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Volumn 383, Issue 1, 2004, Pages 149-158

Sputa nerve growth factor forms a preferable substitute to mouse 7S-β nerve growth factor

Author keywords

Naja sputatrix; Nerve growth factor (NGF); Neurite outgrowth; PC12 cells; Sputa NGF

Indexed keywords

CELLS; DNA; GELS; LIVING SYSTEMS STUDIES; PROTEINS;

EID: 6344238883     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20040569     Document Type: Article
Times cited : (13)

References (53)
  • 1
    • 0027218098 scopus 로고
    • Neurotrophins and their receptors - Current concepts and implications for neurologic disease
    • Eide, F. F., Lowenstein, D. H. and Reichardt, L. F. (1993) Neurotrophins and their receptors - current concepts and implications for neurologic disease. Exp. Neural. 121, 200-214
    • (1993) Exp. Neural. , vol.121 , pp. 200-214
    • Eide, F.F.1    Lowenstein, D.H.2    Reichardt, L.F.3
  • 2
    • 0037121659 scopus 로고    scopus 로고
    • Nerve growth factor survival signaling in cultured hippocampal neurons is mediated through TrkA and requires the common neurotrophin receptor P75
    • Culmsee, C., Gerling, N., Lehmann, M., Nikolova-Karakashian, M., Prehn, J. H., Mattson, M. P. and Krieglstein, J. (2002) Nerve growth factor survival signaling in cultured hippocampal neurons is mediated through TrkA and requires the common neurotrophin receptor P75. Neuroscience 115, 1089-1108
    • (2002) Neuroscience , vol.115 , pp. 1089-1108
    • Culmsee, C.1    Gerling, N.2    Lehmann, M.3    Nikolova-Karakashian, M.4    Prehn, J.H.5    Mattson, M.P.6    Krieglstein, J.7
  • 4
    • 0036319594 scopus 로고    scopus 로고
    • p75 neurotrophin receptor is required for constitutive and NGF-induced survival signalling in PC12 cells and rat hippocampal neurones
    • Bui, N. T., Konig, H. G., Culmsee, C., Bauerbach, E., Poppe, M., Krieglstein, J. and Prehn, J. H. (2002) p75 neurotrophin receptor is required for constitutive and NGF-induced survival signalling in PC12 cells and rat hippocampal neurones. J. Neurochem. 81, 594-605
    • (2002) J. Neurochem. , vol.81 , pp. 594-605
    • Bui, N.T.1    Konig, H.G.2    Culmsee, C.3    Bauerbach, E.4    Poppe, M.5    Krieglstein, J.6    Prehn, J.H.7
  • 6
    • 0033024118 scopus 로고    scopus 로고
    • Cloning of a cDNAencoding a nerve growth factor precursor from the Agkistrodon halys Pallas
    • Guo, L. Y., Zhu, J. F., Wu, X. F. and Zhou, Y. C. (1999) Cloning of a cDNAencoding a nerve growth factor precursor from the Agkistrodon halys Pallas. Toxicon 37, 465-470
    • (1999) Toxicon , vol.37 , pp. 465-470
    • Guo, L.Y.1    Zhu, J.F.2    Wu, X.F.3    Zhou, Y.C.4
  • 7
    • 0033679677 scopus 로고    scopus 로고
    • Isolation of nerve growth factor (NGF) from human body fluids; saliva, serum and urine: Comparison between cobra venom and cobra serum NGF
    • Lipps, B. V. (2000) Isolation of nerve growth factor (NGF) from human body fluids; saliva, serum and urine: comparison between cobra venom and cobra serum NGF. J. Nat. Toxins 9, 349-356
    • (2000) J. Nat. Toxins , vol.9 , pp. 349-356
    • Lipps, B.V.1
  • 8
    • 0018238503 scopus 로고
    • Isolation of human nerve growth factor from placental tissue
