메뉴 건너뛰기




Volumn 37, Issue 4, 2005, Pages 293-308

Actin, myosin, cytokeratins and spectrin are components of the guinea pig sperm nuclear matrix

Author keywords

Cytochalasin D; Diacetyl monoxime; Gelsolin; Heparin; Nuclear decondensation; Phalloidin; Protamines

Indexed keywords

ACTIN; ANTIBODY; CYTOCHALASIN D; CYTOKERATIN; DIACETYL OXIME; DNA; F ACTIN; GELSOLIN; HEPARIN; MICROCOCCAL NUCLEASE; MYOSIN; MYOSIN ADENOSINE TRIPHOSPHATASE; NUCLEAR PROTEIN; PHALLOIDIN; SPECTRIN;

EID: 21644440011     PISSN: 00408166     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tice.2005.03.003     Document Type: Article
Times cited : (27)

References (60)
  • 2
    • 0000721357 scopus 로고
    • The purification and properties of micrococcal nuclease
    • M. Alexander L.A. Heppel J. Hurwitz The purification and properties of micrococcal nuclease J. Biol. Chem. 236 1961 3014-3019
    • (1961) J. Biol. Chem. , vol.236 , pp. 3014-3019
    • Alexander, M.1    Heppel, L.A.2    Hurwitz, J.3
  • 3
    • 0026782783 scopus 로고
    • The perinuclear matrix as a structural element of the mouse sperm nucleus
    • A.R. Bellvé R. Chandrika Y.S. Martinova A.H. Barth The perinuclear matrix as a structural element of the mouse sperm nucleus Biol. Reprod. 47 1992 451-465
    • (1992) Biol. Reprod. , vol.47 , pp. 451-465
    • Bellvé, A.R.1    Chandrika, R.2    Martinova, Y.S.3    Barth, A.H.4
  • 4
    • 0029620266 scopus 로고
    • The nuclear matrix: A structural milieu for nuclear genomic function
    • Berezney, R., Jeon, K.W. (Eds.) International Review of Cytology/A Survey of Cell Biology
    • Berezney, R., Mortillaro, M.J., Ma, H., Wei, X., Samarabandu, J., 1995. The nuclear matrix: A structural milieu for nuclear genomic function. In: Berezney, R., Jeon, K.W. (Eds.), Structural and Functional Organization of the Nuclear Matrix. International Review of Cytology/A Survey of Cell Biology, vol. 162A, pp. 1-66.
    • (1995) Structural and Functional Organization of the Nuclear Matrix , vol.162 A , pp. 1-66
    • Berezney, R.1    Mortillaro, M.J.2    Ma, H.3    Wei, X.4    Samarabandu, J.5
  • 5
    • 0033485815 scopus 로고    scopus 로고
    • Study of demembranated, reactivated human spermatozoa with decondensed nuclei
    • H. Bezanehtak M.A. Swan Study of demembranated, reactivated human spermatozoa with decondensed nuclei J. Exp. Zool. 284 1999 789-797
    • (1999) J. Exp. Zool. , vol.284 , pp. 789-797
    • Bezanehtak, H.1    Swan, M.A.2
  • 6
    • 0141730256 scopus 로고    scopus 로고
    • The role of F-actin cytoskeleton-associated gelsolin in the guinea pig capacitation and acrosome reaction
    • J.F. Cabello-Agüeros E.O. Hernández-González A. Mújica The role of F-actin cytoskeleton-associated gelsolin in the guinea pig capacitation and acrosome reaction Cell Motil. Cytoskeleton 56 2003 94-108
    • (2003) Cell Motil. Cytoskeleton , vol.56 , pp. 94-108
    • Cabello-Agüeros, J.F.1    Hernández-González, E.O.2    Mújica, A.3
  • 7
    • 0020162216 scopus 로고
    • The nuclear matrix: Three dimensional architecture and protein composition
    • D.G. Capco K.M. Wan S. Penman The nuclear matrix: Three dimensional architecture and protein composition Cell 29 1982 847-858
    • (1982) Cell , vol.29 , pp. 847-858
    • Capco, D.G.1    Wan, K.M.2    Penman, S.3
  • 8
    • 0019829488 scopus 로고
    • Cytochalasin D inhibits actin polymerization and induces depolymerization of actin filaments formed during platelet shape change
    • J.F. Casella M.D. Flanagan S. Lin Cytochalasin D inhibits actin polymerization and induces depolymerization of actin filaments formed during platelet shape change Nature 293 1981 302-305
    • (1981) Nature , vol.293 , pp. 302-305
    • Casella, J.F.1    Flanagan, M.D.2    Lin, S.3
  • 10
    • 0002638476 scopus 로고
    • The nucleoskeleton: Artefact, passive framework or site active?
