293:2002;649-663.
    • (2002) J. Exp. Zool. , vol.293 , pp. 649-663
    • Fujinoki, M.1    Tomiyama, T.2    Ishimoda-Takagi, T.3
  • 13
    • 0242600645 scopus 로고    scopus 로고
    • Identification of 36 kDa flagellar phosphoproteins associated with hamster sperm motility
    • Fujinoki M., Kawamura T., Toda T., Ohtake H., Ishimoda-Takagi T., Shimizu N., et al. Identification of 36 kDa flagellar phosphoproteins associated with hamster sperm motility. J. Biochem. 133:2003;361-369.
    • (2003) J. Biochem. , vol.133 , pp. 361-369
    • Fujinoki, M.1    Kawamura, T.2    Toda, T.3    Ohtake, H.4    Ishimoda-Takagi, T.5    Shimizu, N.6
  • 15
    • 0019785213 scopus 로고
    • Two-dimensional gel electrophoresis of chicken skeletal muscle proteins with agarose gels in the first dimension
    • Hirabayashi T. Two-dimensional gel electrophoresis of chicken skeletal muscle proteins with agarose gels in the first dimension. Anal. Biochem. 117:1981;443-451.
    • (1981) Anal. Biochem. , vol.117 , pp. 443-451
    • Hirabayashi, T.1
  • 16
    • 0026753356 scopus 로고
    • Transcriptional expression of a testis-specific variant of the mouse pyruvate dehydrogenase E1α subunit
    • Iannello R.C., Dahl H-H.M. Transcriptional expression of a testis-specific variant of the mouse pyruvate dehydrogenase E1α subunit. Biol. Reprod. 47:1992;48-58.
    • (1992) Biol. Reprod. , vol.47 , pp. 48-58
    • Iannello, R.C.1    Dahl, H.-H.M.2
  • 17
    • 0031959999 scopus 로고    scopus 로고
    • Proteasomes regulate the motility of salmonid fish sperm through modulation of cAMP-dependent phosphorylation of an outer arm dynein light chain
    • Inaba K., Morisawa S., Morisawa M. Proteasomes regulate the motility of salmonid fish sperm through modulation of cAMP-dependent phosphorylation of an outer arm dynein light chain. J. Cell Sci. 111:1998;1105-1115.
    • (1998) J. Cell Sci. , vol.111 , pp. 1105-1115
    • Inaba, K.1    Morisawa, S.2    Morisawa, M.3
  • 19
    • 0013236925 scopus 로고    scopus 로고
    • Motility-associated and cyclic AMP-dependent protein phosphorylation in the sperm of the chum salmon, Oncorhynchus keta
    • Itoh A., Inaba K., Fujinoki M., Morisawa M. Motility-associated and cyclic AMP-dependent protein phosphorylation in the sperm of the chum salmon, Oncorhynchus keta. Biomed. Res. 22:2001;241-248.
    • (2001) Biomed. Res. , vol.22 , pp. 241-248
    • Itoh, A.1    Inaba, K.2    Fujinoki, M.3    Morisawa, M.4
  • 20
    • 0037566889 scopus 로고    scopus 로고
    • Characterization of a cAMP-dependent protein kinase catalytic subunit from rainbow trout spermatozoa
    • Itoh A., Inaba K., Ohtake H., Fujinoki M., Morisawa M. Characterization of a cAMP-dependent protein kinase catalytic subunit from rainbow trout spermatozoa. Biochem. Biophys. Res. Commun. 305:2003;855-861.
    • (2003) Biochem. Biophys. Res. Commun. , vol.305 , pp. 855-861
    • Itoh, A.1    Inaba, K.2    Ohtake, H.3    Fujinoki, M.4    Morisawa, M.5
  • 21
    • 0022969384 scopus 로고
    • Properties of a newly characterized protein of the bovine kidney pyruvate dehydrogenase complex
    • Jilka J.M., Rahmatullah M., Kazemi M., Roche T.E. Properties of a newly characterized protein of the bovine kidney pyruvate dehydrogenase complex. J. Biol. Chem. 261:1986;1858-1867.