    • Goldstein, L. D., Reynolds, C. P. and Perez-Polo, J. R. (1978) Isolation of human nerve growth factor from placental tissue. Neurochem. Res. 3, 175-183
    • (1978) Neurochem. Res. , vol.3 , pp. 175-183
    • Goldstein, L.D.1    Reynolds, C.P.2    Perez-Polo, J.R.3
  • 9
    • 0032104406 scopus 로고    scopus 로고
    • Biological and immunological properties of nerve growth factor from snake venoms
    • Lipps, B. V. (1998) Biological and immunological properties of nerve growth factor from snake venoms. J. Nat. Toxins 7, 121-130
    • (1998) J. Nat. Toxins , vol.7 , pp. 121-130
    • Lipps, B.V.1
  • 10
    • 0017294091 scopus 로고
    • Comparison of the nerve growth factor proteins from cobra venom (Naja naja) and mouse submaxillary gland
    • Server, A. C., Herrup, K., Shooter, E. M., Hogue-Angeletti, R. A., Frazier, W. A. and Bradshaw, R. A. (1976) Comparison of the nerve growth factor proteins from cobra venom (Naja naja) and mouse submaxillary gland. Biochemistry 15, 35-39
    • (1976) Biochemistry , vol.15 , pp. 35-39
    • Server, A.C.1    Herrup, K.2    Shooter, E.M.3    Hogue-Angeletti, R.A.4    Frazier, W.A.5    Bradshaw, R.A.6
  • 11
    • 0030199728 scopus 로고    scopus 로고
    • Nerve growth factors from snake venoms: Chemical properties, mode of action and biological significance
    • Kostiza, T. and Meier, J. (1996) Nerve growth factors from snake venoms: chemical properties, mode of action and biological significance. Toxicon 34, 787-806
    • (1996) Toxicon , vol.34 , pp. 787-806
    • Kostiza, T.1    Meier, J.2
  • 13
    • 0345704610 scopus 로고
    • Establishment of a noradrenergic clonal line of rat adrenal pheochromocytoma cells which respond to nerve growth factor
    • Greene, L. A. and Tishler, A. S. (1976) Establishment of a noradrenergic clonal line of rat adrenal pheochromocytoma cells which respond to nerve growth factor. Proc. Natl. Acad. Sci. U.S.A. 73, 2424-2428
    • (1976) Proc. Natl. Acad. Sci. U.S.A. , vol.73 , pp. 2424-2428
    • Greene, L.A.1    Tishler, A.S.2
  • 14
    • 0031024254 scopus 로고    scopus 로고
    • Cloning and characterization of cDNAs encoding three isoforms of phospholipase A2 in Malayan spitting cobra (Naja naja sputatrix) venom
    • Armugam, A., Earnest, L., Chung, M. C. M., Gopalakrishnakone, P., Tan, C. H., Tan, N. H. and Jeyaseelan, K. (1997) Cloning and characterization of cDNAs encoding three isoforms of phospholipase A2 in Malayan spitting cobra (Naja naja sputatrix) venom. Toxicon 35, 27-37
    • (1997) Toxicon , vol.35 , pp. 27-37
    • Armugam, A.1    Earnest, L.2    Chung, M.C.M.3    Gopalakrishnakone, P.4    Tan, C.H.5    Tan, N.H.6    Jeyaseelan, K.7
  • 15
    • 0023277545 scopus 로고
    • Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction
    • Chomczynski, P. and Sacchi, N. (1987) Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction. Anal. Biochem. 162, 156-159
    • (1987) Anal. Biochem. , vol.162 , pp. 156-159
    • Chomczynski, P.1    Sacchi, N.2
  • 18
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • Schagger, H. and Von-Jagow, G. (1987) Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal. Biochem. 166, 368-379
    • (1987) Anal. Biochem. , vol.166 , pp. 368-379
    • Schagger, H.1    Von-Jagow, G.2
