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Volumn 17, Issue 12, 1998, Pages 3277-3289

Chromogranin B (secretogranin I), a neuroendocrine-regulated secretory protein, is sorted to exocrine secretory granules in transgenic mice

Author keywords

Exocrine pancreas; Granins; Protein sorting; Secretory granules; Transgenic mice

Indexed keywords

AMYLASE; CHROMOGRANIN B; MATRIX PROTEIN; SECRETORY PROTEIN; ZYMOGEN GRANULE;

EID: 0032526709     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/17.12.3277     Document Type: Article
Times cited : (26)

References (52)
  • 1
    • 0026729952 scopus 로고
    • Protein sorting and secretion granule formation in regulated secretory cells
    • Arvan, P. and Castle, D. (1992) Protein sorting and secretion granule formation in regulated secretory cells. Trends Cell Biol., 2, 327-331.
    • (1992) Trends Cell Biol. , vol.2 , pp. 327-331
    • Arvan, P.1    Castle, D.2
  • 3
    • 0025002294 scopus 로고
    • Co-localization of secretogranins/chromogranins with thyrotropin and luteinizing hormone in secretory granules of cow anterior pituitary
    • Bassetti, M., Huttner, W.B., Zanini, A. and Rosa, P. (1990) Co-localization of secretogranins/chromogranins with thyrotropin and luteinizing hormone in secretory granules of cow anterior pituitary. J. Histochem. Cytochem., 38, 1353-1363.
    • (1990) J. Histochem. Cytochem. , vol.38 , pp. 1353-1363
    • Bassetti, M.1    Huttner, W.B.2    Zanini, A.3    Rosa, P.4
  • 4
    • 0027179911 scopus 로고
    • Selective storage of acetylcholine, but not catecholamines, in neuroendocrine synaptic-like microvesicles of early endosomal origin
    • Bauerfeind, R., Régnier-Vigouroux, A., Flatmark, T. and Huttner, W.B. (1993) Selective storage of acetylcholine, but not catecholamines, in neuroendocrine synaptic-like microvesicles of early endosomal origin. Neuron, 11, 105-121.
    • (1993) Neuron , vol.11 , pp. 105-121
    • Bauerfeind, R.1    Régnier-Vigouroux, A.2    Flatmark, T.3    Huttner, W.B.4
  • 5
    • 0023332890 scopus 로고
    • The primary structure of human secretogranin I (chromogranin B): Comparison with chromogranin a reveals homologous terminal domains and a large intervening variable region
    • Benedum, U.M. et al. (1987) The primary structure of human secretogranin I (chromogranin B): comparison with chromogranin A reveals homologous terminal domains and a large intervening variable region. EMBO J., 6, 1203-1211.
    • (1987) EMBO J. , vol.6 , pp. 1203-1211
    • Benedum, U.M.1
  • 6
    • 0023463127 scopus 로고
    • Constitutive and regulated secretion of proteins
    • Burgess, T.L. and Kelly, R.B. (1987) Constitutive and regulated secretion of proteins. Annu. Rev. Cell Biol., 3, 243-293.
    • (1987) Annu. Rev. Cell Biol. , vol.3 , pp. 243-293
    • Burgess, T.L.1    Kelly, R.B.2
  • 7
    • 0021997190 scopus 로고
    • The exocrine protein trypsinogen is targeted into the secretory granules of an endocrine cell line: Studies by gene transfer
    • Burgess, T.L., Craik, C.S. and Kelly, R.G. (1985) The exocrine protein trypsinogen is targeted into the secretory granules of an endocrine cell line: studies by gene transfer. J. Cell Biol., 101, 639-645.
    • (1985) J. Cell Biol. , vol.101 , pp. 639-645
    • Burgess, T.L.1    Craik, C.S.2    Kelly, R.G.3
  • 8
    • 0026652417 scopus 로고
    • A 13-amino acid N-terminal domain of a basic proline-rich protein is necessary for storage in secretory granules and facilitates exit from the endoplasmic reticulum
    • Castle, A.M., Stahl, L.E. and Castle, J.D. (1992) A 13-amino acid N-terminal domain of a basic proline-rich protein is necessary for storage in secretory granules and facilitates exit from the endoplasmic reticulum. J. Biol. Chem., 267, 13093-13100.
    • (1992) J. Biol. Chem. , vol.267 , pp. 13093-13100
    • Castle, A.M.1    Stahl, L.E.2    Castle, J.D.3
  • 9
    • 0030840688 scopus 로고    scopus 로고
    • Passive sorting in maturing granules of AtT-20 cells: The entry and exit of salivary amylase and proline-rich protein
    • Castle, A.M., Huang, A.Y. and Castle, J.D. (1997) Passive sorting in maturing granules of AtT-20 cells: the entry and exit of salivary amylase and proline-rich protein. J. Cell Biol., 138, 45-54.
