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Volumn 120, Issue 2, 2000, Pages 211-221

Conversion and storage of somatostatin are established before response to secretagogue stimuli in P19 neurons

Author keywords

Embryonal carcinoma; Neuronal cell line; Neuropeptide conversion; Neuropeptide release; Proprotein convertase; Secretory granule protein

Indexed keywords

FURIN; SOMATOSTATIN;

EID: 0034647096     PISSN: 01653806     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0165-3806(00)00011-0     Document Type: Article
Times cited : (9)

References (64)
  • 1
    • 0027145167 scopus 로고
    • The release of somatostatin-14 from human submucosal ganglia in tissue culture
    • E.A. Accili, C.H.S. McIntosh, A.M.J. Buchan, The release of somatostatin-14 from human submucosal ganglia in tissue culture, Can. J. Physiol. Pharmacol. 71 (1993) 619-624.
    • (1993) Can. J. Physiol. Pharmacol. , vol.71 , pp. 619-624
    • Accili, E.A.1    McIntosh, C.H.S.2    Buchan, A.M.J.3
  • 2
    • 0021112344 scopus 로고
    • Nucleotide and amino acid sequence comparison of preprosomatostatins
    • P. Argos, W.L. Taylor, C.D. Minth, J.E. Dixon, Nucleotide and amino acid sequence comparison of preprosomatostatins, J. Biol. Chem. 258 (1983) 8788-8793.
    • (1983) J. Biol. Chem. , vol.258 , pp. 8788-8793
    • Argos, P.1    Taylor, W.L.2    Minth, C.D.3    Dixon, J.E.4
  • 3
    • 0026012088 scopus 로고
    • Chromogranin A: Posttranslational modifications in secretory granules
    • J.A. Barbosa, B.M. Gill, M.A. Takiyyuddin, D.T. O'Connor, Chromogranin A: posttranslational modifications in secretory granules, Endocrinology 128 (1991) 174-190.
    • (1991) Endocrinology , vol.128 , pp. 174-190
    • Barbosa, J.A.1    Gill, B.M.2    Takiyyuddin, M.A.3    O'Connor, D.T.4
  • 4
    • 0027368472 scopus 로고
    • Comparative biosynthesis, covalent posttranslational modifications and efficiency of pro-segment cleavage of the prohormone convertases PC1 and PC2: Glycosylation, sulphation and identification of the intracellular site of pro-segment cleavage of PC1 and PC2
    • S. Benjannet, N. Rondeau, L. Paquet, A. Boudreault, C. Lazure, M. Chrétien, N.G. Seidah, Comparative biosynthesis, covalent posttranslational modifications and efficiency of pro-segment cleavage of the prohormone convertases PC1 and PC2: glycosylation, sulphation and identification of the intracellular site of pro-segment cleavage of PC1 and PC2, Biochem. J. 294 (1993) 735-743.
    • (1993) Biochem. J. , vol.294 , pp. 735-743
    • Benjannet, S.1    Rondeau, N.2    Paquet, L.3    Boudreault, A.4    Lazure, C.5    Chrétien, M.6    Seidah, N.G.7
  • 6
    • 0023513798 scopus 로고
    • A new prosomatostatin-derived peptide reveals a pattern for prohormone cleavage at monobasic sites
    • R. Benoit, N. Ling, F. Esch, A new prosomatostatin-derived peptide reveals a pattern for prohormone cleavage at monobasic sites, Science 238 (1987) 1126-1129.
    • (1987) Science , vol.238 , pp. 1126-1129
    • Benoit, R.1    Ling, N.2    Esch, F.3
  • 7
    • 0031307787 scopus 로고    scopus 로고
    • Proteolytic profile of recombinant pro-opiomelanocortin in embryonal carcinoma P19 cells: Conversion to β-lipotropin and secretion are inhibited following incubation with canavanine
    • D. Bolduc, N. Cadet, K. Sayasith, J. Paquin, Proteolytic profile of recombinant pro-opiomelanocortin in embryonal carcinoma P19 cells: conversion to β-lipotropin and secretion are inhibited following incubation with canavanine, Biochem. Cell Biol. 75 (1997) 237-2546.