    • (1986) J. Biol. Chem. , vol.261 , pp. 1858-1867
    • Jilka, J.M.1    Rahmatullah, M.2    Kazemi, M.3    Roche, T.E.4
  • 22
    • 0028230419 scopus 로고
    • Role of cAMP in the reactivation of demembranated ram spermatozoa
    • Jovenal T., Agustin S., Witman G.B. Role of cAMP in the reactivation of demembranated ram spermatozoa. Cell Motil. Cytoskel. 27:1994;206-218.
    • (1994) Cell Motil. Cytoskel. , vol.27 , pp. 206-218
    • Jovenal, T.1    Agustin, S.2    Witman, G.B.3
  • 23
    • 0031687185 scopus 로고    scopus 로고
    • Regulation of protein tyrosine phosphorylation in boar sperm through a cAMP-dependent pathway
    • Kaláb P., Pêknicová J., Geussová G., Moos J. Regulation of protein tyrosine phosphorylation in boar sperm through a cAMP-dependent pathway. Mol. Reprod. Dev. 51:1998;304-314.
    • (1998) Mol. Reprod. Dev. , vol.51 , pp. 304-314
    • Kaláb, P.1    Pêknicová, J.2    Geussová, G.3    Moos, J.4
  • 24
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during assembly of the head of bacteriophage T4. Nature. 227:1970;680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 25
    • 0029792629 scopus 로고    scopus 로고
    • Cyclic adenosine 3′,5′ monophosphate-dependent regulation of protein tyrosine phosphorylation in relation to human sperm capacitation and motility
    • Leclerc P., De Lamirande E., Gagnon C. Cyclic adenosine 3′,5′ monophosphate-dependent regulation of protein tyrosine phosphorylation in relation to human sperm capacitation and motility. Biol. Reprod. 55:1996;684-692.
    • (1996) Biol. Reprod. , vol.55 , pp. 684-692
    • Leclerc, P.1    De Lamirande, E.2    Gagnon, C.3
  • 26
    • 0017839969 scopus 로고
    • A cAMP-induced increase in motility of demembranated bull sperm models
    • Lindemann C.B. A cAMP-induced increase in motility of demembranated bull sperm models. Cell. 13:1978;9-18.
    • (1978) Cell , vol.13 , pp. 9-18
    • Lindemann, C.B.1
  • 28
    • 0020045317 scopus 로고
    • Cyclic AMP induces maturation of trout sperm axoneme to initiate motility
    • Morisawa M., Okuno M. Cyclic AMP induces maturation of trout sperm axoneme to initiate motility. Nature. 295:1982;703-704.
    • (1982) Nature , vol.295 , pp. 703-704
    • Morisawa, M.1    Okuno, M.2
  • 29
    • 0021791297 scopus 로고
    • Phosphorylation of a 15K axonemal protein is the trigger initiate trout sperm motility
    • Morisawa M., Hayashi H. Phosphorylation of a 15K axonemal protein is the trigger initiate trout sperm motility. Biomed. Res. 6:1985;181-184.
    • (1985) Biomed. Res. , vol.6 , pp. 181-184
    • Morisawa, M.1    Hayashi, H.2
  • 30
    • 0028520903 scopus 로고
    • Cell signaling mechanisms for sperm motility
    • Morisawa M. Cell signaling mechanisms for sperm motility. Zool. Sci. 11:1994;647-662.
    • (1994) Zool. Sci. , vol.11 , pp. 647-662
    • Morisawa, M.1
  • 31
    • 1842820883 scopus 로고    scopus 로고
    • A novel regulatory system of mouse sperm motility by glucose: The relationship between energy metabolism and motility
    • Mukai C., Okuno M. A novel regulatory system of mouse sperm motility by glucose: the relationship between energy metabolism and motility. Zool. Sci. 19:(Suppl):2002;1435.
    • (2002) Zool. Sci. , vol.19 , Issue.SUPPL , pp. 1435
    • Mukai, C.1    Okuno, M.2
  • 32
    • 0032971198 scopus 로고    scopus 로고
    • Involvement of protein serine and threonine phosphorylation in human sperm capacitation
    • Naz R.K. Involvement of protein serine and threonine phosphorylation in human sperm capacitation. Biol. Reprod. 60:1999;1402-1409.
