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Volumn 37, Issue 4, 2000, Pages 299-306

B2 exon splicing of nonmuscle myosin heavy chain IIB is differently regulated in developing and adult rat brain

Author keywords

Alternative splicing; B2 exon cassette; Brain; Development; Immunohistochemistry; In situ hybridization; Myosin heavy chain; Myosin II

Indexed keywords

ACTIN BINDING PROTEIN; MESSENGER RNA; MYOSIN HEAVY CHAIN;

EID: 0033848433     PISSN: 01680102     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0168-0102(00)00130-9     Document Type: Article
Times cited : (15)

References (41)
  • 1
    • 0028149789 scopus 로고
    • Deficient cerebellar long-term depression and impaired motor learning in mGluR1 mutant mice
    • Aiba A., Kano M., Chen C., Stanton M.E., Fox G.D., Herrup K., Zwingman T.A., Tonegawa S. Deficient cerebellar long-term depression and impaired motor learning in mGluR1 mutant mice. Cell. 79:1994;377-388.
    • (1994) Cell , vol.79 , pp. 377-388
    • Aiba, A.1    Kano, M.2    Chen, C.3    Stanton, M.E.4    Fox, G.D.5    Herrup, K.6    Zwingman, T.A.7    Tonegawa, S.8
  • 2
    • 0015383228 scopus 로고
    • Postnatal development of the cerebellar cortex in the rat. II. Phases in the maturation of Purkinje cells and of the molecular layer
    • Altman J. Postnatal development of the cerebellar cortex in the rat. II. Phases in the maturation of Purkinje cells and of the molecular layer. J. Comp. Neurol. 145:1972;399-464.
    • (1972) J. Comp. Neurol. , vol.145 , pp. 399-464
    • Altman, J.1
  • 3
    • 0029936941 scopus 로고    scopus 로고
    • Conformational changes of smooth endoplasmic reticulum induced by brief anoxia in rat Purkinje cells
    • Banno T., Kohno K. Conformational changes of smooth endoplasmic reticulum induced by brief anoxia in rat Purkinje cells. J. Comp. Neurol. 369:1996;462-471.
    • (1996) J. Comp. Neurol. , vol.369 , pp. 462-471
    • Banno, T.1    Kohno, K.2
  • 4
    • 0032517733 scopus 로고    scopus 로고
    • Conformational changes of the smooth endoplasmic reticulum are facilitated by L-glutamate and its receptors in rat Purkinje cells
    • Banno T., Kohno K. Conformational changes of the smooth endoplasmic reticulum are facilitated by L-glutamate and its receptors in rat Purkinje cells. J. Comp. Neurol. 402:1998;252-263.
    • (1998) J. Comp. Neurol. , vol.402 , pp. 252-263
    • Banno, T.1    Kohno, K.2
  • 5
    • 0027476024 scopus 로고
    • A synaptic model of memory: Long-term potentiation in the hippocampus
    • Bliss T.V.P., Collingridge G.L. A synaptic model of memory: long-term potentiation in the hippocampus. Nature. 361:1993;31-39.
    • (1993) Nature , vol.361 , pp. 31-39
    • Bliss, T.V.P.1    Collingridge, G.L.2
  • 6
    • 0015799240 scopus 로고
    • Long-lasting potentiation of synaptic transmission in the dentate area of the anaesthetized rabbit following stimulation of the perforant path
    • Bliss T.V., Lomo T. Long-lasting potentiation of synaptic transmission in the dentate area of the anaesthetized rabbit following stimulation of the perforant path. J. Physiol. 232:1973;331-356.
    • (1973) J. Physiol. , vol.232 , pp. 331-356
    • Bliss, T.V.1    Lomo, T.2
  • 7
    • 0029798061 scopus 로고    scopus 로고
    • Induction of long-term potentiation is associated with major ultrastructual changes of activated synapses
    • Buchs P.A., Muller D. Induction of long-term potentiation is associated with major ultrastructual changes of activated synapses. Proc. Natl. Acad. Sci. USA. 93:1996;8040-8045.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 8040-8045
    • Buchs, P.A.1    Muller, D.2
  • 8
    • 0026757844 scopus 로고
    • Localization of myosin IIB at the leading edge of growth cones from rat dorsal root ganglionic cells
