메뉴 건너뛰기




Volumn 20, Issue 11, 2000, Pages 4059-4068

Neurotrophin-3 sorts to the constitutive secretory pathway of hippocampal neurons and is diverted to the regulated secretory pathway by coexpression with brain-derived neurotrophic factor

Author keywords

BDNF; Constitutive pathway; Heterodimer; Neurotrophin; NT 3; Regulated secretory pathway

Indexed keywords

BRAIN DERIVED NEUROTROPHIC FACTOR; NERVE GROWTH FACTOR; NEUROTROPHIN 3;

EID: 0034212624     PISSN: 02706474     EISSN: None     Source Type: Journal    
DOI: 10.1523/jneurosci.20-11-04059.2000     Document Type: Article
Times cited : (112)

References (55)
  • 1
    • 0025880071 scopus 로고
    • Detection of brain-derived neurotrophic factor-like activity in fibroblasts and Schwann cells: Inhibition by antibodies to NGF
    • Acheson A, Barker PA, Alderson RF, Miller FD, Murphy RA (1991) Detection of brain-derived neurotrophic factor-like activity in fibroblasts and Schwann cells: inhibition by antibodies to NGF. Neuron 7:265-275.
    • (1991) Neuron , vol.7 , pp. 265-275
    • Acheson, A.1    Barker, P.A.2    Alderson, R.F.3    Miller, F.D.4    Murphy, R.A.5
  • 3
    • 0000429264 scopus 로고    scopus 로고
    • Neurotrophin trafficking by anterograde transport
    • Altar CA, DiStefano PS (1998) Neurotrophin trafficking by anterograde transport. Trends Neurosci 21:433-437.
    • (1998) Trends Neurosci , vol.21 , pp. 433-437
    • Altar, C.A.1    Distefano, P.S.2
  • 4
    • 0027429771 scopus 로고
    • Inhibition of HIV-1 gp160-dependent membrane fusion by a furin-directed α1-antitrypsin variant
    • Anderson FD, Thomas L, Hayflick JS, Thomas G (1993) Inhibition of HIV-1 gp160-dependent membrane fusion by a furin-directed α1-antitrypsin variant. J Biol Chem 268:24887-24891.
    • (1993) J Biol Chem , vol.268 , pp. 24887-24891
    • Anderson, F.D.1    Thomas, L.2    Hayflick, J.S.3    Thomas, G.4
  • 6
    • 0017350927 scopus 로고
    • Rat hippocampal neurons in dispersed cell culture
    • Banker GA, Cowan WM (1977) Rat hippocampal neurons in dispersed cell culture. Brain Res 126:397-442.
    • (1977) Brain Res , vol.126 , pp. 397-442
    • Banker, G.A.1    Cowan, W.M.2
  • 7
    • 0030611878 scopus 로고    scopus 로고
    • α1-antitrypsin Portland inhibits processing of precursors mediated by pro-protein convertases primarily within the constitutive secretory pathway
    • Benjannet S, Savaria D, Laslop A, Munzer JC, Chretien M, Marcinkiewicz M, Seidah NG (1997) α1-antitrypsin Portland inhibits processing of precursors mediated by pro-protein convertases primarily within the constitutive secretory pathway. J Biol Chem 272:26210-26218.
    • (1997) J Biol Chem , vol.272 , pp. 26210-26218
    • Benjannet, S.1    Savaria, D.2    Laslop, A.3    Munzer, J.C.4    Chretien, M.5    Marcinkiewicz, M.6    Seidah, N.G.7
  • 9
    • 0026739387 scopus 로고
    • Differential sorting of lutropin and the free α-subunit in cultured bovine pituitary cells
    • Blomquist JF, Baenziger JU (1992) Differential sorting of lutropin and the free α-subunit in cultured bovine pituitary cells. J Biol Chem 267:20798-20803.