    • (1999) Biol. Reprod. , vol.60 , pp. 1402-1409
    • Naz, R.K.1
  • 33
    • 0043185695 scopus 로고    scopus 로고
    • Cyclic AMP- and calmodulin-dependent phosphorylation of 21 and 26 kDa proteins in axoneme is a prerequisite for SAAF-induced motile activation in ascidian spermatozoa
    • Nomura M., Inaba K., Morisawa M. Cyclic AMP- and calmodulin-dependent phosphorylation of 21 and 26 kDa proteins in axoneme is a prerequisite for SAAF-induced motile activation in ascidian spermatozoa. Dev. Growth Differ. 42:2000;129-138.
    • (2000) Dev. Growth Differ. , vol.42 , pp. 129-138
    • Nomura, M.1    Inaba, K.2    Morisawa, M.3
  • 34
    • 77956938088 scopus 로고
    • Pyruvate dehydrogenase
    • P.D. Boyer. New York: Academic Press
    • Reed L.J., Yeaman S.J. Pyruvate dehydrogenase. Boyer P.D. The Enzymes. 1987;77-95 Academic Press, New York.
    • (1987) The Enzymes , pp. 77-95
    • Reed, L.J.1    Yeaman, S.J.2
  • 35
    • 0032544711 scopus 로고    scopus 로고
    • The catalytic subunit of the cAMP-dependent protein kinase of ovine sperm flagella has a unique amino-terminal sequence
    • 874-24 883
    • San Agustin J.T., Leszyk J.D., Nuwaysir L.M., Witman G.B. The catalytic subunit of the cAMP-dependent protein kinase of ovine sperm flagella has a unique amino-terminal sequence. J. Biol. Chem. 273:1998;24 874-24 883.
    • (1998) J. Biol. Chem. , vol.273 , pp. 24
    • San Agustin, J.T.1    Leszyk, J.D.2    Nuwaysir, L.M.3    Witman, G.B.4
  • 36
    • 0034492398 scopus 로고    scopus 로고
    • The unique catalytic subunit of sperm cAMP-dependent protein kinase is the product of an alternative Ca mRNA expressed specifically in spermatogenic cells
    • San Agustin J.T., Wilkerson C.G., Witman G.B. The unique catalytic subunit of sperm cAMP-dependent protein kinase is the product of an alternative Ca mRNA expressed specifically in spermatogenic cells. Mol. Biol. Cell. 11:2000;3031-3044.
    • (2000) Mol. Biol. Cell , vol.11 , pp. 3031-3044
    • San Agustin, J.T.1    Wilkerson, C.G.2    Witman, G.B.3
  • 37
    • 0027199204 scopus 로고
    • The sliding of the fibrous sheath through the axoneme proximally together with microtubule extrusion
    • Si Y., Okuno M. The sliding of the fibrous sheath through the axoneme proximally together with microtubule extrusion. Exp. Cell Res. 208:1993;170-174.
    • (1993) Exp. Cell Res. , vol.208 , pp. 170-174
    • Si, Y.1    Okuno, M.2
  • 38
    • 0028850054 scopus 로고
    • Activation of mammalian sperm motility by regulation of microtubule sliding via cyclic adenosine 5′-monophosphate-dependent phosphorylation
    • Si Y., Okuno M. Activation of mammalian sperm motility by regulation of microtubule sliding via cyclic adenosine 5′-monophosphate-dependent phosphorylation. Biol. Reprod. 53:1995;1081-1087.
    • (1995) Biol. Reprod. , vol.53 , pp. 1081-1087
    • Si, Y.1    Okuno, M.2
  • 39
    • 0032924291 scopus 로고    scopus 로고
    • Regulation of microtubule sliding by a 36-kDa phosphoprotein in hamster sperm flagella
    • Si Y., Okuno M. Regulation of microtubule sliding by a 36-kDa phosphoprotein in hamster sperm flagella. Mol. Reprod. Dev. 52:1999a;328-334.
    • (1999) Mol. Reprod. Dev. , vol.52 , pp. 328-334
    • Si, Y.1    Okuno, M.2
  • 40
    • 0033024113 scopus 로고    scopus 로고
    • Role of tyrosine phosphorylation of flagellar proteins in hamster sperm hyperactivation
    • Si Y., Okuno M. Role of tyrosine phosphorylation of flagellar proteins in hamster sperm hyperactivation. Biol. Reprod. 61:1999b;240-246.