    • (1997) J. Cell Biol. , vol.138 , pp. 45-54
    • Castle, A.M.1    Huang, A.Y.2    Castle, J.D.3
  • 10
    • 0027322942 scopus 로고
    • Reduction of the disulfide bond of chromogranin B (secretogranin I) in the trans-Golgi network causes its missorting to the constitutive secretory pathway
    • Chanat, E., Weiß, U., Huttner, W.B. and Tooze, S.A. (1993) Reduction of the disulfide bond of chromogranin B (secretogranin I) in the trans-Golgi network causes its missorting to the constitutive secretory pathway. EMBO J., 12, 2159-2168.
    • (1993) EMBO J. , vol.12 , pp. 2159-2168
    • Chanat, E.1    Weiß, U.2    Huttner, W.B.3    Tooze, S.A.4
  • 11
    • 0028093660 scopus 로고
    • Exocrine granule specific packaging signals are present in the polypeptide moiety of the pancreatic granule membrane protein GP2 and in amylase: Implications for protein targeting to secretory granules
    • Colomer, V. Lal, K., Hoops, T.C. and Rindler, M.J. (1994) Exocrine granule specific packaging signals are present in the polypeptide moiety of the pancreatic granule membrane protein GP2 and in amylase: implications for protein targeting to secretory granules. EMBO J., 13, 3711-3719.
    • (1994) EMBO J. , vol.13 , pp. 3711-3719
    • Colomer, V.1    Lal, K.2    Hoops, T.C.3    Rindler, M.J.4
  • 12
    • 0030043593 scopus 로고    scopus 로고
    • Secretory granule content proteins and the luminal domains of granule membrane proteins aggregate in vitro at mildly acidic pH
    • Colomer, V., Kieska, G.A. and Rindler, M.J. (1996) Secretory granule content proteins and the luminal domains of granule membrane proteins aggregate in vitro at mildly acidic pH. J. Biol. Chem., 271, 48-55.
    • (1996) J. Biol. Chem. , vol.271 , pp. 48-55
    • Colomer, V.1    Kieska, G.A.2    Rindler, M.J.3
  • 16
    • 0030051441 scopus 로고    scopus 로고
    • The AP-1 adaptor complex binds to immature secretory granules from PC12 cells, and is regulated by ADP-ribosylation factor
    • Dittié, A.S., Hajibagheri, N. and Tooze, S.A. (1996) The AP-1 adaptor complex binds to immature secretory granules from PC12 cells, and is regulated by ADP-ribosylation factor. J. Cell Biol., 132, 523-536.
    • (1996) J. Cell Biol. , vol.132 , pp. 523-536
    • Dittié, A.S.1    Hajibagheri, N.2    Tooze, S.A.3
  • 17
    • 0023003030 scopus 로고
    • Chromogranin a in the pancreatic islet: Cellular and subcellular distribution
    • Ehrhart, M., Grube, D., Bader, M.-F., Aunis, D. and Gratzl, M. (1986) Chromogranin A in the pancreatic islet: cellular and subcellular distribution. J. Histochem. Cytochem., 34, 1673-1682.
    • (1986) J. Histochem. Cytochem. , vol.34 , pp. 1673-1682
    • Ehrhart, M.1    Grube, D.2    Bader, M.-F.3    Aunis, D.4    Gratzl, M.5
  • 18
    • 0023821576 scopus 로고
    • Multiple neuropeptides derived from a common precursor are differentially packaged and transported
    • Fisher, J.M., Sossin, W., Newcomb, R. and Scheller, R.H. (1988) Multiple neuropeptides derived from a common precursor are differentially packaged and transported. Cell, 54, 813-822.
    • (1988) Cell , vol.54 , pp. 813-822
    • Fisher, J.M.1    Sossin, W.2    Newcomb, R.3    Scheller, R.H.4
  • 19
    • 0027730475 scopus 로고
    • Regulated secretory proteins in the exocrine pancreas aggregate under conditions that mimic the trans-Golgi network
    • Freedman, S.D. and Scheele, G.A. (1993) Regulated secretory proteins in the exocrine pancreas aggregate under conditions that mimic the trans-Golgi network. Biochem. Biophys. Res. Commun., 197, 992-999.
