메뉴 건너뛰기




Volumn 88, Issue 1, 1999, Pages 327-336

Neurofilament phosphorylation and axon diameter in the squid giant fibre system

Author keywords

Axon diameter; Electron spectroscopic imaging; Neurofilament phosphorylation; Phosphorylation gradient; Squid giant axon; Squid synapse

Indexed keywords

ANIMAL TISSUE; ARTICLE; CYTOSKELETON; NERVE FIBER; NEUROFILAMENT; NONHUMAN; PRIORITY JOURNAL; PROTEIN PHOSPHORYLATION; SPECTROMETRY; SQUID;

EID: 0032889354     PISSN: 03064522     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0306-4522(98)00244-9     Document Type: Article
Times cited : (30)

References (38)
  • 2
    • 0023372926 scopus 로고
    • Biochemical and immunocytochemical characterization and distribution of phosphorylated and non-phosphorylated subunits of neurofilaments in squid giant axon and stellate ganglion
    • Cohen R. S., Pant H. J., House S., Gainer H. Biochemical and immunocytochemical characterization and distribution of phosphorylated and non-phosphorylated subunits of neurofilaments in squid giant axon and stellate ganglion. J. Neurosci. 7:1987;2056-2074.
    • (1987) J. Neurosci. , vol.7 , pp. 2056-2074
    • Cohen, R.S.1    Pant, H.J.2    House, S.3    Gainer, H.4
  • 3
    • 0028152464 scopus 로고
    • Modulation of axon diameter and neurofilaments by hypomyelinating Schwann cells in transgenic mice
    • Cole J. S., Messing A., Trojanowski J. Q., Lee V. M.-Y. Modulation of axon diameter and neurofilaments by hypomyelinating Schwann cells in transgenic mice. J. Neurosci. 14:1994;6956-6966.
    • (1994) J. Neurosci. , vol.14 , pp. 6956-6966
    • Cole, J.S.1    Messing, A.2    Trojanowski, J.Q.3    Lee, V.M.-Y.4
  • 4
    • 0030816360 scopus 로고    scopus 로고
    • Video densitometric analysis of electron spectroscopic micrographs - A tool for detection of biologically relevant elements with high resolution
    • Door R., Breitig D., Martin R. Video densitometric analysis of electron spectroscopic micrographs - a tool for detection of biologically relevant elements with high resolution. J. Microsc. 187:1997;170-183.
    • (1997) J. Microsc. , vol.187 , pp. 170-183
    • Door, R.1    Breitig, D.2    Martin, R.3
  • 5
    • 0025869515 scopus 로고
    • Estimation of section thickness and quantification of iron standards with EELS
    • Door R., Frösch D., Martin R. Estimation of section thickness and quantification of iron standards with EELS. J. Microsc. 162:1991;15-22.
    • (1991) J. Microsc. , vol.162 , pp. 15-22
    • Door, R.1    Frösch, D.2    Martin, R.3
  • 6
    • 0030833947 scopus 로고    scopus 로고
    • Detection of low phosphorus contents in neurofilaments of squid axons by image-EELS contrast spectroscopy
    • Door R., Richter K., Martin R. Detection of low phosphorus contents in neurofilaments of squid axons by image-EELS contrast spectroscopy. J. Microsc. 188:1997;173-181.
    • (1997) J. Microsc. , vol.188 , pp. 173-181
    • Door, R.1    Richter, K.2    Martin, R.3
  • 7
    • 0028261670 scopus 로고
    • Neurofilament-deficient axons and perikaryal aggregates in viable transgenic mice expressing a neurofilament-β-galactosidase fusion protein
    • Eyer J., Petersen A. Neurofilament-deficient axons and perikaryal aggregates in viable transgenic mice expressing a neurofilament-β-galactosidase fusion protein. Neuron. 12:1994;389-405.