    • (1997) Biochem. Cell Biol. , vol.75 , pp. 237-2546
    • Bolduc, D.1    Cadet, N.2    Sayasith, K.3    Paquin, J.4
  • 8
    • 0028130660 scopus 로고
    • Processing of human prosomatostatin in AtT-20 cells: S-28 and S-14 are generated in different secretory pathways
    • N. Brakch, P. Cohen, G. Boileau, Processing of human prosomatostatin in AtT-20 cells: S-28 and S-14 are generated in different secretory pathways, Biochem. Biophys. Res. Commun. 205 (1994) 221-229.
    • (1994) Biochem. Biophys. Res. Commun. , vol.205 , pp. 221-229
    • Brakch, N.1    Cohen, P.2    Boileau, G.3
  • 9
    • 0028906683 scopus 로고
    • Comparative proteolytic processing of rat prosomatostatin by the convertases PC1, PC2, furin, PACE4 and PC5 in constitutive and regulated secretory pathways
    • N. Brakch, A.S. Galanopoulou, Y.C. Patel, G. Boileau, N.G. Seidah, Comparative proteolytic processing of rat prosomatostatin by the convertases PC1, PC2, furin, PACE4 and PC5 in constitutive and regulated secretory pathways, FEBS Lett. 362 (1995) 143-146.
    • (1995) FEBS Lett. , vol.362 , pp. 143-146
    • Brakch, N.1    Galanopoulou, A.S.2    Patel, Y.C.3    Boileau, G.4    Seidah, N.G.5
  • 10
    • 0025312761 scopus 로고
    • Canine jejunal submucosa cultures: Characterization and release of neural somatostatin
    • A.M.J. Buchan, A.D. Doyle, E. Accili, Canine jejunal submucosa cultures: characterization and release of neural somatostatin, Can. J. Physiol. Pharmacol. 68 (1990) 705-710.
    • (1990) Can. J. Physiol. Pharmacol. , vol.68 , pp. 705-710
    • Buchan, A.M.J.1    Doyle, A.D.2    Accili, E.3
  • 11
  • 12
    • 0026693294 scopus 로고
    • Secretogranin I/chromogranin B is a heparin-binding adhesive protein
    • M. Chen, P. Tempst, B.A. Yankner, Secretogranin I/chromogranin B is a heparin-binding adhesive protein, J. Neurochem. 58 (1992) 1691-1698.
    • (1992) J. Neurochem. , vol.58 , pp. 1691-1698
    • Chen, M.1    Tempst, P.2    Yankner, B.A.3
  • 13
    • 0029868318 scopus 로고    scopus 로고
    • Identification of a functional cAMP response element in the secretogranin II gene
    • G. Cibelli, S. Jungling, S. Schoch, H.H. Gerdes, G. Thiel, Identification of a functional cAMP response element in the secretogranin II gene, Eur. J. Biochem. 236 (1996) 171-179.
    • (1996) Eur. J. Biochem. , vol.236 , pp. 171-179
    • Cibelli, G.1    Jungling, S.2    Schoch, S.3    Gerdes, H.H.4    Thiel, G.5
  • 15
    • 0030029125 scopus 로고    scopus 로고
    • Antigenic regions of human chromogranin A and their topographic relationship with structural/functional domains
    • A. Corti, R. Longhi, A. Gasparri, F.-X. Chen, M. Pelagi, A.G. Siccardi, Antigenic regions of human chromogranin A and their topographic relationship with structural/functional domains, Eur. J. Biochem. 235 (1996) 275-280.
    • (1996) Eur. J. Biochem. , vol.235 , pp. 275-280
    • Corti, A.1    Longhi, R.2    Gasparri, A.3    Chen, F.-X.4    Pelagi, M.5    Siccardi, A.G.6
  • 16
    • 0028916194 scopus 로고
    • Maintained PC1 and PC2 expression in the AtT-20 variant cell line 6T3 lacking regulated secretion and POMC: Restored POMC expression and regulated secretion after cAMP treatment
    • R. Day, S. Benjannet, L. Matsuuchi, R.B. Kelly, M. Marcinkiewicz, M. Chrétien, N.G. Seidah, Maintained PC1 and PC2 expression in the AtT-20 variant cell line 6T3 lacking regulated secretion and POMC: restored POMC expression and regulated secretion after cAMP treatment, DNA Cell Biol. 14 (1995) 175-188.