    • (1999) Biol. Reprod. , vol.61 , pp. 240-246
    • Si, Y.1    Okuno, M.2
  • 41
    • 0033031174 scopus 로고    scopus 로고
    • Hyperactivation of hamster sperm motility by temperature-dependent tyrosine phosphorylation of an 80-kDa protein
    • Si Y. Hyperactivation of hamster sperm motility by temperature-dependent tyrosine phosphorylation of an 80-kDa protein. Biol. Reprod. 61:1999;247-252.
    • (1999) Biol. Reprod. , vol.61 , pp. 247-252
    • Si, Y.1
  • 42
    • 0026572430 scopus 로고
    • The expression pattern of the pyruvate dehydrogenase E1α subunit genes during spermatogenesis in adult mouse
    • Takakubo F., Dahl H-H.M. The expression pattern of the pyruvate dehydrogenase E1α subunit genes during spermatogenesis in adult mouse. Exp. Cell Res. 199:1992;39-49.
    • (1992) Exp. Cell Res. , vol.199 , pp. 39-49
    • Takakubo, F.1    Dahl, H.-H.M.2
  • 43
    • 0021184785 scopus 로고
    • Flagellar motility requires the cAMP-dependent phosphorylation of a heat-stable NP-40-soluble 56 kd protein, axokinin
    • Tash J.S., Kakar S.S., Means A.R. Flagellar motility requires the cAMP-dependent phosphorylation of a heat-stable NP-40-soluble 56 kd protein, axokinin. Cell. 38:1984;551-559.
    • (1984) Cell , vol.38 , pp. 551-559
    • Tash, J.S.1    Kakar, S.S.2    Means, A.R.3
  • 44
    • 0032552877 scopus 로고    scopus 로고
    • Identification of phosphoproteins coupled to initiation of motility in live epididymal mouse sperm
    • Tash J.S., Bracho G.E. Identification of phosphoproteins coupled to initiation of motility in live epididymal mouse sperm. Biochem. Biophy. Res. Commun. 251:1998;557-563.
    • (1998) Biochem. Biophy. Res. Commun. , vol.251 , pp. 557-563
    • Tash, J.S.1    Bracho, G.E.2
  • 45
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin H., Staehelin T., Gordon J. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. USA. 76:1979;4350-4354.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 46
    • 0343351112 scopus 로고
    • Isoelectric focusing of proteins
    • Vesterberg O. Isoelectric focusing of proteins. Method Enzymol. 22:1971;399-412.
    • (1971) Method Enzymol. , vol.22 , pp. 399-412
    • Vesterberg, O.1
  • 47
    • 0028957362 scopus 로고
    • Capacitation of mouse spermatozoa. I. Correlation between the capacitation state and protein tyrosine phosphorylation
    • Visconti P.E., Bailey J.L., Moore G.D., Pan D., Olds-Clarke P., Kopf G.S. Capacitation of mouse spermatozoa. I. Correlation between the capacitation state and protein tyrosine phosphorylation. Development. 121:1995a;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
  • 48
    • 0028936801 scopus 로고
    • Capacitation of mouse spermatozoa. II. Protein tyrosine phosphorylation and capacitation are regulated by a cAMP-dependent pathway
    • Visconti P.E., Moore G.D., Bailey J.L., Leclerc P., Connors S.A., Pan D., et al. Capacitation of mouse spermatozoa. II. Protein tyrosine phosphorylation and capacitation are regulated by a cAMP-dependent pathway. Development. 121:1995b;1149-1150.
    • (1995) Development , vol.121 , pp. 1149-1150
    • Visconti, P.E.1    Moore, G.D.2    Bailey, J.L.3    Leclerc, P.4    Connors, S.A.5    Pan, D.6
  • 50
    • 0002302562 scopus 로고
    • Mammalian fertilization
    • E. Knobil, Neill J.D. New York: Raven Press
    • Yanagimachi R. Mammalian fertilization. Knobil E., Neill J.D. The Physiology of Reproduction. 1:1994;189-317 Raven Press, New York.
    • (1994) The Physiology of Reproduction , vol.1 , pp. 189-317
    • Yanagimachi, R.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.