    • Cheng T.P.O., Murakami N., Elzinga M. Localization of myosin IIB at the leading edge of growth cones from rat dorsal root ganglionic cells. FEBS Lett. 311:1992;91-94.
    • (1992) FEBS Lett. , vol.311 , pp. 91-94
    • Cheng, T.P.O.1    Murakami, N.2    Elzinga, M.3
  • 9
    • 0025356888 scopus 로고
    • Developmental changes of expression of non-muscle (β and γ) actin mRNAs in the central nervous system studied by in situ hybridization
    • Chiba T., Nakamura Y., Sakiyama S. Developmental changes of expression of non-muscle (β and γ) actin mRNAs in the central nervous system studied by in situ hybridization. Neurosci. Lett. 112:1990;31-36.
    • (1990) Neurosci. Lett. , vol.112 , pp. 31-36
    • Chiba, T.1    Nakamura, Y.2    Sakiyama, S.3
  • 11
    • 0032078861 scopus 로고    scopus 로고
    • Rapid actin-based plasticity in dendritic spines
    • Fischer M., Kaech S., Knutti D., Matus A. Rapid actin-based plasticity in dendritic spines. Neuron. 20:1998;847-854.
    • (1998) Neuron , vol.20 , pp. 847-854
    • Fischer, M.1    Kaech, S.2    Knutti, D.3    Matus, A.4
  • 12
    • 0020394540 scopus 로고
    • Cytoplasmic actin in neuronal processes as a possible mediator of synaptic plasticity
    • Fifkova E., Delay R.J. Cytoplasmic actin in neuronal processes as a possible mediator of synaptic plasticity. J. Cell Biol. 95:1982;345-350.
    • (1982) J. Cell Biol. , vol.95 , pp. 345-350
    • Fifkova, E.1    Delay, R.J.2
  • 13
    • 0027052542 scopus 로고
    • Actin matrix of dendritic spines, synaptic plasticity, and long-term potentiation
    • Fifkova E., Morales M. Actin matrix of dendritic spines, synaptic plasticity, and long-term potentiation. Int. Rev. Cytol. 139:1992;267-307.
    • (1992) Int. Rev. Cytol. , vol.139 , pp. 267-307
    • Fifkova, E.1    Morales, M.2
  • 14
    • 0025935249 scopus 로고
    • Induction of long-term potentiation is associated with an increase in the number of axospinous synapses with segmented postsynaptic densities
    • Geinisman Y., deToledo-Morrell L., Morrell F. Induction of long-term potentiation is associated with an increase in the number of axospinous synapses with segmented postsynaptic densities. Brain Res. 566:1991;77-88.
    • (1991) Brain Res. , vol.566 , pp. 77-88
    • Geinisman, Y.1    Detoledo-Morrell, L.2    Morrell, F.3
  • 15
    • 0034007509 scopus 로고    scopus 로고
    • Clustering of δ glutamate receptors is regulated by the actin cytoskeleton in the dendritic spines of cultured rat Purkinje cells
    • Hirai H. Clustering of δ glutamate receptors is regulated by the actin cytoskeleton in the dendritic spines of cultured rat Purkinje cells. Eur. J. Neurosci. 12:2000;563-570.
    • (2000) Eur. J. Neurosci. , vol.12 , pp. 563-570
    • Hirai, H.1
  • 16
    • 0022871572 scopus 로고
    • Long-term depression as a memory process in the cerebellum
    • Ito M. Long-term depression as a memory process in the cerebellum. Neurosci. Res. 3:1986;531-539.
    • (1986) Neurosci. Res. , vol.3 , pp. 531-539
    • Ito, M.1
  • 17
    • 0029008046 scopus 로고
    • Neuronal cell expression of inserted isoforms of vertebrate nonmuscle myosin heavy chain II-B
    • Itoh K., Adelstein R.S. Neuronal cell expression of inserted isoforms of vertebrate nonmuscle myosin heavy chain II-B. J. Biol. Chem. 270:1995;14533-14540.
    • (1995) J. Biol. Chem. , vol.270 , pp. 14533-14540
    • Itoh, K.1    Adelstein, R.S.2
  • 18
    • 0031439662 scopus 로고    scopus 로고
    • Isoform specificity in the relationship of actin to dendritic spines
    • Kaech S., Fischer M., Doll T., Matus A. Isoform specificity in the relationship of actin to dendritic spines. J. Neurosci. 17:1997;9565-9572.
    • (1997) J. Neurosci. , vol.17 , pp. 9565-9572
    • Kaech, S.1    Fischer, M.2    Doll, T.3    Matus, A.4