    • (1993) Biochem. Biophys. Res. Commun. , vol.197 , pp. 992-999
    • Freedman, S.D.1    Scheele, G.A.2
  • 20
    • 0023864209 scopus 로고
    • Carboxypeptidase E
    • Fricker, L.D. (1988) Carboxypeptidase E. Annu. Rev. Physiol., 50, 309-321.
    • (1988) Annu. Rev. Physiol. , vol.50 , pp. 309-321
    • Fricker, L.D.1
  • 21
    • 0025727369 scopus 로고
    • A single gene encodes membrane-bound and free forms of GP-2, the major glycoprotein in pancreatic secretory (zymogen) granule membranes
    • Fukuoka, S.-I., Freedman, S.D. and Scheele, G.A. (1991) A single gene encodes membrane-bound and free forms of GP-2, the major glycoprotein in pancreatic secretory (zymogen) granule membranes. Proc. Natl Acad. Sci. USA, 88, 2898-2902.
    • (1991) Proc. Natl Acad. Sci. USA , vol.88 , pp. 2898-2902
    • Fukuoka, S.-I.1    Freedman, S.D.2    Scheele, G.A.3
  • 22
    • 0021813718 scopus 로고
    • In cow anterior pituitary, growth hormone and prolactin can be packed in separate granules of the same cell
    • Fumagalli, G. and Zanini, A. (1985) In cow anterior pituitary, growth hormone and prolactin can be packed in separate granules of the same cell. J. Cell Biol., 100, 2019-2024.
    • (1985) J. Cell Biol. , vol.100 , pp. 2019-2024
    • Fumagalli, G.1    Zanini, A.2
  • 23
    • 0024344257 scopus 로고
    • The primary structure of human secretogranin II, a widespread tyrosine-sulfated secretory granule protein that exhibits low pH- and calcium-induced aggregation
    • Gerdes, H.-H., Rosa, P., Phillips, E., Baeuerle, P.A., Frank, R., Argos, P. and Huttner, W.B. (1989) The primary structure of human secretogranin II, a widespread tyrosine-sulfated secretory granule protein that exhibits low pH- and calcium-induced aggregation. J. Biol. Chem., 264, 12009-12015.
    • (1989) J. Biol. Chem. , vol.264 , pp. 12009-12015
    • Gerdes, H.-H.1    Rosa, P.2    Phillips, E.3    Baeuerle, P.A.4    Frank, R.5    Argos, P.6    Huttner, W.B.7
  • 26
    • 0028329930 scopus 로고
    • Sorting and processing of secretory proteins
    • Halban, P.A. and Irminger, J.-C. (1994) Sorting and processing of secretory proteins. Biochem. J., 299, 1-18.
    • (1994) Biochem. J. , vol.299 , pp. 1-18
    • Halban, P.A.1    Irminger, J.-C.2
  • 27
    • 0023431906 scopus 로고
    • Sorting of three secretory proteins to distinct secretory granules in acidophilic cells of cow anterior pituitary
    • Hashimoto, S., Fumagalli, G., Zanini, A. and Meldolesi, J. (1987) Sorting of three secretory proteins to distinct secretory granules in acidophilic cells of cow anterior pituitary. J. Cell Biol., 105, 1579-1586.
    • (1987) J. Cell Biol. , vol.105 , pp. 1579-1586
    • Hashimoto, S.1    Fumagalli, G.2    Zanini, A.3    Meldolesi, J.4
  • 28
  • 30
    • 0031026949 scopus 로고    scopus 로고
    • Identification of the secretory vesicle membrane binding region of chromogranin A
    • Kang, Y.K. and Yoo, S.H. (1997) Identification of the secretory vesicle membrane binding region of chromogranin A. FEBS Lett., 404, 87-90.
    • (1997) FEBS Lett. , vol.404 , pp. 87-90
    • Kang, Y.K.1    Yoo, S.H.2
  • 31
    • 0039359126 scopus 로고    scopus 로고
    • Essential role of the disulfide-bonded loop of chromogranin B for sorting to secretory granules is revealed by expression of a deletion mutant in the absence of endogenous granin synthesis
    • Krömer, A., Glombik, M.M., Huttner, W.B. and Gerdes, H.-H. (1998) Essential role of the disulfide-bonded loop of chromogranin B for sorting to secretory granules is revealed by expression of a deletion mutant in the absence of endogenous granin synthesis. J. Cell Biol., 140, 1331-1346.
    • (1998) J. Cell Biol. , vol.140 , pp. 1331-1346
    • Krömer, A.1    Glombik, M.M.2    Huttner, W.B.3    Gerdes, H.-H.4
  • 32
    • 0026695156 scopus 로고
    • Protein targeting via the 'constitutive-like' secretory pathway in isolated pancreatic islets: Passive sorting in the immature granule compartment
    • Kuliawat, R. and Arvan, P. (1992) Protein targeting via the 'constitutive-like' secretory pathway in isolated pancreatic islets: passive sorting in the immature granule compartment. J. Cell Biol., 118, 521-529.