  • 19
    • 0037103746 scopus 로고    scopus 로고
    • Cytotoxic potency of cardiotoxin from Naja sputatrix: Development of a new cytolytic assay
    • Ma, D., Armugam, A. and Jeyaseelan, K. (2002) Cytotoxic potency of cardiotoxin from Naja sputatrix: development of a new cytolytic assay. Biochem. J. 366, 35-43
    • (2002) Biochem. J. , vol.366 , pp. 35-43
    • Ma, D.1    Armugam, A.2    Jeyaseelan, K.3
  • 21
    • 0026033032 scopus 로고
    • Amino acid sequences of nerve growth factors derived from cobra venoms
    • Inoue, S., Oda, T., Koyama, J., Ikeda, K. and Hayashi, K. (1991) Amino acid sequences of nerve growth factors derived from cobra venoms. FEBS Lett. 279, 38-40
    • (1991) FEBS Lett. , vol.279 , pp. 38-40
    • Inoue, S.1    Oda, T.2    Koyama, J.3    Ikeda, K.4    Hayashi, K.5
  • 22
    • 0028839771 scopus 로고
    • Nerve growth factor from the venom of the Chinese cobra Naja naja atra: Purification and description of non-neuronal activities
    • Kostiza, T., Dahinden, C. A., Rihs, S., Often, U. and Meier, J. (1995) Nerve growth factor from the venom of the Chinese cobra Naja naja atra: purification and description of non-neuronal activities. Toxicon 33, 1249-1261
    • (1995) Toxicon , vol.33 , pp. 1249-1261
    • Kostiza, T.1    Dahinden, C.A.2    Rihs, S.3    Often, U.4    Meier, J.5
  • 25
    • 2042465006 scopus 로고    scopus 로고
    • The nerve growth factor precursor proNGF exhibits neurotrophic activity but is less active than mature nerve growth factor
    • Fahnestock, M., Yu, G., Michalski, B., Mathew, S., Colquhoun, A., Ross, G. M. and Coughlin, M. D. (2004) The nerve growth factor precursor proNGF exhibits neurotrophic activity but is less active than mature nerve growth factor. J. Neurochem. 89, 581-592
    • (2004) J. Neurochem. , vol.89 , pp. 581-592
    • Fahnestock, M.1    Yu, G.2    Michalski, B.3    Mathew, S.4    Colquhoun, A.5    Ross, G.M.6    Coughlin, M.D.7
  • 26
    • 0025886159 scopus 로고
    • Two conserved domains in the NGF propeptide are necessary and sufficient for the biosynthesis of correctly processed and biologically active NGF
    • Suter, U., Heymach, Jr, J. V. and Shooter, E. M. (1991) Two conserved domains in the NGF propeptide are necessary and sufficient for the biosynthesis of correctly processed and biologically active NGF. EMBO J. 10, 2395-2400
    • (1991) EMBO J. , vol.10 , pp. 2395-2400
    • Suter, U.1    Heymach Jr., J.V.2    Shooter, E.M.3
  • 27
  • 28
    • 0037064037 scopus 로고    scopus 로고
    • Trafficking of TrkA-green fluorescent protein chimerae during nerve growth factor-induced differentiation
    • Jullien, J., Gulli, V., Reichardt, L. F. and Rudkin, B. B. (2002) Trafficking of TrkA-green fluorescent protein chimerae during nerve growth factor-induced differentiation. J. Biol. Chem. 277, 38700-38708
    • (2002) J. Biol. Chem. , vol.277 , pp. 38700-38708
    • Jullien, J.1    Gulli, V.2    Reichardt, L.F.3    Rudkin, B.B.4
  • 29
    • 0033067786 scopus 로고    scopus 로고
    • The anti-p75 antibody, MC192, and brain-derived neurotrophic factor inhibit nerve growth factor-dependent neurite growth from adult sensory neurons