  • 20
    • 0024438147 scopus 로고
    • Two distinct nonmuscle myosin-heavy-chain mRNAs are differentially expressed in various chicken tissues. Identification of a novel gene family of vertebrate non-sarcomeric myosin heavy chains
    • Katsuragawa Y., Yanagisawa M., Inoue A., Masaki T. Two distinct nonmuscle myosin-heavy-chain mRNAs are differentially expressed in various chicken tissues. Identification of a novel gene family of vertebrate non-sarcomeric myosin heavy chains. Eur. J. Biochem. 184:1989;611-616.
    • (1989) Eur. J. Biochem. , vol.184 , pp. 611-616
    • Katsuragawa, Y.1    Yanagisawa, M.2    Inoue, A.3    Masaki, T.4
  • 21
    • 0026029783 scopus 로고
    • Chicken nonmuscle myosin heavy chains: Differential expression of two mRNAs and evidence for two different polypeptides
    • Kawamoto S., Adelstein R.S. Chicken nonmuscle myosin heavy chains: differential expression of two mRNAs and evidence for two different polypeptides. J. Cell Biol. 112:1991;915-924.
    • (1991) J. Cell Biol. , vol.112 , pp. 915-924
    • Kawamoto, S.1    Adelstein, R.S.2
  • 23
    • 0032559349 scopus 로고    scopus 로고
    • Unconventional myosins in cell movement, membrane traffic, and signal transduction
    • Mermall V., Post P.L., Mooseker M.S. Unconventional myosins in cell movement, membrane traffic, and signal transduction. Science. 279:1998;527-533.
    • (1998) Science , vol.279 , pp. 527-533
    • Mermall, V.1    Post, P.L.2    Mooseker, M.S.3
  • 24
    • 0026557199 scopus 로고
    • Myosin II distribution in neurons is consistent with a role in growth cone motility but not synaptic vesicle mobilization
    • Miller M., Bower E., Levitt P., Li D., Chantler P.D. Myosin II distribution in neurons is consistent with a role in growth cone motility but not synaptic vesicle mobilization. Neuron. 8:1992;25-44.
    • (1992) Neuron , vol.8 , pp. 25-44
    • Miller, M.1    Bower, E.2    Levitt, P.3    Li, D.4    Chantler, P.D.5
  • 25
    • 0027983926 scopus 로고
    • Myosin II is involved in transmitter release at synapses formed between rat sympathetic neurons in culture
    • Mochida S., Kobayashi H., Matsuda Y., Yuda Y., Muramoto K., Nonomura Y. Myosin II is involved in transmitter release at synapses formed between rat sympathetic neurons in culture. Neuron. 13:1994;1131-1142.
    • (1994) Neuron , vol.13 , pp. 1131-1142
    • Mochida, S.1    Kobayashi, H.2    Matsuda, Y.3    Yuda, Y.4    Muramoto, K.5    Nonomura, Y.6
  • 26
    • 0024557848 scopus 로고
    • In situ localization of myosin and actin in dendritic spines with the immunogold technique
    • Morales M., Fifkova E. In situ localization of myosin and actin in dendritic spines with the immunogold technique. J. Comp. Neurol. 279:1989;666-674.
    • (1989) J. Comp. Neurol. , vol.279 , pp. 666-674
    • Morales, M.1    Fifkova, E.2
  • 27
    • 0031013107 scopus 로고    scopus 로고
    • Nonmuscle myosin heavy chain B is recognized by a monoclonal antibody that inhibits GM1-enhanced neuritogenesis
    • Mummert C.M., Schengrund C.L. Nonmuscle myosin heavy chain B is recognized by a monoclonal antibody that inhibits GM1-enhanced neuritogenesis. J. Neurochem. 68:1997;596-600.
    • (1997) J. Neurochem. , vol.68 , pp. 596-600
    • Mummert, C.M.1    Schengrund, C.L.2
  • 28
    • 0026652360 scopus 로고
    • Immunohistochemical studies on the distribution of cellular myosin II isoforms in brain and aorta
    • Murakami N., Elzinga M. Immunohistochemical studies on the distribution of cellular myosin II isoforms in brain and aorta. Cell Motil. Cytoskel. 22:1992;281-295.
    • (1992) Cell Motil. Cytoskel. , vol.22 , pp. 281-295
    • Murakami, N.1    Elzinga, M.2
  • 29
    • 0033405201 scopus 로고    scopus 로고