    • (1992) J. Cell Biol. , vol.118 , pp. 521-529
    • Kuliawat, R.1    Arvan, P.2
  • 33
    • 0030943904 scopus 로고    scopus 로고
    • Differential sorting of lysosomal enzymes out of the regulated secretory pathway in pancreatic β-cells
    • Kuliawat, R., Klumpermann, J., Ludwig, T. and Arvan, P. (1997) Differential sorting of lysosomal enzymes out of the regulated secretory pathway in pancreatic β-cells. J. Cell Biol., 137, 595-608.
    • (1997) J. Cell Biol. , vol.137 , pp. 595-608
    • Kuliawat, R.1    Klumpermann, J.2    Ludwig, T.3    Arvan, P.4
  • 34
    • 0027412124 scopus 로고
    • Reconstitution in vitro of the pH-dependent aggregation of pancreatic zymogens en route to the secretory granule: Implication of GP-2
    • Leblond, F.A., Viau, J.L., Lainé, J. and Lebel, D. (1993) Reconstitution in vitro of the pH-dependent aggregation of pancreatic zymogens en route to the secretory granule: implication of GP-2. Biochem. J., 291, 289-296.
    • (1993) Biochem. J. , vol.291 , pp. 289-296
    • Leblond, F.A.1    Viau, J.L.2    Lainé, J.3    Lebel, D.4
  • 35
    • 0023243230 scopus 로고
    • The condensing vacuole of exocrine cells is more acidic than the mature secretory vesicle
    • Orci, L., Ravazzola, M. and Anderson, R.G.W. (1987) The condensing vacuole of exocrine cells is more acidic than the mature secretory vesicle. Nature, 326, 77-79.
    • (1987) Nature , vol.326 , pp. 77-79
    • Orci, L.1    Ravazzola, M.2    Anderson, R.G.W.3
  • 36
    • 0021961473 scopus 로고
    • Specific expression of an elastase-human growth hormone fusion gene in pancreatic acinar cells of transgenic mice
    • Ornitz, D.M., Palmiter, R.D., Hammer, R.E., Brinster, R.L., Swift, G.H. and MacDonald, R.J. (1985) Specific expression of an elastase-human growth hormone fusion gene in pancreatic acinar cells of transgenic mice. Nature, 313, 600-602.
    • (1985) Nature , vol.313 , pp. 600-602
    • Ornitz, D.M.1    Palmiter, R.D.2    Hammer, R.E.3    Brinster, R.L.4    Swift, G.H.5    MacDonald, R.J.6
  • 38
    • 0028672753 scopus 로고
    • The granin protein family: Markers for neuroendocrine cells and tools for the diagnosis of neuroendocrine tumors
    • Rosa, P. and Gerdes, H.-H. (1994) The granin protein family: markers for neuroendocrine cells and tools for the diagnosis of neuroendocrine tumors. J. Endocrinol Invest., 17, 207-225.
    • (1994) J. Endocrinol Invest. , vol.17 , pp. 207-225
    • Rosa, P.1    Gerdes, H.-H.2
  • 39
    • 0022341945 scopus 로고
    • Secretogranins I and II: Two tyrosine-sulfated secretory proteins common to a variety of cells secreting peptides by the regulated pathway
    • Rosa, P. Hille, A., Lee, R.W.H., Zanini, A., De Camilli, P. and Huttner, W.B. (1985) Secretogranins I and II: two tyrosine-sulfated secretory proteins common to a variety of cells secreting peptides by the regulated pathway. J. Cell Biol., 101, 1999-2011.
    • (1985) J. Cell Biol. , vol.101 , pp. 1999-2011
    • Rosa, P.1    Hille, A.2    Lee, R.W.H.3    Zanini, A.4    De Camilli, P.5    Huttner, W.B.6
  • 40
    • 0026566296 scopus 로고
    • Widespread occurrence of chromogranins/secretogranins in the matrix of secretory granules of endocrinologically silent pituitary adenomas
    • Rosa, P., Bassetti, M., Weiss, U. and Huttner, W.B. (1992) Widespread occurrence of chromogranins/secretogranins in the matrix of secretory granules of endocrinologically silent pituitary adenomas. J. Histochem. Cytochem., 40, 523-533.