    • (1992) J Biol Chem , vol.267 , pp. 20798-20803
    • Blomquist, J.F.1    Baenziger, J.U.2
  • 10
    • 0029787008 scopus 로고    scopus 로고
    • A protease processing site is essential for prorenin sorting to the regulated secretory pathway
    • Brechler V, Chu WN, Baxter JD, Thibault G, Reudelhuher TL (1996) A protease processing site is essential for prorenin sorting to the regulated secretory pathway, J Biol Chem 271:20636-20640.
    • (1996) J Biol Chem , vol.271 , pp. 20636-20640
    • Brechler, V.1    Chu, W.N.2    Baxter, J.D.3    Thibault, G.4    Reudelhuher, T.L.5
  • 11
    • 0027226219 scopus 로고
    • Optimized survival of hippocampal neurons in B27-supplemented neurobasal, a new serum-free medium combination
    • Brewer GJ, Torricelli JR, Evege EK, Price PJ (1993) Optimized survival of hippocampal neurons in B27-supplemented Neurobasal, a new serum-free medium combination. J Neurosci Res 35:567-576.
    • (1993) J Neurosci Res , vol.35 , pp. 567-576
    • Brewer, G.J.1    Torricelli, J.R.2    Evege, E.K.3    Price, P.J.4
  • 12
    • 0030078595 scopus 로고    scopus 로고
    • Neurotrophin-3 as an essential signal for the developing nervous system
    • Chalazonitis A (1996) Neurotrophin-3 as an essential signal for the developing nervous system. Mol Neurobiol 12:39-53.
    • (1996) Mol Neurobiol , vol.12 , pp. 39-53
    • Chalazonitis, A.1
  • 13
    • 0033568871 scopus 로고    scopus 로고
    • Relative contribution of endogenous neurotrophins in hippocampal long-term potentiation
    • Chen G, Kolheck R, Barde YA, Bonhoeffer T, Kossel A (1999) Relative contribution of endogenous neurotrophins in hippocampal long-term potentiation. J Neurosci 19:7983-7990.
    • (1999) J Neurosci , vol.19 , pp. 7983-7990
    • Chen, G.1    Kolheck, R.2    Barde, Y.A.3    Bonhoeffer, T.4    Kossel, A.5
  • 14
    • 0025042577 scopus 로고
    • Perturbation ol intestinal microvillar enzyme biosynthesis by amino acid analogs. Evidence that dimerization is required for the transport of aminopeptidase N out of the endoplasmic reticulum
    • Danielsen HM (1990) Perturbation ol intestinal microvillar enzyme biosynthesis by amino acid analogs. Evidence that dimerization is required for the transport of aminopeptidase N out of the endoplasmic reticulum J Biol Chem 265:14566-14571.
    • (1990) J Biol Chem , vol.265 , pp. 14566-14571
    • Danielsen, H.M.1
  • 16
    • 0024027151 scopus 로고
    • Processing and secretion of nerve growth factor: Expression in mammalian cells with a vaccinia virus vector
    • Edwards RH, Selby MJ, Mobky WC, Weinrich SL, Hruhy DE, Rutter WJ (1988) Processing and secretion of nerve growth factor: expression in mammalian cells with a vaccinia virus vector. Mol Cell Biol 8:2456-2464.
    • (1988) Mol Cell Biol , vol.8 , pp. 2456-2464
    • Edwards, R.H.1    Selby, M.J.2    Mobky, W.C.3    Weinrich, S.L.4    Hruhy, D.E.5    Rutter, W.J.6
  • 17
    • 0343113182 scopus 로고    scopus 로고
    • Constitutively secreted neurotrophin-3 can be directed to the regulated secretory pathway by dimerization with BDNF
    • 318.3
    • Farhadi HF, Mowla SJ, Petrecca K, Morris SJ, Seidah NG, Murphy RA (1998) Constitutively secreted neurotrophin-3 can be directed to the regulated secretory pathway by dimerization with BDNF. Soc Neurosci Abstr 28:318.3.