    • (1995) DNA Cell Biol. , vol.14 , pp. 175-188
    • Day, R.1    Benjannet, S.2    Matsuuchi, L.3    Kelly, R.B.4    Marcinkiewicz, M.5    Chrétien, M.6    Seidah, N.G.7
  • 17
    • 0023001095 scopus 로고
    • Specific release of a novel pituitary polypeptide, 7B2, from rat anterior pituitary cells in vitro by luteinizing hormone-releasing hormone
    • J.Y. Deng, J.S. Chan, N.G. Seidah, M. Chrétien, Specific release of a novel pituitary polypeptide, 7B2, from rat anterior pituitary cells in vitro by luteinizing hormone-releasing hormone, Neuroendocrinology 44 (1986) 373-377.
    • (1986) Neuroendocrinology , vol.44 , pp. 373-377
    • Deng, J.Y.1    Chan, J.S.2    Seidah, N.G.3    Chrétien, M.4
  • 19
    • 0030016321 scopus 로고    scopus 로고
    • Chromogranin A processing and secretion: Specific role of endogenous and exogenous prohormone convertases in the regulated secretory pathway
    • N.L. Eskeland, A. Zhou, T.Q. Dinh, H. Wu, R.J. Parmer, R.E. Mains, D.T. O'Connor, Chromogranin A processing and secretion: specific role of endogenous and exogenous prohormone convertases in the regulated secretory pathway, J. Clin. Invest. 98 (1996) 148-156.
    • (1996) J. Clin. Invest. , vol.98 , pp. 148-156
    • Eskeland, N.L.1    Zhou, A.2    Dinh, T.Q.3    Wu, H.4    Parmer, R.J.5    Mains, R.E.6    O'Connor, D.T.7
  • 21
    • 0029985691 scopus 로고    scopus 로고
    • Synapse formation and establishment of neuronal polarity by P19 embryonic carcinoma cells and embryonic stem cells
    • M.F.A. Finley, N. Kulkarni, J.E. Huettner, Synapse formation and establishment of neuronal polarity by P19 embryonic carcinoma cells and embryonic stem cells, J. Neurosci. 16 (1996) 1056-1065.
    • (1996) J. Neurosci. , vol.16 , pp. 1056-1065
    • Finley, M.F.A.1    Kulkarni, N.2    Huettner, J.E.3
  • 22
    • 0029102824 scopus 로고
    • Heterologous processing of rat prosomatostatin to somatostatin-14 by PC2: Requirement for secretory cell but not the secretion granule
    • A.S. Galanopoulou, N.G. Seidah, Y.C. Patel, Heterologous processing of rat prosomatostatin to somatostatin-14 by PC2: requirement for secretory cell but not the secretion granule, Biochem. J. 311 (1995) 111-118.
    • (1995) Biochem. J. , vol.311 , pp. 111-118
    • Galanopoulou, A.S.1    Seidah, N.G.2    Patel, Y.C.3
  • 23
    • 0030796230 scopus 로고    scopus 로고
    • Chromogranin A fragments modulate cell adhesion. Identification and characterization of a pro-adhesive domain
    • A. Gasparri, A. Sidoli, L.P. Sanchez, R. Longhi, A.G. Siccardi, P.C. Marchisio, A. Corti, Chromogranin A fragments modulate cell adhesion. Identification and characterization of a pro-adhesive domain, J. Biol. Chem. 272 (1997) 20835-20843.