    • (1994) Neuron , vol.12 , pp. 389-405
    • Eyer, J.1    Petersen, A.2
  • 8
    • 0022503140 scopus 로고
    • Calcium-activated proteolysis of neurofilament proteins in the squid giant neuron
    • Gallant P. E., Pant H. C., Pruss R. M., Gainer H. Calcium-activated proteolysis of neurofilament proteins in the squid giant neuron. J. Neurochem. 46:1986;1573-1581.
    • (1986) J. Neurochem. , vol.46 , pp. 1573-1581
    • Gallant, P.E.1    Pant, H.C.2    Pruss, R.M.3    Gainer, H.4
  • 9
    • 0003239212 scopus 로고
    • Protein-chemical characterization of NF-H, the largest mammalian neurofilament component; Intermediate filament-type sequences followed by a unique carboxy-terminal extension
    • Geisler N., Fischer S., Vandekerckhove J., Van Damme J., Plessmann U., Weber K. Protein-chemical characterization of NF-H, the largest mammalian neurofilament component; intermediate filament-type sequences followed by a unique carboxy-terminal extension. Eur. molec. Biol. Org. J. 4:1985;57-63.
    • (1985) Eur. Molec. Biol. Org. J. , vol.4 , pp. 57-63
    • Geisler, N.1    Fischer, S.2    Vandekerckhove, J.3    Van Damme, J.4    Plessmann, U.5    Weber, K.6
  • 10
    • 0023653418 scopus 로고
    • Location and sequence characterization of the major phosphorylation sites of the high molecular mass neurofilament proteins M and H
    • Geisler N., Vandekerckhove J., Weber K. Location and sequence characterization of the major phosphorylation sites of the high molecular mass neurofilament proteins M and H. Fedn Eur. biochem. Socs Lett. 221:1987;403-407.
    • (1987) Fedn Eur. Biochem. Socs Lett. , vol.221 , pp. 403-407
    • Geisler, N.1    Vandekerckhove, J.2    Weber, K.3
  • 12
    • 0002671681 scopus 로고
    • Molecular architecture and dynamics of the neuronal cytoskeleton
    • (ed. Bourgoyn R. D.), Wiley-Liss, New York.
    • Hirokawa N. (1991) Molecular architecture and dynamics of the neuronal cytoskeleton. In The Neuronal Cytoskeleton (ed. Bourgoyn R. D.), pp. 5-74. Wiley-Liss, New York.
    • (1991) In the Neuronal Cytoskeleton , pp. 5-74
    • Hirokawa, N.1
  • 13
    • 0021261943 scopus 로고
    • Organization of mammalian neurofilament polypeptides within the neuronal cytoskeleton
    • Hirokawa N., Glicksman M. A., Willard M. B. Organization of mammalian neurofilament polypeptides within the neuronal cytoskeleton. J. Cell Biol. 98:1984;1523-1536.
    • (1984) J. Cell Biol. , vol.98 , pp. 1523-1536
    • Hirokawa, N.1    Glicksman, M.A.2    Willard, M.B.3
  • 15
    • 0027595786 scopus 로고
    • An inexpensive computer-aided morphometric device for the analysis of dissociated brain cell cultures
    • Kolbinger W., Warchol W. An inexpensive computer-aided morphometric device for the analysis of dissociated brain cell cultures. Comput. Meth. Programs Biomed. 40:1993;3-6.
    • (1993) Comput. Meth. Programs Biomed. , vol.40 , pp. 3-6
    • Kolbinger, W.1    Warchol, W.2
  • 16
    • 0018600329 scopus 로고
    • Identification of the subunit proteins of 10 nm neurofilaments isolated from axoplasm of squid and Myxicola giant axons
    • Lasek R. J., Krishnan N., Kaiserman-Abramoff I. R. Identification of the subunit proteins of 10 nm neurofilaments isolated from axoplasm of squid and Myxicola giant axons. J. Cell Biol. 82:1979;336-346.
    • (1979) J. Cell Biol. , vol.82 , pp. 336-346
    • Lasek, R.J.1    Krishnan, N.2    Kaiserman-Abramoff, I.R.3
  • 17
    • 0029972544 scopus 로고    scopus 로고
    • Neuronal intermediate filaments
    • Lee M. K., Cleveland D. W. Neuronal intermediate filaments. A. Rev. Neurosci. 19:1996;187-217.