    • (1998) Soc Neurosci Abstr , vol.28
    • Farhadi, H.F.1    Mowla, S.J.2    Petrecca, K.3    Morris, S.J.4    Seidah, N.G.5    Murphy, R.A.6
  • 19
    • 0033995149 scopus 로고    scopus 로고
    • Evidence that brain-derived neurotrophic factor from presynaptic nerve terminals regulates the phenotype of calbindin-containing neurons in the lateral septum
    • Fawcett JP, Alonso-Vanegas MA, Morris SJ, Miller FD, Sadikot AF, Murphy RA (2000) Evidence that brain-derived neurotrophic factor from presynaptic nerve terminals regulates the phenotype of calbindin-containing neurons in the lateral septum. J Neurosci 20:274-282.
    • (2000) J Neurosci , vol.20 , pp. 274-282
    • Fawcett, J.P.1    Alonso-Vanegas, M.A.2    Morris, S.J.3    Miller, F.D.4    Sadikot, A.F.5    Murphy, R.A.6
  • 21
    • 0029010194 scopus 로고
    • The biosynthesis of neurotrophin heterodimers by transfected mammalian cells
    • Heymach JV, Shooter EM (1995) The biosynthesis of neurotrophin heterodimers by transfected mammalian cells. J Biol Chem 270:12297-12304.
    • (1995) J Biol Chem , vol.270 , pp. 12297-12304
    • Heymach, J.V.1    Shooter, E.M.2
  • 22
    • 0029845927 scopus 로고    scopus 로고
    • The regulated secretion and vectorial targeting of neurotrophins in neuroendocrine and epithelial cells
    • Heymach JV, Kruttgen A, Suter U, Shooter EM (1996) The regulated secretion and vectorial targeting of neurotrophins in neuroendocrine and epithelial cells. J Biol Chem 271:254300-25437.
    • (1996) J Biol Chem , vol.271 , pp. 254300-325437
    • Heymach, J.V.1    Kruttgen, A.2    Suter, U.3    Shooter, E.M.4
  • 23
    • 0025763281 scopus 로고
    • Peptide processing and targeting in the neuronal secretory pathway
    • Jung LJ, Scheller RH (1991) Peptide processing and targeting in the neuronal secretory pathway. Science 251:1330-1335.
    • (1991) Science , vol.251 , pp. 1330-1335
    • Jung, L.J.1    Scheller, R.H.2
  • 24
    • 0028177535 scopus 로고
    • Purification and characterisation of a brain-derived neurotrophic factor/neurotrophin-3 (BDNF/ NT-3) heterodimer
    • Jungbluth S, Bailey K, Barde YA (1994) Purification and characterisation of a brain-derived neurotrophic factor/neurotrophin-3 (BDNF/ NT-3) heterodimer. Eur J Biochem 221:677-685.
    • (1994) Eur J Biochem , vol.221 , pp. 677-685
    • Jungbluth, S.1    Bailey, K.2    Barde, Y.A.3
  • 25
    • 0028988240 scopus 로고
    • Long-lasting neurotrophin-induced enhancement of synaptic transmission in the adult hippocampus
    • Kang H, Schuman EM (1995) Long-lasting neurotrophin-induced enhancement of synaptic transmission in the adult hippocampus. Science 267:1658-1662.
    • (1995) Science , vol.267 , pp. 1658-1662
    • Kang, H.1    Schuman, E.M.2
  • 26
    • 0033613422 scopus 로고    scopus 로고
    • Neurotrophin-evoked rapid excitation through TrkB receptors
    • Kafitz KW, Rose CR, Thoenen H, Konnerth A (1999) Neurotrophin-evoked rapid excitation through TrkB receptors. Nature 401:918-921.