    • (1997) J. Biol. Chem. , vol.272 , pp. 20835-20843
    • Gasparri, A.1    Sidoli, A.2    Sanchez, L.P.3    Longhi, R.4    Siccardi, A.G.5    Marchisio, P.C.6    Corti, A.7
  • 24
    • 0030954743 scopus 로고    scopus 로고
    • Role of glutamate receptor subtypes in the differential release of somatostatin, neuropeptide Y, and substance P in primary serum-free cultures of striatal neurons
    • S. Garside, M.F. Mazurek, Role of glutamate receptor subtypes in the differential release of somatostatin, neuropeptide Y, and substance P in primary serum-free cultures of striatal neurons, Synapse 27 (1997) 161-167.
    • (1997) Synapse , vol.27 , pp. 161-167
    • Garside, S.1    Mazurek, M.F.2
  • 25
    • 0025729117 scopus 로고
    • Chromogranin B: Isolation from pheochromocytoma, N-terminal sequence, tissue distribution and secretory vesicle processing
    • B.M. Gill, J.A. Barbosa, R. Hogue-Angeletti, N. Varki, D.T. O'Connor, Chromogranin B: isolation from pheochromocytoma, N-terminal sequence, tissue distribution and secretory vesicle processing, Regul. Pept. 33 (1991) 223-235.
    • (1991) Regul. Pept. , vol.33 , pp. 223-235
    • Gill, B.M.1    Barbosa, J.A.2    Hogue-Angeletti, R.3    Varki, N.4    O'Connor, D.T.5
  • 26
    • 0030020242 scopus 로고    scopus 로고
    • Differential storage of prolactin, granins (chromogranin B and secretogranin II), and constitutive secretory markers in rat pituitary GH4C1 cells
    • S.-U. Gorr, Differential storage of prolactin, granins (chromogranin B and secretogranin II), and constitutive secretory markers in rat pituitary GH4C1 cells, J. Biol. Chem. 271 (1996) 3575-3580.
    • (1996) J. Biol. Chem. , vol.271 , pp. 3575-3580
    • Gorr, S.-U.1
  • 27
    • 0028968096 scopus 로고
    • Processing of secretogranin II by prohormone convertases: Importance of PC1 in generation of secretoneurin
    • J. Hoflehner, U. Eder, A. Laslop, N.G. Seidah, R. Fischer-Colbrie, H. Winkler, Processing of secretogranin II by prohormone convertases: importance of PC1 in generation of secretoneurin, FEBS Lett. 360 (1995) 294-298.
    • (1995) FEBS Lett. , vol.360 , pp. 294-298
    • Hoflehner, J.1    Eder, U.2    Laslop, A.3    Seidah, N.G.4    Fischer-Colbrie, R.5    Winkler, H.6
  • 29
    • 0030724213 scopus 로고    scopus 로고
    • Convertase PC2 and the neuroendocrine polypeptide 7B2 are co-induced and processed during neuronal differentiation of P19 embryonal carcinoma cells
    • R. Jeannotte, J. Paquin, C. Petit-Turcotte, R. Day, Convertase PC2 and the neuroendocrine polypeptide 7B2 are co-induced and processed during neuronal differentiation of P19 embryonal carcinoma cells, DNA Cell Biol. 16 (1997) 1175-1187.
    • (1997) DNA Cell Biol. , vol.16 , pp. 1175-1187
    • Jeannotte, R.1    Paquin, J.2    Petit-Turcotte, C.3    Day, R.4
  • 30
    • 0027537114 scopus 로고
    • Differentiation of human pituitary adenomas determines the pattern of chromogranin/secretogranin messenger ribonucleic acid expression
    • L. Jin, W.F. Chandler, J.B. Smart, B.G. England, R.V. Lloyd, Differentiation of human pituitary adenomas determines the pattern of chromogranin/secretogranin messenger ribonucleic acid expression, J. Clin. Endocrinol. Metab. 76 (1993) 728-735.
    • (1993) J. Clin. Endocrinol. Metab. , vol.76 , pp. 728-735
    • Jin, L.1    Chandler, W.F.2    Smart, J.B.3    England, B.G.4    Lloyd, R.V.5
  • 31
    • 0027354448 scopus 로고
    • Storage and release of neurotransmitters
    • R.B. Kelly, Storage and release of neurotransmitters, Cell 72 (1993) 43-53.