    • Kimpinski, K., Jelinski, S. and Mearow, K. (1999) The anti-p75 antibody, MC192, and brain-derived neurotrophic factor inhibit nerve growth factor-dependent neurite growth from adult sensory neurons. Neuroscience 93, 253-263
    • (1999) Neuroscience , vol.93 , pp. 253-263
    • Kimpinski, K.1    Jelinski, S.2    Mearow, K.3
  • 30
    • 0034667635 scopus 로고    scopus 로고
    • NF-κ B signaling promotes both cell survival and neurite process formation in nerve growth factor-stimulated PC12 cells
    • Foehr, E. D., Lin, X., O'Mahony, A., Geleziunas, R., Bradshaw, R. A. and Greene, W. C. (2000) NF-κ B signaling promotes both cell survival and neurite process formation in nerve growth factor-stimulated PC12 cells. J. Neurosci. 20, 7556-7563
    • (2000) J. Neurosci. , vol.20 , pp. 7556-7563
    • Foehr, E.D.1    Lin, X.2    O'Mahony, A.3    Geleziunas, R.4    Bradshaw, R.A.5    Greene, W.C.6
  • 31
    • 0033979816 scopus 로고    scopus 로고
    • Functional interplay between nuclear factor-κB and c-Jun integrated by coactivator p300 determines the survival of nerve growth factor-dependent PC12 cells
    • Maggirwar, S. B., Ramirez, S., Tong, N., Gelbard, H. A. and Dewhurst, S. (2000) Functional interplay between nuclear factor-κB and c-Jun integrated by coactivator p300 determines the survival of nerve growth factor-dependent PC12 cells. J. Neurochem. 74, 527-539
    • (2000) J. Neurochem. , vol.74 , pp. 527-539
    • Maggirwar, S.B.1    Ramirez, S.2    Tong, N.3    Gelbard, H.A.4    Dewhurst, S.5
  • 32
    • 0027745628 scopus 로고
    • Mechanisms of neurotrophic factor protection against calcium- and free radical-mediated excitotoxic injury: Implications for treating neurodegenerative disorders
    • Mattson, M. P., Cheng, B. and Smith-Swintosky, V. L. (1993) Mechanisms of neurotrophic factor protection against calcium- and free radical-mediated excitotoxic injury: implications for treating neurodegenerative disorders. Exp. Neural. 124, 89-95
    • (1993) Exp. Neural. , vol.124 , pp. 89-95
    • Mattson, M.P.1    Cheng, B.2    Smith-Swintosky, V.L.3
  • 33
    • 0028202461 scopus 로고
    • Deferoxamine posttreatment reduces ischemic brain injury in neonatal rats
    • Palmer, C., Roberts, R. L. and Bero, C. (1994) Deferoxamine posttreatment reduces ischemic brain injury in neonatal rats. Stroke 25, 1039-1045
    • (1994) Stroke , vol.25 , pp. 1039-1045
    • Palmer, C.1    Roberts, R.L.2    Bero, C.3
  • 34
    • 0035021950 scopus 로고    scopus 로고
    • ERK induces p35, a neuron-specific activator of Cdk5, through induction of Egr1
    • Harada, T., Morooka, T., Ogawa, S. and Nishida, E. (2001) ERK induces p35, a neuron-specific activator of Cdk5, through induction of Egr1. Nat. Cell Biol. 3, 453-459
    • (2001) Nat. Cell Biol. , vol.3 , pp. 453-459
    • Harada, T.1    Morooka, T.2    Ogawa, S.3    Nishida, E.4
  • 35
    • 0034890273 scopus 로고    scopus 로고
    • Identification of the human homologue of the early-growth response gene Snk, encoding a serum-inducible kinase
    • Liby, K., Wu, H., Ouyang, B., Wu, S., Chen, J. and Dai, W. (2001) Identification of the human homologue of the early-growth response gene Snk, encoding a serum-inducible kinase. DNA Seq. 11, 527-533
    • (2001) DNA Seq. , vol.11 , pp. 527-533