    • (1999) Nature , vol.401 , pp. 918-921
    • Kafitz, K.W.1    Rose, C.R.2    Thoenen, H.3    Konnerth, A.4
  • 27
    • 0033009090 scopus 로고    scopus 로고
    • Brain-derived neurotrophic factor levels in the nervous system of wild-type and neurotrophin gene mutant mice
    • Kolbeck R, Bartke I, Eberle W, Barde YA (1999) Brain-derived neurotrophic factor levels in the nervous system of wild-type and neurotrophin gene mutant mice. J Neurochem 72:1930-1938.
    • (1999) J Neurochem , vol.72 , pp. 1930-1938
    • Kolbeck, R.1    Bartke, I.2    Eberle, W.3    Barde, Y.A.4
  • 28
    • 0029021177 scopus 로고
    • Hippocampal long-term potentiation is impaired in mice lacking brain-derived neurotrophic factor
    • Korte M, Carroll P, Wolff E, Brem G, Thoenen H, Bonhoeffer T (1995) Hippocampal long-term potentiation is impaired in mice lacking brain-derived neurotrophic factor. Proe Natl Acad Sci USA 92:8856-8860.
    • (1995) Proe Natl Acad Sci USA , vol.92 , pp. 8856-8860
    • Korte, M.1    Carroll, P.2    Wolff, E.3    Brem, G.4    Thoenen, H.5    Bonhoeffer, T.6
  • 29
    • 0025148186 scopus 로고
    • Identification, sequencing, and expression of an internal membrane protein of the trans-Golgi network (TGN38)
    • Luzio JP, Brake B, Banting G, Howell KE, Bragetta P, Stanley KK (1990) Identification, sequencing, and expression of an internal membrane protein of the trans-Golgi network (TGN38). Biochem J 270:97-102.
    • (1990) Biochem J , vol.270 , pp. 97-102
    • Luzio, J.P.1    Brake, B.2    Banting, G.3    Howell, K.E.4    Bragetta, P.5    Stanley, K.K.6
  • 30
    • 0032853797 scopus 로고    scopus 로고
    • Neuronal NT-3 is not required for synaptic transmission or long-term potentiation in area CA1 of the adult rat hippocampus
    • Ma L, Reis G, Parada LE, Schuman EM (1999) Neuronal NT-3 is not required for synaptic transmission or long-term potentiation in area CA1 of the adult rat hippocampus. Learn Mem 6:267-275.
    • (1999) Learn Mem , vol.6 , pp. 267-275
    • Ma, L.1    Reis, G.2    Parada, L.E.3    Schuman, E.M.4
  • 33
    • 0030776204 scopus 로고    scopus 로고
    • Nerve growth factor treatment increases brain-derived neurotrophic factor selectively in TrkA-expressing dorsal root ganglion cells and in their central terminations within the spinal cord
    • Michael GJ, Averill S, Nitkunan A, Rattray M, Bennett DLH, Yan Q, Priestly JV (1997) Nerve growth factor treatment increases brain-derived neurotrophic factor selectively in TrkA-expressing dorsal root ganglion cells and in their central terminations within the spinal cord. J Neurosci 17:8476-8490.
    • (1997) J Neurosci , vol.17 , pp. 8476-8490
    • Michael, G.J.1    Averill, S.2    Nitkunan, A.3    Rattray, M.4    Bennett, D.L.H.5    Yan, Q.6    Priestly, J.V.7
  • 34
    • 2642683228 scopus 로고    scopus 로고
    • Subcellular localization of epitope-tagged neurotrophins in neuroendocrine cells
    • Moller JC, Kruttgen A, Heymach JV, Ghori N, Shooter EM (1998) Subcellular localization of epitope-tagged neurotrophins in neuroendocrine cells. J Neurosci Res 51:463-472.
    • (1998) J Neurosci Res , vol.51 , pp. 463-472
    • Moller, J.C.1    Kruttgen, A.2    Heymach, J.V.3    Ghori, N.4    Shooter, E.M.5
  • 35
    • 0021024216 scopus 로고
    • Expressing a human proinsulin cDNA in a mouse ACTH-secreting cell. Intracellular storage, proteolytic processing, and secretion on stimulation
    • Moore HP, Walker MD, Lee F, Kelly RB (1983) Expressing a human proinsulin cDNA in a mouse ACTH-secreting cell. Intracellular storage, proteolytic processing, and secretion on stimulation. Cell 35:531-538.