    • (1993) Cell , vol.72 , pp. 43-53
    • Kelly, R.B.1
  • 32
    • 0029120751 scopus 로고
    • Release of somatostatin-like immunoreactivity from enriched enteric nerve varicosities of rat ileum
    • M. Kurjak, V. Schusdziarra, H.D. Allescher, Release of somatostatin-like immunoreactivity from enriched enteric nerve varicosities of rat ileum, Eur. J. Pharmacol. 281 (1995) 295-301.
    • (1995) Eur. J. Pharmacol. , vol.281 , pp. 295-301
    • Kurjak, M.1    Schusdziarra, V.2    Allescher, H.D.3
  • 33
    • 0027466425 scopus 로고
    • Secretoneurin-A neuropeptide generated in brain, adrenal medulla and other endocrine tissues by proteolytic processing of secretogranin II (chromogranin C)
    • R. Kirchmair, R. Hogue-Angeletti, J. Gutierrez, R. Fischer-Colbrie, H. Winkler, Secretoneurin-A neuropeptide generated in brain, adrenal medulla and other endocrine tissues by proteolytic processing of secretogranin II (chromogranin C), Neuroscience 53 (1993) 359-365.
    • (1993) Neuroscience , vol.53 , pp. 359-365
    • Kirchmair, R.1    Hogue-Angeletti, R.2    Gutierrez, J.3    Fischer-Colbrie, R.4    Winkler, H.5
  • 35
    • 0029671031 scopus 로고    scopus 로고
    • GABAA receptors modulate early spontaneous excitatory activity in differentiating P19 neurons
    • P. Lin, K. Kusano, Q. Zhang, C.C. Felder, P.M. Geiger, L.C. Mahan, GABAA receptors modulate early spontaneous excitatory activity in differentiating P19 neurons, J. Neurochem. 66 (1996) 233-242.
    • (1996) J. Neurochem. , vol.66 , pp. 233-242
    • Lin, P.1    Kusano, K.2    Zhang, Q.3    Felder, C.C.4    Geiger, P.M.5    Mahan, L.C.6
  • 36
    • 0029124983 scopus 로고
    • P19 embryonal carcinoma cells: A source of cultured neurons amenable to genetic manipulation
    • P.A. MacPhersonm, M.W. McBurney, P19 embryonal carcinoma cells: a source of cultured neurons amenable to genetic manipulation, Methods, Companion Methods Enzymol. 7 (1995) 238-252.
    • (1995) Methods, Companion Methods Enzymol. , vol.7 , pp. 238-252
    • MacPhersonm, P.A.1    McBurney, M.W.2
  • 37
    • 0030818219 scopus 로고    scopus 로고
    • P19 cells differentiate into glutamatergic and glutamate-responsive neurons in vitro
    • P.A. MacPherson, S. Jones, P.A. Pawson, K.C. Marshall, M.W. McBurney, P19 cells differentiate into glutamatergic and glutamate-responsive neurons in vitro, Neuroscience 80 (1997) 487-499.
    • (1997) Neuroscience , vol.80 , pp. 487-499
    • MacPherson, P.A.1    Jones, S.2    Pawson, P.A.3    Marshall, K.C.4    McBurney, M.W.5
  • 38
    • 0027475453 scopus 로고
    • Molecular basis of neural-specific gene expression
    • G. Mandel, D. McKinnon, Molecular basis of neural-specific gene expression, Annu. Rev. Neurosci. 16 (1993) 323-345.
    • (1993) Annu. Rev. Neurosci. , vol.16 , pp. 323-345
    • Mandel, G.1    McKinnon, D.2
  • 39
    • 0027482844 scopus 로고
    • Ontogenic development and distribution of mRNAs of chromogranin A and B, secretogranin II, p65 and synaptin/synaptophysin in rat brain
    • M. Mahata, S.K. Mahata, R. Fischer-Colbne, H. Winkler, Ontogenic development and distribution of mRNAs of chromogranin A and B, secretogranin II, p65 and synaptin/synaptophysin in rat brain, Dev. Brain Res. 76 (1993) 43-58.