    • P.R. Cook The nucleoskeleton: Artefact, passive framework or site active? J. Cell Sci. 90 1988 1-6
    • (1988) J. Cell Sci. , vol.90 , pp. 1-6
    • Cook, P.R.1
  • 11
    • 32644480062 scopus 로고
    • Micrococcal nuclease and some products of its action
    • L. Cunningham Micrococcal nuclease and some products of its action Ann. N.Y. Acad. Sci. 81 1959 788-791
    • (1959) Ann. N.Y. Acad. Sci. , vol.81 , pp. 788-791
    • Cunningham, L.1
  • 14
    • 0016691976 scopus 로고
    • The mammalian spermatozoon
    • D.W. Fawcett The mammalian spermatozoon Dev. Biol. 44 1975 394-436
    • (1975) Dev. Biol. , vol.44 , pp. 394-436
    • Fawcett, D.W.1
  • 15
    • 0023704381 scopus 로고
    • Nuclear matrix proteins reflect cell type of origin in cultured human cells
    • E.G. Fey S. Penman Nuclear matrix proteins reflect cell type of origin in cultured human cells Proc. Natl. Acad. Sci. U.S.A. 85 1988 121-125
    • (1988) Proc. Natl. Acad. Sci. U.S.A. , vol.85 , pp. 121-125
    • Fey, E.G.1    Penman, S.2
  • 17
    • 0028275319 scopus 로고
    • Towards an understandig of nuclear morphogenesis
    • E.D. Georgatos Towards an understandig of nuclear morphogenesis J. Cell. Biochem. 55 1994 69-76
    • (1994) J. Cell. Biochem. , vol.55 , pp. 69-76
    • Georgatos, E.D.1
  • 18
    • 0026317357 scopus 로고
    • Identification of nuclear matrix proteins in the cancer and normal rat prostate
    • R.H. Getzenberg K.J. Pienta E.Y.W. Wang D.S. Coffey Identification of nuclear matrix proteins in the cancer and normal rat prostate Cancer Res. 51 1991 6514-6520
    • (1991) Cancer Res. , vol.51 , pp. 6514-6520
    • Getzenberg, R.H.1    Pienta, K.J.2    Wang, E.Y.W.3    Coffey, D.S.4
  • 19
    • 0025270026 scopus 로고
    • Core filaments of the nuclear matrix
    • D. He J.A. Nickerson S. Penman Core filaments of the nuclear matrix J. Cell Biol. 110 1990 569-580
    • (1990) J. Cell Biol. , vol.110 , pp. 569-580
    • He, D.1    Nickerson, J.A.2    Penman, S.3
  • 20
    • 0028566338 scopus 로고
    • Calmodulin-binding proteins in the membrane vesicles released during the acrosome reaction and in the perinuclear material in isolated acrosome reacted sperm heads
    • E.O. Hernández R. Trejo A.M. Espinosa A. González A. Mújica Calmodulin-binding proteins in the membrane vesicles released during the acrosome reaction and in the perinuclear material in isolated acrosome reacted sperm heads Tissue Cell 26 1994 849-865
    • (1994) Tissue Cell , vol.26 , pp. 849-865
    • Hernández, E.O.1    Trejo, R.2    Espinosa, A.M.3    González, A.4    Mújica, A.5
  • 22
    • 0015582075 scopus 로고
    • Selective solubilization of mammalian spermatozoa structures
    • H. Hernández-Montes G. Iglesias A. Mújica Selective solubilization of mammalian spermatozoa structures Exp. Cell. Res. 76 1973 437-440
    • (1973) Exp. Cell. Res. , vol.76 , pp. 437-440
    • Hernández-Montes, H.1    Iglesias, G.2    Mújica, A.3
  • 23
    • 0028923173 scopus 로고
    • Lamin proteins form an internal nucleoskeleton as well as a peripheral lamina in human cells
    • P. Hozák A.M-J. Sasseville Y. Raymond P. Cook Lamin proteins form an internal nucleoskeleton as well as a peripheral lamina in human cells J. Cell Sci. 108 1995 635-644
    • (1995) J. Cell Sci. , vol.108 , pp. 635-644
    • Hozák, P.1    Sasseville, A.M.-J.2    Raymond, Y.3    Cook, P.4
  • 24
    • 0019347575 scopus 로고
    • In vitro decondensation of human sperm chromatin
    • A. Incharoensakdi S. Panyim In vitro decondensation of human sperm chromatin Andrologia 13 1981 322-329
    • (1981) Andrologia , vol.13 , pp. 322-329
    • Incharoensakdi, A.1    Panyim, S.2
  • 25
    • 0023773201 scopus 로고
    • A gentle method for preparing cyto- and nucleo-skeletons and associated chromatin
    • D.A. Jackson J. Yuan P.R. Cook A gentle method for preparing cyto- and nucleo-skeletons and associated chromatin J. Cell Sci. 90 1988 365-378
    • (1988) J. Cell Sci. , vol.90 , pp. 365-378
    • Jackson, D.A.1    Yuan, J.2    Cook, P.R.3
  • 26
    • 0025646501 scopus 로고