    • (1983) Cell , vol.35 , pp. 531-538
    • Moore, H.P.1    Walker, M.D.2    Lee, F.3    Kelly, R.B.4
  • 39
    • 0028077586 scopus 로고
    • Interactions of ncurotrophin-3 (NT-3), brain-derived neurotrophic factor (BDNF), and the NT-3-BDNF heterodimer with the extracellular domains of the TrkB and TrkC receptors
    • Philo J, Talvenheimo J, Wen J, Rosenfeld R, Welcher A, Arakawa T (1994) Interactions of ncurotrophin-3 (NT-3), brain-derived neurotrophic factor (BDNF), and the NT-3-BDNF heterodimer with the extracellular domains of the TrkB and TrkC receptors. J Biol Chem 269:27840-27846.
    • (1994) J Biol Chem , vol.269 , pp. 27840-27846
    • Philo, J.1    Talvenheimo, J.2    Wen, J.3    Rosenfeld, R.4    Welcher, A.5    Arakawa, T.6
  • 40
    • 0027771130 scopus 로고
    • Heterodimers of the neurotrophic factors: Formation, isolation, and differential stability
    • Radziejewski C, Robinson RC (1993) Heterodimers of the neurotrophic factors: formation, isolation, and differential stability. Biochemistry 32:13350-13356.
    • (1993) Biochemistry , vol.32 , pp. 13350-13356
    • Radziejewski, C.1    Robinson, R.C.2
  • 41
    • 0028913014 scopus 로고
    • Structure of the brain-derived neurotrophic factor/neurotrophin 3 heterodimer
    • Robinson RC, Radziejewski C, Stuart DI, Yvonne Jones E (1995) Structure of the brain-derived neurotrophic factor/neurotrophin 3 heterodimer. Biochemistry 34:4139-4146.
    • (1995) Biochemistry , vol.34 , pp. 4139-4146
    • Robinson, R.C.1    Radziejewski, C.2    Stuart, D.I.3    Yvonne Jones, E.4
  • 42
    • 0030050741 scopus 로고    scopus 로고
    • Cellular processing of the neurotrophin precursors of NT3 and BDNF by the mammalian proprotein convertases
    • Seidah NG, Benjannet S, Pareek S, Chretien M, Murphy RA (1996a) Cellular processing of the neurotrophin precursors of NT3 and BDNF by the mammalian proprotein convertases. FEBS Lett 379:247-250.
    • (1996) FEBS Lett , vol.379 , pp. 247-250
    • Seidah, N.G.1    Benjannet, S.2    Pareek, S.3    Chretien, M.4    Murphy, R.A.5
  • 44
    • 0032524834 scopus 로고    scopus 로고
    • Precursor convertases: An evolutionary ancient, cell-specific, combinatorial mechanism yielding diverse bioactive peptides and proteins
    • Seidah NG, Day R, Marcinkiewicz M, Chretien M (1998) Precursor convertases: an evolutionary ancient, cell-specific, combinatorial mechanism yielding diverse bioactive peptides and proteins. Ann NY Acad Sci 839:9-24.
    • (1998) Ann NY Acad Sci , vol.839 , pp. 9-24
    • Seidah, N.G.1    Day, R.2    Marcinkiewicz, M.3    Chretien, M.4
  • 45
    • 0026787533 scopus 로고
    • Novel roles for neurotrophins are suggested by BDNF and NT-3 mRNA expression in developing neurons
    • Schecterson LC, Bothwell M (1992) Novel roles for neurotrophins are suggested by BDNF and NT-3 mRNA expression in developing neurons. Neuron 9:449-463.