    • (1996) A. Rev. Neurosci. , vol.19 , pp. 187-217
    • Lee, M.K.1    Cleveland, D.W.2
  • 18
    • 0022642328 scopus 로고
    • Novel monoclonal antibodies provide evidence for the in situ existence of a non-phosphorylated form of the largest neurofilament subunit
    • Lee V. M.-Y., Carden M. J., Trojanowski J. Q. Novel monoclonal antibodies provide evidence for the in situ existence of a non-phosphorylated form of the largest neurofilament subunit. J. Neurosci. 6:1986;850-858.
    • (1986) J. Neurosci. , vol.6 , pp. 850-858
    • Lee, V.M.-Y.1    Carden, M.J.2    Trojanowski, J.Q.3
  • 19
    • 0029845538 scopus 로고    scopus 로고
    • The structure of the neurofilament cytoskeleton in the squid giant axon and synapse
    • Martin R. The structure of the neurofilament cytoskeleton in the squid giant axon and synapse. J. Neurocytol. 255:1996;547-554.
    • (1996) J. Neurocytol. , vol.255 , pp. 547-554
    • Martin, R.1
  • 20
    • 0027317265 scopus 로고
    • High resolution imaging of protein phosphorylation in squid axons and synapse by electron energy loss spectroscopy
    • Martin R., Door R., Breitig D. High resolution imaging of protein phosphorylation in squid axons and synapse by electron energy loss spectroscopy. J. Histochem. Cytochem. 41:1993;1133-1139.
    • (1993) J. Histochem. Cytochem. , vol.41 , pp. 1133-1139
    • Martin, R.1    Door, R.2    Breitig, D.3
  • 21
    • 0001090410 scopus 로고
    • The form and dimensions of the giant synapse of squids
    • Martin R., Miledi R. The form and dimensions of the giant synapse of squids. Phil. Trans. R. Soc. Lond. B. 312:1986;355-377.
    • (1986) Phil. Trans. R. Soc. Lond. B , vol.312 , pp. 355-377
    • Martin, R.1    Miledi, R.2
  • 22
    • 0025170679 scopus 로고
    • Visualization of differential neurofilament phosphorylation in the pre- And postsynaptic axoplasm of the squid giant synapse: An electron spectroscopic study
    • Martin R., Schilling K., Fritz W., Giuditta A. Visualization of differential neurofilament phosphorylation in the pre- and postsynaptic axoplasm of the squid giant synapse: an electron spectroscopic study. Neuroscience. 37:1990;553-562.
    • (1990) Neuroscience , vol.37 , pp. 553-562
    • Martin, R.1    Schilling, K.2    Fritz, W.3    Giuditta, A.4
  • 23
    • 0028900588 scopus 로고
    • Two distinct functions of the carboxyl-terminal tail domain of NF-M upon neurofilament assembly: Cross bridge formation and longitudinal elongation of filaments
    • Nakagawa T., Chen J., Zhang Z., Kanai Y., Hirokawa N. Two distinct functions of the carboxyl-terminal tail domain of NF-M upon neurofilament assembly: cross bridge formation and longitudinal elongation of filaments. J. Cell Biol. 129:1995;411-429.
    • (1995) J. Cell Biol. , vol.129 , pp. 411-429
    • Nakagawa, T.1    Chen, J.2    Zhang, Z.3    Kanai, Y.4    Hirokawa, N.5
  • 24
    • 0027531842 scopus 로고
    • The regulation of neurofilament protein dynamics by phosphorylation: Clues to neurofibrillary pathobiology
    • Nixon R. A. The regulation of neurofilament protein dynamics by phosphorylation: clues to neurofibrillary pathobiology. Brain Path. 3:1993;29-38.