    • Studies on the decondensation of human, mouse and bull sperm nuclei by heparin and other polyanions
    • S. Jager J. Wijchman J. Kremer Studies on the decondensation of human, mouse and bull sperm nuclei by heparin and other polyanions J. Exp. Zool. 256 1990 315-322
    • (1990) J. Exp. Zool. , vol.256 , pp. 315-322
    • Jager, S.1    Wijchman, J.2    Kremer, J.3
  • 27
    • 84907133950 scopus 로고
    • Decondensation of human spermatozoal chromatin by nuclear actin polimerization
    • K. Jamil Decondensation of human spermatozoal chromatin by nuclear actin polimerization Arch. Androl. 13 1984 137-146
    • (1984) Arch. Androl. , vol.13 , pp. 137-146
    • Jamil, K.1
  • 28
    • 0342905060 scopus 로고    scopus 로고
    • A perinuclear theca substructure is formed during epididymal guinea pig sperm maturation and disappears in acrosome reacted cells
    • M.L. Juárez-Mosqueda A. Mújica A perinuclear theca substructure is formed during epididymal guinea pig sperm maturation and disappears in acrosome reacted cells J. Struct. Biol. 128 1999 225-236
    • (1999) J. Struct. Biol. , vol.128 , pp. 225-236
    • Juárez-Mosqueda, M.L.1    Mújica, A.2
  • 29
    • 0001166951 scopus 로고
    • A formaldehyde-glutaraldehyde fixative of high osmolarity for use in electron microscopy
    • M.J. Karnowsky A formaldehyde-glutaraldehyde fixative of high osmolarity for use in electron microscopy J. Cell Biol. 27 1965 137A
    • (1965) J. Cell Biol. , vol.27
    • Karnowsky, M.J.1
  • 30
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • U.K. Laemmli Cleavage of structural proteins during the assembly of the head of bacteriophage T4 Nature 227 1970 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 33
    • 0030111475 scopus 로고    scopus 로고
    • Myosin II function in non-muscle cells
    • S.K. Maciver Myosin II function in non-muscle cells BioEssays 18 1996 179-182
    • (1996) BioEssays , vol.18 , pp. 179-182
    • Maciver, S.K.1
  • 34
    • 5644301011 scopus 로고    scopus 로고
    • Electron microscopic observations of human sperm whole-mounts after extraction for nuclear matrix and intermediate filaments (NM-IF)
    • M.D. Markova Electron microscopic observations of human sperm whole-mounts after extraction for nuclear matrix and intermediate filaments (NM-IF) Int. J. Androl. 27 2004 291-295
    • (2004) Int. J. Androl. , vol.27 , pp. 291-295
    • Markova, M.D.1
  • 35
    • 0026662066 scopus 로고
    • F-actin in guinea pig spermatozoa: Its role in calmodulin traslocation during acrosome reaction
    • L. Moreno-Fierros E.O. Hernández Z.O. Salgado A. Mújica F-actin in guinea pig spermatozoa: Its role in calmodulin traslocation during acrosome reaction Mol. Reprod. Dev. 33 1992 172-181
    • (1992) Mol. Reprod. Dev. , vol.33 , pp. 172-181
    • Moreno-Fierros, L.1    Hernández, E.O.2    Salgado, Z.O.3    Mújica, A.4
  • 36
    • 0019800463 scopus 로고
    • Silver stain for proteins in polyacrylamide gels: A modified procedure with enhanced uniform sensitivity
    • J.H. Morrissey Silver stain for proteins in polyacrylamide gels: A modified procedure with enhanced uniform sensitivity Anal. Biochem. 117 1981 307-310
    • (1981) Anal. Biochem. , vol.117 , pp. 307-310
    • Morrissey, J.H.1
  • 37
    • 0021037294 scopus 로고
    • On the role of glucose in capacitation and acrosomal reaction of guinea pig sperm
    • A. Mújica M.A. Valdes Ruíz On the role of glucose in capacitation and acrosomal reaction of guinea pig sperm Gamete Res. 8 1983 335-344
    • (1983) Gamete Res. , vol.8 , pp. 335-344
    • Mújica, A.1    Valdes Ruíz, M.A.2
  • 38
    • 0029558856 scopus 로고
    • The architectural organization of nuclear metabolism
    • Berezney, R., Jeon, K.W. (Eds.) International Review of Citology/A Survey of Cell Biology
    • Nickerson, J.A., Blencowe, B.J., Penman, S., 1995. The architectural organization of nuclear metabolism. In: Berezney, R., Jeon, K.W. (Eds.), Structural and Functional Organization of the Nuclear Matrix. International Review of Citology/A Survey of Cell Biology. vol. 162A, pp. 67-224.