    • Liby, K.1    Wu, H.2    Ouyang, B.3    Wu, S.4    Chen, J.5    Dai, W.6
  • 37
    • 0038452604 scopus 로고    scopus 로고
    • Expression of the activating transcription factor 3 prevents c-Jun N-terminal kinase-induced neuronal death by promoting heat shock protein 27 expression and Akt activation
    • Nakagomi, S., Suzuki, Y., Namikawa, K., Kiryu-Seo, S. and Kiyama, H. (2003) Expression of the activating transcription factor 3 prevents c-Jun N-terminal kinase-induced neuronal death by promoting heat shock protein 27 expression and Akt activation. J. Neurosci. 23, 5187-5196
    • (2003) J. Neurosci. , vol.23 , pp. 5187-5196
    • Nakagomi, S.1    Suzuki, Y.2    Namikawa, K.3    Kiryu-Seo, S.4    Kiyama, H.5
  • 39
    • 0029835216 scopus 로고    scopus 로고
    • Regulation of cathepsin E expression during human B cell differentiation in vitro
    • Sealy, L., Mota, F., Rayment, N., Tatnell, P., Kay, J. and Chain, B. (1996) Regulation of cathepsin E expression during human B cell differentiation in vitro. Eur. J. Immunol. 26, 1838-1843
    • (1996) Eur. J. Immunol. , vol.26 , pp. 1838-1843
    • Sealy, L.1    Mota, F.2    Rayment, N.3    Tatnell, P.4    Kay, J.5    Chain, B.6
  • 40
    • 0034009825 scopus 로고    scopus 로고
    • Nerve growth factor-β induces mast-cell marker expression during in vitro culture of human umbilical cord blood cells
    • Welker, P., Grabbe, J., Gibbs, B., Zuberbier, T. and Henz, B. M. (2000) Nerve growth factor-β induces mast-cell marker expression during in vitro culture of human umbilical cord blood cells: Immunology 9S, 418-426
    • (2000) Immunology , vol.9 S , pp. 418-426
    • Welker, P.1    Grabbe, J.2    Gibbs, B.3    Zuberbier, T.4    Henz, B.M.5
  • 41
    • 0035397488 scopus 로고    scopus 로고
    • Identification of the glycosylation sites utilized on the Via vasopressin receptor and assessment of their role in receptor signalling and expression
    • Hawtin, S. R., Davies, A. R., Matthews, G. and Wheatley, M. (2001) Identification of the glycosylation sites utilized on the Via vasopressin receptor and assessment of their role in receptor signalling and expression. Biochem. J. 357, 73-81
    • (2001) Biochem. J. , vol.357 , pp. 73-81
    • Hawtin, S.R.1    Davies, A.R.2    Matthews, G.3    Wheatley, M.4
  • 42
    • 0028948773 scopus 로고
    • Localization of the gene (SLC1A3) encoding human glutamate transporter (GluT-1) to 5p13 by fluorescence in situ hybridization
    • Takai, S., Yamada, K., Kawakami, H., Tanaka, K. and Nakamura, S. (1995) Localization of the gene (SLC1A3) encoding human glutamate transporter (GluT-1) to 5p13 by fluorescence in situ hybridization. Cytogenet. Cell Genet. 69, 209-210
    • (1995) Cytogenet. Cell Genet. , vol.69 , pp. 209-210
    • Takai, S.1    Yamada, K.2    Kawakami, H.3    Tanaka, K.4    Nakamura, S.5
  • 43
    • 0035545360 scopus 로고    scopus 로고
    • The α11 T-type calcium channel exhibits faster gating properties when overexpressed in neuroblastoma/glioma NG 108-15 cells
    • Chemin, J., Monteil, A., Dubel, S., Nargeot, J. and Lory, P. (2001) The α11 T-type calcium channel exhibits faster gating properties when overexpressed in neuroblastoma/glioma NG 108-15 cells. Eur. J. Neurosci. 14, 1678-1686.