    • (1993) Dev. Brain Res. , vol.76 , pp. 43-58
    • Mahata, M.1    Mahata, S.K.2    Fischer-Colbne, R.3    Winkler, H.4
  • 40
    • 0029835805 scopus 로고    scopus 로고
    • Immunocytochemical localization of chromogranin A in the normal and stimulated hypothalamoneurohypophysal system of the rat
    • M.E. Majdoubi, M.-H. Metz-Boutigue, P. Garcia-Sablone, D.T. Theodosis, D. Aunis, Immunocytochemical localization of chromogranin A in the normal and stimulated hypothalamoneurohypophysal system of the rat, J. Neurocytol. 25 (1996) 405-416.
    • (1996) J. Neurocytol. , vol.25 , pp. 405-416
    • Majdoubi, M.E.1    Metz-Boutigue, M.-H.2    Garcia-Sablone, P.3    Theodosis, D.T.4    Aunis, D.5
  • 41
    • 0027250171 scopus 로고
    • Accumulation of mRNAs encoding synaptic vesicle-specific proteins precedes neurite extension during early neuronal development
    • G. Marazzi, K.M. Buckley, Accumulation of mRNAs encoding synaptic vesicle-specific proteins precedes neurite extension during early neuronal development, Dev. Dyn. 197 (1993) 115-124.
    • (1993) Dev. Dyn. , vol.197 , pp. 115-124
    • Marazzi, G.1    Buckley, K.M.2
  • 42
    • 0027153542 scopus 로고
    • P19 embryonal carcinoma cells
    • M.W. McBurney, P19 embryonal carcinoma cells, Int. J. Dev. Biol. 37 (1993) 135-140.
    • (1993) Int. J. Dev. Biol. , vol.37 , pp. 135-140
    • McBurney, M.W.1
  • 44
    • 0021172478 scopus 로고
    • Subcellular distribution of somatostatin 14, somatostatin 28 and somatostatin 28 (1-12) in the rat brain and comparison of their respective binding sites in brain and pituitary
    • E. Moyse, R. Benoit, A. Enjalbert, J.P. Gautron, C. Kordon, N. Ling, J. Epelbaum, Subcellular distribution of somatostatin 14, somatostatin 28 and somatostatin 28 (1-12) in the rat brain and comparison of their respective binding sites in brain and pituitary, Regul. Pept. 9 (1984) 129-137.
    • (1984) Regul. Pept. , vol.9 , pp. 129-137
    • Moyse, E.1    Benoit, R.2    Enjalbert, A.3    Gautron, J.P.4    Kordon, C.5    Ling, N.6    Epelbaum, J.7
  • 45
    • 0021361309 scopus 로고
    • Chromogranin A the major catecholamine storage vesicle soluble protein
    • D.T. O'Connor, R. Frigon, Chromogranin A the major catecholamine storage vesicle soluble protein, J. Biol. Chem. 259 (1984) 3237-3247.
    • (1984) J. Biol. Chem. , vol.259 , pp. 3237-3247
    • O'Connor, D.T.1    Frigon, R.2
  • 46
    • 0030816437 scopus 로고    scopus 로고
    • Acceleration of neuronal maturation of P19 cells by increasing culture density
    • D. Parnas, M. Linial, Acceleration of neuronal maturation of P19 cells by increasing culture density, Dev. Brain Res. 101 (1997) 115-124.
    • (1997) Dev. Brain Res. , vol.101 , pp. 115-124
    • Parnas, D.1    Linial, M.2
  • 47
    • 0031110467 scopus 로고    scopus 로고
    • Culture density regulates both the cholinergic phenotype and the expression of the CNTF receptor in P19 neurons
    • D. Parnas, M. Linial, Culture density regulates both the cholinergic phenotype and the expression of the CNTF receptor in P19 neurons, J. Mol. Neurosci. 8 (1997) 115-130.