    • (1995) Structural and Functional Organization of the Nuclear Matrix , vol.162 A , pp. 67-224
    • Nickerson, J.A.1    Blencowe, B.J.2    Penman, S.3
  • 39
    • 0025261920 scopus 로고
    • Immunolocalization in three dimensions: Immunogold staining of cytoskeletal and nuclear matrix proteins in resinless electron microscopy sections
    • J.A. Nickerson G. Krockmalnic H. Dacheng S. Penman Immunolocalization in three dimensions: Immunogold staining of cytoskeletal and nuclear matrix proteins in resinless electron microscopy sections Proc. Natl. Acad. Sci. U.S.A. 87 1990 2259-2263
    • (1990) Proc. Natl. Acad. Sci. U.S.A. , vol.87 , pp. 2259-2263
    • Nickerson, J.A.1    Krockmalnic, G.2    Dacheng, H.3    Penman, S.4
  • 40
    • 0014478325 scopus 로고
    • High resolution acrylamide gel electrophoresis of histones
    • S. Panyim R. Chalkley High resolution acrylamide gel electrophoresis of histones Arch. Biochem. Biophys. 130 1969 337-346
    • (1969) Arch. Biochem. Biophys. , vol.130 , pp. 337-346
    • Panyim, S.1    Chalkley, R.2
  • 42
    • 0021318182 scopus 로고
    • The role of disulfide bond reduction during mammalian sperm nuclear decondensation in vivo
    • D.S. Perreault R.A. Wolff B.R. Zirkin The role of disulfide bond reduction during mammalian sperm nuclear decondensation in vivo Dev. Biol. 101 1984 160-167
    • (1984) Dev. Biol. , vol.101 , pp. 160-167
    • Perreault, D.S.1    Wolff, R.A.2    Zirkin, B.R.3
  • 43
    • 0028279510 scopus 로고
    • Coupling of cell structure to cell metabolism and function
    • K.J. Pienta C.N. Hoover Coupling of cell structure to cell metabolism and function J. Cell. Biochem. 55 1994 16-21
    • (1994) J. Cell. Biochem. , vol.55 , pp. 16-21
    • Pienta, K.J.1    Hoover, C.N.2
  • 44
    • 0017183616 scopus 로고
    • The heterogeneity of the protamines from human spermatozoa
    • P. Pongsawasdi J. Svasti The heterogeneity of the protamines from human spermatozoa Biochim. Biophys. Acta 434 1976 462-473
    • (1976) Biochim. Biophys. Acta , vol.434 , pp. 462-473
    • Pongsawasdi, P.1    Svasti, J.2
  • 47
    • 0017902242 scopus 로고
    • 2+-dependent class of thick filaments and correlated nuclei chromatin condensation in catfish photoreceptors
    • 2+-dependent class of thick filaments and correlated nuclei chromatin condensation in catfish photoreceptors J. Neurocytol. 7 1978 313-321
    • (1978) J. Neurocytol. , vol.7 , pp. 313-321
    • Ryan, T.1    Potter, H.D.2
  • 50
    • 0028049984 scopus 로고
    • An actin infrastructure is associated with eukaryotic chromosomes: Structural and functional significance
    • I. Sauman S.J. Berry An actin infrastructure is associated with eukaryotic chromosomes: Structural and functional significance Eur. J. Cell Biol. 64 1994 348-356
    • (1994) Eur. J. Cell Biol. , vol.64 , pp. 348-356
    • Sauman, I.1    Berry, S.J.2
  • 51
    • 0020487454 scopus 로고
    • Transmission and scanning electron microscopic studies of the human sperm chromatin decondensed by microccocal nuclease and salt
    • P. Sobhon C. Chutatape P. Chalermisarachai P. Vongpayabal N. Tanphaichitr Transmission and scanning electron microscopic studies of the human sperm chromatin decondensed by microccocal nuclease and salt J. Exp. Zool. 221 1982 61-79
    • (1982) J. Exp. Zool. , vol.221 , pp. 61-79