    • (1992) J. Histochem. Cytochem. , vol.40 , pp. 523-533
    • Rosa, P.1    Bassetti, M.2    Weiss, U.3    Huttner, W.B.4
  • 42
    • 9444259319 scopus 로고    scopus 로고
    • Nonradioactive in situ hybridization for detection of mRNAs encoding for peroxisomal proteins: Heterogeneous hepatic lobular distribution after treatment with a single dose of bezafibrate
    • Schad, A., Fahimi, H.D., Völkl, A. and Baumgart, E. (1996) Nonradioactive in situ hybridization for detection of mRNAs encoding for peroxisomal proteins: heterogeneous hepatic lobular distribution after treatment with a single dose of bezafibrate. J. Histochem. Cytochem., 44, 825-834.
    • (1996) J. Histochem. Cytochem. , vol.44 , pp. 825-834
    • Schad, A.1    Fahimi, H.D.2    Völkl, A.3    Baumgart, E.4
  • 43
    • 0030974124 scopus 로고    scopus 로고
    • fat mice associated with a carboxypeptidase e mutation
    • fat mice associated with a carboxypeptidase E mutation. Proc. Natl Acad. Sci. USA, 94, 5314-5319.
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 5314-5319
    • Shen, F.-S.1    Loh, Y.P.2
  • 45
    • 0025248051 scopus 로고
    • Cell-free protein sorting to the regulated and constitutive secretory pathways
    • Tooze, S.A. and Huttner, W.B. (1990) Cell-free protein sorting to the regulated and constitutive secretory pathways. Cell, 60, 837-847.
    • (1990) Cell , vol.60 , pp. 837-847
    • Tooze, S.A.1    Huttner, W.B.2
  • 46
    • 0027022489 scopus 로고
    • Cell-free formation of immature secretory granules and constitutive secretory vesicles from the trans-Golgi network
    • Tooze, S.A. and Huttner, W.B. (1992) Cell-free formation of immature secretory granules and constitutive secretory vesicles from the trans-Golgi network. Methods Enzymol., 219, 81-93.
    • (1992) Methods Enzymol. , vol.219 , pp. 81-93
    • Tooze, S.A.1    Huttner, W.B.2
  • 47
    • 0024400243 scopus 로고
    • Condensation-sorting events in the rough endoplasmic reticulum of exocrine pancreatic cells
    • Tooze, J., Kern, H.F., Fuller, S.D. and Howell, K.E. (1989) Condensation-sorting events in the rough endoplasmic reticulum of exocrine pancreatic cells. J. Cell Biol., 109, 35-50.
    • (1989) J. Cell Biol. , vol.109 , pp. 35-50
    • Tooze, J.1    Kern, H.F.2    Fuller, S.D.3    Howell, K.E.4
  • 49
    • 0025732765 scopus 로고
    • Acceleration of asynchronous enzyme transport in the rat exocrine pancreas following hormonal stimulation in vivo
    • Vasiloudes, P., Paul, N., Tooze, J. and Kern, H.F. (1991) Acceleration of asynchronous enzyme transport in the rat exocrine pancreas following hormonal stimulation in vivo. Eur. J. Cell Biol., 54, 27-37.
    • (1991) Eur. J. Cell Biol. , vol.54 , pp. 27-37
    • Vasiloudes, P.1    Paul, N.2    Tooze, J.3    Kern, H.F.4
  • 50
    • 0023605612 scopus 로고
    • Protein sorting among two distinct export pathways occurs from the content of maturing exocrine storage granules
    • von Zastrow, M. and Castle, J.D. (1987) Protein sorting among two distinct export pathways occurs from the content of maturing exocrine storage granules. J. Cell Biol., 105, 2675-2684.
    • (1987) J. Cell Biol. , vol.105 , pp. 2675-2684
    • Von Zastrow, M.1    Castle, J.D.2
  • 51
    • 0026680263 scopus 로고
    • The chromogranins A and B: The first 25 years and future perspectives
    • Winkler, H. and Fischer-Colbrie, R. (1992) The chromogranins A and B: the first 25 years and future perspectives. Neuroscience, 49, 497-528.
    • (1992) Neuroscience , vol.49 , pp. 497-528
    • Winkler, H.1    Fischer-Colbrie, R.2
  • 52
    • 0031002651 scopus 로고    scopus 로고
    • Identification of the secretory vesicle membrane binding region of chromogranin B
    • Yoo, S.H. and Kang, Y.K. (1997) Identification of the secretory vesicle membrane binding region of chromogranin B. FEBS Lett., 406, 259-262.
    • (1997) FEBS Lett. , vol.406 , pp. 259-262
    • Yoo, S.H.1    Kang, Y.K.2


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