    • (1993) Brain Path. , vol.3 , pp. 29-38
    • Nixon, R.A.1
  • 25
    • 0027931132 scopus 로고
    • Phosphorylation on carboxyl terminus domains of neurofilament proteins in retinal ganglion cell neurons in vivo: Influences on regional neurofilament accumulation, interneurofilament spacing, and axon caliber
    • Nixon R. A., Paskevichm P. A., Sihak R. K., Thayer C. Y. Phosphorylation on carboxyl terminus domains of neurofilament proteins in retinal ganglion cell neurons in vivo: influences on regional neurofilament accumulation, interneurofilament spacing, and axon caliber. J. Cell Biol. 126:1994;1031-1046.
    • (1994) J. Cell Biol. , vol.126 , pp. 1031-1046
    • Nixon, R.A.1    Paskevichm, P.A.2    Sihak, R.K.3    Thayer, C.Y.4
  • 26
    • 0023387422 scopus 로고
    • Characterization of posttranslational processing of the mammalian high-molecular-weight neurofilament protein in vivo
    • Oblinger M. M. Characterization of posttranslational processing of the mammalian high-molecular-weight neurofilament protein in vivo. J. Neurosci. 7:1987;2510-2520.
    • (1987) J. Neurosci. , vol.7 , pp. 2510-2520
    • Oblinger, M.M.1
  • 27
    • 0020405808 scopus 로고
    • Distribution of calcium-activated protease activity and endogenous substrates in the squid nervous system
    • Pant H. C., Gallant P. E., Gould R., Gainer H. Distribution of calcium-activated protease activity and endogenous substrates in the squid nervous system. J. Neurosci. 2:1982;1578-1587.
    • (1982) J. Neurosci. , vol.2 , pp. 1578-1587
    • Pant, H.C.1    Gallant, P.E.2    Gould, R.3    Gainer, H.4
  • 28
    • 0002918293 scopus 로고
    • Monoclonal antibodies distinguish phosphorylated and nonphosphorylated forms of neurofilaments in situ
    • Sternberger L. A., Sternberger N. H. Monoclonal antibodies distinguish phosphorylated and nonphosphorylated forms of neurofilaments in situ. Proc. natn. Acad. Sci. U.S.A. 80:1983;6126-6130.
    • (1983) Proc. Natn. Acad. Sci. U.S.A. , vol.80 , pp. 6126-6130
    • Sternberger, L.A.1    Sternberger, N.H.2
  • 29
    • 0025787346 scopus 로고
    • Squid low molecular weight neurofilament proteins are a novel class of neurofilament protein
    • Szaro B. G., Pant H. C., Way J., Battey J. Squid low molecular weight neurofilament proteins are a novel class of neurofilament protein. J. biol. Chem. 266:1991;15035-15041.
    • (1991) J. Biol. Chem. , vol.266 , pp. 15035-15041
    • Szaro, B.G.1    Pant, H.C.2    Way, J.3    Battey, J.4
  • 30
    • 0029052277 scopus 로고
    • Overexpression of the human NFM subunit in transgenic mice modifies the level of endogenous NFL and the phosphorylation state of NFH subunits
    • Tu P.-H., Elder G., Lazzarini R. A., Nelson D., Trojanowski J. K., Lee V. M.-Y. Overexpression of the human NFM subunit in transgenic mice modifies the level of endogenous NFL and the phosphorylation state of NFH subunits. J. Cell Biol. 129:1995;1629-1640.
    • (1995) J. Cell Biol. , vol.129 , pp. 1629-1640
    • Tu, P.-H.1    Elder, G.2    Lazzarini, R.A.3    Nelson, D.4    Trojanowski, J.K.5    Lee, V.M.-Y.6
  • 31
    • 0025289033 scopus 로고
    • Characterization of the distinctive neurofilament subunits of the soma and axon initial segments in the squid stellate ganglion
    • Tytell M., Pant H. C., Gainer H., Hill W. D. Characterization of the distinctive neurofilament subunits of the soma and axon initial segments in the squid stellate ganglion. J. Neurosci. Res. 25:1990;153-161.