    • Sobhon, P.1    Chutatape, C.2    Chalermisarachai, P.3    Vongpayabal, P.4    Tanphaichitr, N.5
  • 52
    • 0036073008 scopus 로고    scopus 로고
    • ROCK-II-induced membrane blebbing and chromatin condensation require actin cytoskeleton
    • Y. Song B.Q. Hoang D.D. Chang ROCK-II-induced membrane blebbing and chromatin condensation require actin cytoskeleton Exp. Cell Res. 278 2002 45-52
    • (2002) Exp. Cell Res. , vol.278 , pp. 45-52
    • Song, Y.1    Hoang, B.Q.2    Chang, D.D.3
  • 53
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from poliacrilamide gels to nitrocellulose sheets: Procedure and some applications
    • H. Towbin T. Staenhelin J. Gordon Electrophoretic transfer of proteins from poliacrilamide gels to nitrocellulose sheets: Procedure and some applications Proc. Natl. Acad. Sci. U.S.A. 76 1979 4350-4354
    • (1979) Proc. Natl. Acad. Sci. U.S.A. , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staenhelin, T.2    Gordon, J.3
  • 54
    • 0025179017 scopus 로고
    • Changes in calmodulin compartmentalization throughout capacitation and acrosome reaction in guinea pig-spermatozoa
    • R. Trejo A. Mújica Changes in calmodulin compartmentalization throughout capacitation and acrosome reaction in guinea pig-spermatozoa Mol. Reprod. Dev. 26 1990 366-376
    • (1990) Mol. Reprod. Dev. , vol.26 , pp. 366-376
    • Trejo, R.1    Mújica, A.2
  • 55
    • 0027283328 scopus 로고
    • Ultrastructure and immunocytochemistry of the isolated human erythrocyte membrane skeleton
    • J.A. Ursitti J.B. Wade Ultrastructure and immunocytochemistry of the isolated human erythrocyte membrane skeleton Cell Motil. Cytoskeleton 25 1993 30-42
    • (1993) Cell Motil. Cytoskeleton , vol.25 , pp. 30-42
    • Ursitti, J.A.1    Wade, J.B.2
  • 57
    • 0028285481 scopus 로고
    • The structure of the sleeping genome: Implications of sperm DNA organization for somatic cells
    • W.S. Ward The structure of the sleeping genome: Implications of sperm DNA organization for somatic cells J. Cell. Biochem. 55 1994 77-82
    • (1994) J. Cell. Biochem. , vol.55 , pp. 77-82
    • Ward, W.S.1
  • 58
    • 0025818959 scopus 로고
    • DNA packaging and organization in mammalian spermatozoa: Comparison with somatic cells
    • W.S. Ward D. Coffey DNA packaging and organization in mammalian spermatozoa: Comparison with somatic cells Biol. Reprod. 44 1991 569-574
    • (1991) Biol. Reprod. , vol.44 , pp. 569-574
    • Ward, W.S.1    Coffey, D.2
  • 59
    • 0002302562 scopus 로고
    • Mammalian fertilization
    • E. Knobil E.J. y Neill (Eds.) Raven Press New York, USA
    • R. Yanagimachi Mammalian fertilization In: E. Knobil E.J. y Neill (Eds.) The Physiology of Reproduction vol. 1 1994 Raven Press New York, USA 1390
    • (1994) The Physiology of Reproduction , vol.1 , pp. 1390
    • Yanagimachi, R.1
  • 60
    • 0022255941 scopus 로고
    • In vitro and in vivo studies of mammalian sperm nuclear decondensation
    • B.R. Zirkin D.A. Soucek T.S.K. Chang S.D. Perreault In vitro and in vivo studies of mammalian sperm nuclear decondensation Gamete Res. 11 1985 349-365
    • (1985) Gamete Res. , vol.11 , pp. 349-365
    • Zirkin, B.R.1    Soucek, D.A.2    Chang, T.S.K.3    Perreault, S.D.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.