    • (1997) J. Mol. Neurosci. , vol.8 , pp. 115-130
    • Parnas, D.1    Linial, M.2
  • 48
    • 0010485687 scopus 로고
    • Radioimmunoassay of somatostatin related peptides
    • S.L. Pohl, J. Larner (Eds.), Wiley, New York
    • Y.C. Patel, Radioimmunoassay of somatostatin related peptides, in: S.L. Pohl, J. Larner (Eds.), Methods in Diabetes Research, Wiley, New York, 1984, pp. 307-327.
    • (1984) Methods in Diabetes Research , pp. 307-327
    • Patel, Y.C.1
  • 49
    • 0023835514 scopus 로고
    • Peptides derived from cleavage of prosomatostatin at carboxyl- and amino-terminal segments. Characterization of tissue and secreted forms in the rat
    • Y.C. Patel, W. O'Neil, Peptides derived from cleavage of prosomatostatin at carboxyl- and amino-terminal segments. Characterization of tissue and secreted forms in the rat, J. Biol. Chem. 263 (1988) 745-751.
    • (1988) J. Biol. Chem. , vol.263 , pp. 745-751
    • Patel, Y.C.1    O'Neil, W.2
  • 50
    • 0030666344 scopus 로고    scopus 로고
    • Regulation of neurofilament L, M and H gene expression during retinoic acid-induced neural differentiation of P19 embryonal carcinoma cells
    • G.D. Paterno, L.L. Gillespie, J.-P. Julien, D. Skup, Regulation of neurofilament L, M and H gene expression during retinoic acid-induced neural differentiation of P19 embryonal carcinoma cells, Mol. Brain Res. 49 (1997) 247-254.
    • (1997) Mol. Brain Res. , vol.49 , pp. 247-254
    • Paterno, G.D.1    Gillespie, L.L.2    Julien, J.-P.3    Skup, D.4
  • 51
    • 0029990156 scopus 로고    scopus 로고
    • Development of the sympathoadrenal system in the chick embryo: An immunocytochemical study with antibodies to pan-neuroendocrine markers, catecholamine-synthesizing enzymes, proprotein-processing enzymes, and neuropeptides
    • I. Sánchez-Montesinos, J.A. Mérida-Velasco, J. Espín-Ferra, L. Scopsi, Development of the sympathoadrenal system in the chick embryo: an immunocytochemical study with antibodies to pan-neuroendocrine markers, catecholamine-synthesizing enzymes, proprotein-processing enzymes, and neuropeptides, Anat. Rec. 245 (1996) 94-101.
    • (1996) Anat. Rec. , vol.245 , pp. 94-101
    • Sánchez-Montesinos, I.1    Mérida-Velasco, J.A.2    Espín-Ferra, J.3    Scopsi, L.4
  • 52
    • 0032524834 scopus 로고    scopus 로고
    • Precursor convertases: An evolutionary ancient, cell-specific, combinatorial mechanism yielding diverse bioactive peptides and proteins
    • N.G. Seidah, R. Day, M. Marcinkiewicz, M. Chrétien, Precursor convertases: an evolutionary ancient, cell-specific, combinatorial mechanism yielding diverse bioactive peptides and proteins, Ann. NY Acad. Sci. 839 (1998) 9-24.
    • (1998) Ann. NY Acad. Sci. , vol.839 , pp. 9-24
    • Seidah, N.G.1    Day, R.2    Marcinkiewicz, M.3    Chrétien, M.4
  • 53
    • 0028343895 scopus 로고
    • Neurons derived from P19 embryonal carcinoma cells have varied morphologies and neurotransmitters
    • W.A. Staines, D.J. Morassutti, K.R. Reuhl, A. Ally, M.W. McBurney, Neurons derived from P19 embryonal carcinoma cells have varied morphologies and neurotransmitters, Neuroscience 58 (1994) 735-751.
    • (1994) Neuroscience , vol.58 , pp. 735-751
    • Staines, W.A.1    Morassutti, D.J.2    Reuhl, K.R.3    Ally, A.4    McBurney, M.W.5
  • 54
  • 55
    • 0029956552 scopus 로고    scopus 로고
    • Antibacterial activity of glycosylated and phosphorylated chromogranin A-derived peptide 173-271 from bovine adrenal medullary chromaffin granules
    • J.-M. Strub, Y. Goumon, K. Lugardon, C. Capon, M. Lopez, M. Moniatte, A. Van Dorsselaer, D. Aunis, M.-H. Metz-Boutigue, Antibacterial activity of glycosylated and phosphorylated chromogranin A-derived peptide 173-271 from bovine adrenal medullary chromaffin granules, J. Biol. Chem. 271 (1996) 28533-28540.
