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Volumn 139, Issue 4, 1998, Pages 2137-2145

Depletion of carboxypeptidase E, a regulated secretory pathway sorting receptor, causes misrouting and constitutive secretion of proinsulin and proenkephalin, but not chromogranin A

Author keywords

[No Author keywords available]

Indexed keywords

CARBOXYPEPTIDASE H; CHROMOGRANIN A; COMPLEMENTARY RNA; PROENKEPHALIN; PROINSULIN;

EID: 0031764282     PISSN: 00137227     EISSN: None     Source Type: Journal    
DOI: 10.1210/endo.139.4.5951     Document Type: Article
Times cited : (74)

References (39)
  • 1
    • 0020062469 scopus 로고
    • Two distinct intracellular pathways transport secretory and membrane glycoproteins to the surface of pituitary tumor cells
    • Gumbiner B, Kelly RB 1982 Two distinct intracellular pathways transport secretory and membrane glycoproteins to the surface of pituitary tumor cells. Cell 28:51-59
    • (1982) Cell , vol.28 , pp. 51-59
    • Gumbiner, B.1    Kelly, R.B.2
  • 2
    • 0022402201 scopus 로고
    • Pathways of protein secretion in eukaryotes
    • Kelly RB 1985 Pathways of protein secretion in eukaryotes. Science 230:25-32
    • (1985) Science , vol.230 , pp. 25-32
    • Kelly, R.B.1
  • 3
    • 0026338163 scopus 로고
    • Milieu-induced, selective aggregation of regulated secretory proteins in the trans-Golgi network
    • Chanat E, Huttner WB1991 Milieu-induced, selective aggregation of regulated secretory proteins in the trans-Golgi network. J Cell Biol 115:1505-1519
    • (1991) J Cell Biol , vol.115 , pp. 1505-1519
    • Chanat, E.1    Huttner, W.B.2
  • 4
    • 0030060886 scopus 로고    scopus 로고
    • ++-dependent aggregation property of secretory vesicle matrix proteins and the potential role of chromogranins a and B in secretory vesicles biogenesis
    • ++-dependent aggregation property of secretory vesicle matrix proteins and the potential role of chromogranins A and B in secretory vesicles biogenesis. J Biol Chem 271:1558-1565
    • (1996) J Biol Chem , vol.271 , pp. 1558-1565
    • Yoo, S.H.1
  • 5
    • 0028873682 scopus 로고
    • pH- and Ca(2+)-induced conformational change and aggregation of chromogranin B. Comparison with chromogranin a and implication
    • Yoo SH 1995 pH- and Ca(2+)-induced conformational change and aggregation of chromogranin B. Comparison with chromogranin A and implication. J Biol Chem 270:12578-12583
    • (1995) J Biol Chem , vol.270 , pp. 12578-12583
    • Yoo, S.H.1
  • 6
    • 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 PA, Frank R, Argos P, Huttner WB 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
  • 7
    • 0028912393 scopus 로고
    • Calcium- and pH-dependent aggregation of carboxypeptidase E
    • Song L, Fricker LD 1995 Calcium- and pH-dependent aggregation of carboxypeptidase E. J Biol Chem 270:7963-7967
    • (1995) J Biol Chem , vol.270 , pp. 7963-7967
    • Song, L.1    Fricker, L.D.2
  • 8
    • 0028238359 scopus 로고
    • Calcium- and pH-dependent aggregation and membrane association of the precursor of the prohormone convertase PC2
    • Shennan KI, Taylor NA, Docherty K 1994 Calcium- and pH-dependent aggregation and membrane association of the precursor of the prohormone convertase PC2. J Biol Chem 269:18646-18650
    • (1994) J Biol Chem , vol.269 , pp. 18646-18650
    • Shennan, K.I.1    Taylor, N.A.2    Docherty, K.3
  • 9
    • 0030043593 scopus 로고    scopus 로고