    • (1990) J. Neurosci. Res. , vol.25 , pp. 153-161
    • Tytell, M.1    Pant, H.C.2    Gainer, H.3    Hill, W.D.4
  • 32
    • 0023946634 scopus 로고
    • Axonal neurofilaments differ in composition and morphology from those in the soma of the squid stellate ganglion
    • Tytell M., Zackroff R. V., Hill W. D. Axonal neurofilaments differ in composition and morphology from those in the soma of the squid stellate ganglion. Cell Motil. Cytoskel. 9:1988;349-360.
    • (1988) Cell Motil. Cytoskel. , vol.9 , pp. 349-360
    • Tytell, M.1    Zackroff, R.V.2    Hill, W.D.3
  • 33
    • 0026580004 scopus 로고
    • Local modulation of neurofilament phosphorylation, axonal caliber, and slow axonal transport by myelinating Schwann cells
    • Waegh S. M. de, Lee M.-Y., Brady S. T. Local modulation of neurofilament phosphorylation, axonal caliber, and slow axonal transport by myelinating Schwann cells. Cell. 68:1992;451-463.
    • (1992) Cell , vol.68 , pp. 451-463
    • De Waegh, S.M.1    Lee, M.-Y.2    Brady, S.T.3
  • 34
    • 0026648109 scopus 로고
    • A high-molecular-weight squid neurofilament protein contains a lamin-like rod domain and a tail domain with Lys-Ser-Pro repeats
    • Way J., Hellmich M. R., Jaffe H., Szaro B., Pant H. C., Gainer H., Battey J. A high-molecular-weight squid neurofilament protein contains a lamin-like rod domain and a tail domain with Lys-Ser-Pro repeats. Proc. natn. Acad. Sci. U.S.A. 89:1992;6963-6967.
    • (1992) Proc. Natn. Acad. Sci. U.S.A. , vol.89 , pp. 6963-6967
    • Way, J.1    Hellmich, M.R.2    Jaffe, H.3    Szaro, B.4    Pant, H.C.5    Gainer, H.6    Battey, J.7
  • 35
    • 0029124072 scopus 로고
    • Increasing NF-M expression reduces axonal NF-H, inhibits radial growth and results in neurofilamentous accumulation in motor neurons
    • Wong P. C., Marszelak J., Crawford T. O., Xu Z.-S., Hsieh S.-T., Griffin J. W., Cleveland D. W. Increasing NF-M expression reduces axonal NF-H, inhibits radial growth and results in neurofilamentous accumulation in motor neurons. J. Cell Biol. 130:1995;1413-1422.
    • (1995) J. Cell Biol. , vol.130 , pp. 1413-1422
    • Wong, P.C.1    Marszelak, J.2    Crawford, T.O.3    Xu, Z.-S.4    Hsieh, S.-T.5    Griffin, J.W.6    Cleveland, D.W.7
  • 36
    • 0000880713 scopus 로고
    • Monte Carlo studies of simple liquid models
    • (eds Temperly H. N. V., Rowlinson J. S. and Rushbrooke G. S.), North-Holland, Amsterdam.
    • Wood W. (1968) Monte Carlo studies of simple liquid models. In Physics of Simple Liquids (eds Temperly H. N. V., Rowlinson J. S. and Rushbrooke G. S.), p. 115. North-Holland, Amsterdam.
    • (1968) In Physics of Simple Liquids , pp. 115
    • Wood, W.1
  • 37
    • 0000529165 scopus 로고
    • Fused neurones and synaptic contacts in the giant nerve fibres of cephalopods
    • Young J. Z. Fused neurones and synaptic contacts in the giant nerve fibres of cephalopods. Phil. Trans. R. Soc. Lond. B. 229:1939;465-503.
    • (1939) Phil. Trans. R. Soc. Lond. B , vol.229 , pp. 465-503
    • Young, J.Z.1
  • 38
    • 0015797258 scopus 로고
    • The giant fibre synapse of Loligo
    • Young J. Z. The giant fibre synapse of Loligo. Brain Res. 57:1973;457-460.
    • (1973) Brain Res. , vol.57 , pp. 457-460
    • Young, J.Z.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.