    • (1992) Neuron , vol.9 , pp. 449-463
    • Schecterson, L.C.1    Bothwell, M.2
  • 47
    • 0028800803 scopus 로고
    • The neurotrophins BDNF, NT-3, and NT-4/5 promote survival and morphological and biochemical differentiation of striatal neurons in vitro
    • Ventimiglia R, Mather PE, Jones BE, Lindsay RM (1995) The neurotrophins BDNF, NT-3, and NT-4/5 promote survival and morphological and biochemical differentiation of striatal neurons in vitro. Eur J Neurosci 7:213-222.
    • (1995) Eur J Neurosci , vol.7 , pp. 213-222
    • Ventimiglia, R.1    Mather, P.E.2    Jones, B.E.3    Lindsay, R.M.4
  • 48
    • 0029868289 scopus 로고    scopus 로고
    • Comparative cellular processing of the human immunodeficiency virus (HIV-1) envelope glycoprotein gp160 by the mammalian subtilisin/kexin-like convertases
    • Vollenweider F, Benjannet S, Decroly E, Savaria D, Lazur C, Thomas G, Chretien M, Seidah NG (1996) Comparative cellular processing of the human immunodeficiency virus (HIV-1) envelope glycoprotein gp160 by the mammalian subtilisin/kexin-like convertases. Biochem J 314:521-532.
    • (1996) Biochem J , vol.314 , pp. 521-532
    • Vollenweider, F.1    Benjannet, S.2    Decroly, E.3    Savaria, D.4    Lazur, C.5    Thomas, G.6    Chretien, M.7    Seidah, N.G.8
  • 49
  • 50
    • 0028960688 scopus 로고
    • Engineered serine protease inhibitor prevents furin-catalyzed activation of the fusion glycoprotein and production of infectious measles virus
    • Watanabe M, Hirano A, Stenglein S, Nelson J, Thomas G, Wong TC (1995) Engineered serine protease inhibitor prevents furin-catalyzed activation of the fusion glycoprotein and production of infectious measles virus. J Virol 69:3206-3210.
    • (1995) J Virol , vol.69 , pp. 3206-3210
    • Watanabe, M.1    Hirano, A.2    Stenglein, S.3    Nelson, J.4    Thomas, G.5    Wong, T.C.6
  • 52
    • 0026658003 scopus 로고
    • Processing of mutated proinsulin with tetrabasic cleavage sites to bioactive insulin in the non-endocrine cell line, COS-7
    • Yanagita M, Nakayama K, Takcuchi T (1992) Processing of mutated proinsulin with tetrabasic cleavage sites to bioactive insulin in the non-endocrine cell line, COS-7. FEBS Lett 311:55-59.
    • (1992) FEBS Lett , vol.311 , pp. 55-59
    • Yanagita, M.1    Nakayama, K.2    Takcuchi, T.3
  • 54
    • 0033597852 scopus 로고    scopus 로고
    • Proteolytic processing in the secretory pathway
    • Zhou A, Webb G, Zhu X, Steiner DF (1999) Proteolytic processing in the secretory pathway. J Biol Chem 274:20745-20748.
    • (1999) J Biol Chem , vol.274 , pp. 20745-20748
    • Zhou, A.1    Webb, G.2    Zhu, X.3    Steiner, D.F.4
  • 55
    • 0029884290 scopus 로고    scopus 로고
    • Dimerization of lactase-phlorizin hydrolase occurs in the endoplasmic reticulum, involves the putative membrane spanning domain and is required for an efficient transport of the enzyme to the cell surface
    • Zhu G, Jaskiewicz E, Bassi R, Darling DS, Young Jr WW (1996) Dimerization of lactase-phlorizin hydrolase occurs in the endoplasmic reticulum, involves the putative membrane spanning domain and is required for an efficient transport of the enzyme to the cell surface. Eur J Cell Biol 3:198-208.
    • (1996) Eur J Cell Biol , vol.3 , pp. 198-208
    • Zhu, G.1    Jaskiewicz, E.2    Bassi, R.3    Darling, D.S.4    Young W.W., Jr.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.