    • Secretory granule content proteins and the lumenal domains of granules membrane proteins aggregate in vitro at mildly acidic pH
    • Colomer V, Kicska GA, Rindler MJ 1996 Secretory granule content proteins and the lumenal domains of granules 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    Kicska, G.A.2    Rindler, M.J.3
  • 10
    • 0028929733 scopus 로고
    • Direct measurement of trans-Golgi pH in living cells and regulation by second messengers
    • Seksek O, Biwersi J, Verkman AS 1995 Direct measurement of trans-Golgi pH in living cells and regulation by second messengers. J Biol Chem 270:4967-4970
    • (1995) J Biol Chem , vol.270 , pp. 4967-4970
    • Seksek, O.1    Biwersi, J.2    Verkman, A.S.3
  • 11
    • 0001307877 scopus 로고    scopus 로고
    • Dynamic measurement of the pH of the Golgi complex in living cells using retrograde transport of the verotoxin receptor
    • Kim JH, Lingwood CA, Williams DB, Furuya W, Manolson MF, Grinstein S 1996 Dynamic measurement of the pH of the Golgi complex in living cells using retrograde transport of the verotoxin receptor. J Cell Biol 134:1387-1399
    • (1996) J Cell Biol , vol.134 , pp. 1387-1399
    • Kim, J.H.1    Lingwood, C.A.2    Williams, D.B.3    Furuya, W.4    Manolson, M.F.5    Grinstein, S.6
  • 12
    • 0026335806 scopus 로고
    • Calcium sequestration in the Golgi apparatus of cultured mammalian cells revealed by laser scanning confocal microscopy and ion microscopy
    • Chandra S, Cable EPW, Morrison GH, Webb WW 1991 Calcium sequestration in the Golgi apparatus of cultured mammalian cells revealed by laser scanning confocal microscopy and ion microscopy. J Cell Sci 10:747-752
    • (1991) J Cell Sci , vol.10 , pp. 747-752
    • Chandra, S.1    Cable, E.P.W.2    Morrison, G.H.3    Webb, W.W.4
  • 13
    • 0027933035 scopus 로고
    • The disulfide bond in chromogranin B, which is essential for its sorting to secretory granules, is not required for its aggregation in the trans Golgi network
    • Chanat E, Weiss U, Huttner W B 1994 The disulfide bond in chromogranin B, which is essential for its sorting to secretory granules, is not required for its aggregation in the trans Golgi network. FEBS Lett 351:225-230
    • (1994) FEBS Lett , vol.351 , pp. 225-230
    • Chanat, E.1    Weiss, U.2    Huttner, W.B.3
  • 14
    • 0027971689 scopus 로고
    • Synthesis and targeting of insulin-like growth factor-I to the hormone storage granules in an endocrine cell line
    • Schmidt WK, Moore H-P 1994 Synthesis and targeting of insulin-like growth factor-I to the hormone storage granules in an endocrine cell line. J Biol Chem 269:27115-27124
    • (1994) J Biol Chem , vol.269 , pp. 27115-27124
    • Schmidt, W.K.1    Moore, H.-P.2
  • 15
    • 0027772562 scopus 로고
    • The amino-terminal sequence of pro-opiomelanocortin directs intracellular targeting to the regulated secretory pathway
    • Tam WHH, Andreasson KA, Loh YP 1993 The amino-terminal sequence of pro-opiomelanocortin directs intracellular targeting to the regulated secretory pathway. Eur J Cell Biol 62:294-306
    • (1993) Eur J Cell Biol , vol.62 , pp. 294-306
    • Tam, W.H.H.1    Andreasson, K.A.2    Loh, Y.P.3
  • 17
    • 0022452276 scopus 로고
    • Re-routing of a secretory protein fusion with human growth hormone sequences
    • Moore H-PH, Kelly RB 1986 Re-routing of a secretory protein fusion with human growth hormone sequences. Nature 321:443-446
    • (1986) Nature , vol.321 , pp. 443-446