    • Activity-dependent formation of perforated synapses in cultured hippocampal neurons
    • Neuhoff H., Roeper J., Schweizer M. Activity-dependent formation of perforated synapses in cultured hippocampal neurons. Eur. J. Neurosci. 11:1999;4241-4250.
    • (1999) Eur. J. Neurosci. , vol.11 , pp. 4241-4250
    • Neuhoff, H.1    Roeper, J.2    Schweizer, M.3
  • 31
    • 0029162555 scopus 로고
    • Cloning of the cDNA encoding human nonmuscle myosin heavy chain-B and analysis of human tissues with isoform-specific antibodies
    • Phillips C.L., Yamakawa K., Adelstein R.S. Cloning of the cDNA encoding human nonmuscle myosin heavy chain-B and analysis of human tissues with isoform-specific antibodies. J. Muscle Res. Cell Motil. 16:1995;379-389.
    • (1995) J. Muscle Res. Cell Motil. , vol.16 , pp. 379-389
    • Phillips, C.L.1    Yamakawa, K.2    Adelstein, R.S.3
  • 32
    • 0029586312 scopus 로고
    • Localization of myosin II A and B isoforms in cultured neurons
    • Rochlin M.W., Itoh K., Adelstein R.S., Bridgman P.C. Localization of myosin II A and B isoforms in cultured neurons. J. Cell Sci. 108:1995;3661-3670.
    • (1995) J. Cell Sci. , vol.108 , pp. 3661-3670
    • Rochlin, M.W.1    Itoh, K.2    Adelstein, R.S.3    Bridgman, P.C.4
  • 34
    • 0024755672 scopus 로고
    • In pursuit of myosin function
    • Spudich J.A. In pursuit of myosin function. Cell Reg. 1:1989;1-11.
    • (1989) Cell Reg. , vol.1 , pp. 1-11
    • Spudich, J.A.1
  • 35
    • 0028075752 scopus 로고
    • How molecular motors work
    • Spudich J.A. How molecular motors work. Nature. 372:1994;515-518.
    • (1994) Nature , vol.372 , pp. 515-518
    • Spudich, J.A.1
  • 36
    • 0026774648 scopus 로고
    • Evidence for inserted sequences in the head region of nonmuscle myosin specific to the nervous system. Cloning of the cDNA encoding the myosin heavy chain-B isoform of vertebrate nonmuscle myosin
    • Takahashi M., Kawamoto S., Adelstein R.S. Evidence for inserted sequences in the head region of nonmuscle myosin specific to the nervous system. Cloning of the cDNA encoding the myosin heavy chain-B isoform of vertebrate nonmuscle myosin. J. Biol. Chem. 267:1992;17864-17871.
    • (1992) J. Biol. Chem. , vol.267 , pp. 17864-17871
    • Takahashi, M.1    Kawamoto, S.2    Adelstein, R.S.3
  • 37
    • 0033609351 scopus 로고    scopus 로고
    • Developmentally regulated expression of a nonmuscle myosin heavy chain IIB inserted isoform in rat brain
    • Takahashi M., Hirano T., Uchida K., Yamagishi A. Developmentally regulated expression of a nonmuscle myosin heavy chain IIB inserted isoform in rat brain. Biochem. Biophys. Res. Commun. 259:1999;29-33.
    • (1999) Biochem. Biophys. Res. Commun. , vol.259 , pp. 29-33
    • Takahashi, M.1    Hirano, T.2    Uchida, K.3    Yamagishi, A.4
  • 38
    • 0026709998 scopus 로고
    • Control of nonmuscle myosins by phosphorylation
    • Tan J.L., Ravid S., Spudich J.A. Control of nonmuscle myosins by phosphorylation. Annu. Rev. Biochem. 61:1992;721-759.
    • (1992) Annu. Rev. Biochem. , vol.61 , pp. 721-759
    • Tan, J.L.1    Ravid, S.2    Spudich, J.A.3
  • 41
    • 0032519871 scopus 로고    scopus 로고
    • Differential regional expression and ultrastructual localization of α-actinin-2, a putative NMDA receptor-anchoring protein, in rat brain
    • Wyszynski M., Kharazia V., Shanghvi R., Rao A., Beggs A.H., Craig A.M., Weinberg R., Sheng M. Differential regional expression and ultrastructual localization of α-actinin-2, a putative NMDA receptor-anchoring protein, in rat brain. J. Neurosci. 18:1998;1383-1392.
    • (1998) J. Neurosci. , vol.18 , pp. 1383-1392
    • Wyszynski, M.1    Kharazia, V.2    Shanghvi, R.3    Rao, A.4    Beggs, A.H.5    Craig, A.M.6    Weinberg, R.7    Sheng, M.8


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