    • (2001) Eur. J. Neurosci. , vol.14 , pp. 1678-1686
    • Chemin, J.1    Monteil, A.2    Dubel, S.3    Nargeot, J.4    Lory, P.5
  • 45
    • 0030744590 scopus 로고    scopus 로고
    • Cyclooxygenase-1 behaves as a delayed response gene in PC12 cells differentiated by nerve growth factor
    • Kaplan, M. D., Olschowka, J. A. and O'Banion, M. K. (1997) Cyclooxygenase-1 behaves as a delayed response gene in PC12 cells differentiated by nerve growth factor. J. Biol. Chem. 272, 18534-18537
    • (1997) J. Biol. Chem. , vol.272 , pp. 18534-18537
    • Kaplan, M.D.1    Olschowka, J.A.2    O'Banion, M.K.3
  • 46
    • 0033989624 scopus 로고    scopus 로고
    • Interleukin-12 promotes neurite outgrowth in mouse sympathetic superior cervical ganglion neurons
    • Lin, H., Hikawa, N., Takenaka, T. and Ishikawa, Y. (2000) Interleukin-12 promotes neurite outgrowth in mouse sympathetic superior cervical ganglion neurons. Neurosci. Lett. 278, 129-132
    • (2000) Neurosci. Lett. , vol.278 , pp. 129-132
    • Lin, H.1    Hikawa, N.2    Takenaka, T.3    Ishikawa, Y.4
  • 47
    • 0027442194 scopus 로고
    • Receptor-mediated stimulation and inhibition of nerve growth factor secretion by vascular smooth muscle
    • Tuttle, J. B., Etheridge, R. and Creedon, D. J. (1993) Receptor-mediated stimulation and inhibition of nerve growth factor secretion by vascular smooth muscle. Exp. Cell Res. 208, 350-361
    • (1993) Exp. Cell Res. , vol.208 , pp. 350-361
    • Tuttle, J.B.1    Etheridge, R.2    Creedon, D.J.3
  • 48
    • 0031441609 scopus 로고    scopus 로고
    • Facilitation of AVP (4-8) on gene expression of BDNF and NGF in rat brain
    • Zhou, A. W., Li, W. X., Guo, J. and Du, Y. C. (1997) Facilitation of AVP (4-8) on gene expression of BDNF and NGF in rat brain. Peptides 18, 1179-1187
    • (1997) Peptides , vol.18 , pp. 1179-1187
    • Zhou, A.W.1    Li, W.X.2    Guo, J.3    Du, Y.C.4
  • 51
    • 0034633680 scopus 로고    scopus 로고
    • Involvement of neurogranin in the modulation of calcium/calmodulin- dependent protein kinase II, synaptic plasticity, and spatial learning: A study with knockout mice
    • Pak, J. H., Huang, F. L., Li, J., Balschun, D., Reymann, K. G., Chiang, C., Westphal, H. and Huang, K. P. (2000) Involvement of neurogranin in the modulation of calcium/calmodulin-dependent protein kinase II, synaptic plasticity, and spatial learning: a study with knockout mice. Proc. Natl. Acad. Sci. U.S.A. 97, 11232-11237
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 11232-11237
    • Pak, J.H.1    Huang, F.L.2    Li, J.3    Balschun, D.4    Reymann, K.G.5    Chiang, C.6    Westphal, H.7    Huang, K.P.8
  • 52
    • 0345700733 scopus 로고    scopus 로고
    • Postnatal maternal separation elevates the expression of the postsynaptic protein kinase C substrate RC3, but not presynaptic GAP-43, in the developing rat hippocampus
    • McNamara, R. K., Huot, R. L., Lenox, R. H. and Plotsky, P. M. (2002) Postnatal maternal separation elevates the expression of the postsynaptic protein kinase C substrate RC3, but not presynaptic GAP-43, in the developing rat hippocampus. Dev. Neurosci. 24, 485-494
    • (2002) Dev. Neurosci. , vol.24 , pp. 485-494
    • McNamara, R.K.1    Huot, R.L.2    Lenox, R.H.3    Plotsky, P.M.4


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