    • (1996) J. Biol. Chem. , vol.271 , pp. 28533-28540
    • Strub, J.-M.1    Goumon, Y.2    Lugardon, K.3    Capon, C.4    Lopez, M.5    Moniatte, M.6    Van Dorsselaer, A.7    Aunis, D.8    Metz-Boutigue, M.-H.9
  • 59
    • 0027354037 scopus 로고
    • Structure and function of eukaryotic proprotein processing enzymes of the subtilisin family of serine proteases
    • W.J.M. Van de Ven, A.J.M. Roebroek, Structure and function of eukaryotic proprotein processing enzymes of the subtilisin family of serine proteases, Crit. Rev. Oncol. 4 (1993) 136-151.
    • (1993) Crit. Rev. Oncol. , vol.4 , pp. 136-151
    • Van De Ven, W.J.M.1    Roebroek, A.J.M.2
  • 60
    • 0026680263 scopus 로고
    • The chromogranins A and B: The first 25 years and future perspectives
    • H. Winkler, R. Fischer-Colbrie, The chromogranins A and B: the first 25 years and future perspectives, Neuroscience 49 (1992) 497-528.
    • (1992) Neuroscience , vol.49 , pp. 497-528
    • Winkler, H.1    Fischer-Colbrie, R.2
  • 61
    • 0029166092 scopus 로고
    • Neuronal differentiation of P19 embryonal carcinoma cells in defined media
    • M. Yao, G. Bain, D.I. Gottlieb, Neuronal differentiation of P19 embryonal carcinoma cells in defined media, J. Neurosci. Res. 41 (1995) 792-804.
    • (1995) J. Neurosci. Res. , vol.41 , pp. 792-804
    • Yao, M.1    Bain, G.2    Gottlieb, D.I.3
  • 62
    • 0030060886 scopus 로고    scopus 로고
    • 2+-dependent aggregation property of secretory vesicle matrix proteins and the potential role of chromogranins A and B in secretory vesicle biogenesis
    • 2+-dependent aggregation property of secretory vesicle matrix proteins and the potential role of chromogranins A and B in secretory vesicle biogenesis, J. Biol. Chem. 271 (1996) 1558-1565.
    • (1996) J. Biol. Chem. , vol.271 , pp. 1558-1565
    • Yoo, S.H.1
  • 63
    • 0028124241 scopus 로고
    • The developmental expression in rat of proteases furin, PC1, PC2 and carboxypeptidase E: Implications for early maturation of proteolytic processing capacity
    • M. Zheng, R.D. Sterck, R.E.M. Scott, N.G. Seidah, J.E. Pintar, The developmental expression in rat of proteases furin, PC1, PC2 and carboxypeptidase E: implications for early maturation of proteolytic processing capacity, J. Neurosci. 14 (1994) 4656-4673.
    • (1994) J. Neurosci. , vol.14 , pp. 4656-4673
    • Zheng, M.1    Sterck, R.D.2    Scott, R.E.M.3    Seidah, N.G.4    Pintar, J.E.5
  • 64
    • 0031568334 scopus 로고    scopus 로고
    • The developmental expression in the rat CNS and peripheral-tissues of protease PC5 and PACE-4 messenger-RNAs. Comparison with other proprotein processing enzymes
    • M. Zheng, N.G. Seidah, J.E. Pintar, The developmental expression in the rat CNS and peripheral-tissues of protease PC5 and PACE-4 messenger-RNAs. Comparison with other proprotein processing enzymes, Dev. Biol. 181 (1997) 268-283.
    • (1997) Dev. Biol. , vol.181 , pp. 268-283
    • Zheng, M.1    Seidah, N.G.2    Pintar, J.E.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.