    • Moore, H.-P.H.1    Kelly, R.B.2
  • 18
    • 0024597892 scopus 로고
    • The propeptide of preprosomatostatin mediates intracellular transport and secretion of alpha-globin from mammalian cells
    • Stoller TJ, Shields D 1989 The propeptide of preprosomatostatin mediates intracellular transport and secretion of alpha-globin from mammalian cells. J Cell Biol 108:1647-1655
    • (1989) J Cell Biol , vol.108 , pp. 1647-1655
    • Stoller, T.J.1    Shields, D.2
  • 19
    • 0024593402 scopus 로고
    • Aminoterminal sequences of prosomatostatin direct intracellular targeting but not processing specificity
    • Sevarino KA, Stork P, Ventimiglia R, Mandel G, Goodman RH 1989 Aminoterminal sequences of prosomatostatin direct intracellular targeting but not processing specificity. Cell 57:11-19
    • (1989) Cell , vol.57 , pp. 11-19
    • Sevarino, K.A.1    Stork, P.2    Ventimiglia, R.3    Mandel, G.4    Goodman, R.H.5
  • 20
    • 0027328074 scopus 로고
    • Secretory protein traffic. Chromogranin a contains a dominant targeting signal for the regulated pathway
    • Parmer RJ, Xi X-P, Wu H-J, Helman LJ, Petz LN 1993 Secretory protein traffic. Chromogranin A contains a dominant targeting signal for the regulated pathway. J Clin Invest 92:1042-1054
    • (1993) J Clin Invest , vol.92 , pp. 1042-1054
    • Parmer, R.J.1    Xi, X.-P.2    Wu, H.-J.3    Helman, L.J.4    Petz, L.N.5
  • 21
    • 0028958751 scopus 로고
    • Identification of the sorting signal motif within pro-opiomelanocortin for the regulated secretory pathway
    • Cool DR, Fenger M, Snell CR, Loh PY 1995 Identification of the sorting signal motif within pro-opiomelanocortin for the regulated secretory pathway. J Biol Chem 270:8723-8729
    • (1995) J Biol Chem , vol.270 , pp. 8723-8729
    • Cool, D.R.1    Fenger, M.2    Snell, C.R.3    Loh, P.Y.4
  • 22
    • 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 WB, Tooze SA 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
  • 24
    • 0031026949 scopus 로고    scopus 로고
    • Identification of the secretory vesicle membrane binding region of chromogranin A
    • Kang YK, Yoo SH 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
  • 26
    • 0030035227 scopus 로고    scopus 로고
    • Identification of routing determinants in the cytosolic domain of a secretory granule-associated integral membrane protein
    • Milgram SL, Mains RE, Eipper BA1996 Identification of routing determinants in the cytosolic domain of a secretory granule-associated integral membrane protein. J Biol Chem 271:17526-17535
    • (1996) J Biol Chem , vol.271 , pp. 17526-17535
    • Milgram, S.L.1    Mains, R.E.2    Eipper, B.A.3
  • 28
    • 0025327208 scopus 로고
    • Identification of the pH-dependent membrane anchor of carboxypeptidase E(EC 3.4.17.10)
    • Fricker LD, Das B, Angeletti RH 1990 Identification of the pH-dependent membrane anchor of carboxypeptidase E(EC 3.4.17.10). J Biol Chem 265:2476-2482
    • (1990) J Biol Chem , vol.265 , pp. 2476-2482
    • Fricker, L.D.1    Das, B.2    Angeletti, R.H.3
  • 29
    • 0020530809 scopus 로고
    • In vitro biosynthesis and processing of immunologically identified methionin-enkephalin precursor protein
    • Sabol SL, Liang C-M, Dandekar S, Kranzel LS 1983 In vitro biosynthesis and processing of immunologically identified methionin-enkephalin precursor protein. J Biol Chem 258:2697-2704
    • (1983) J Biol Chem , vol.258 , pp. 2697-2704
    • Sabol, S.L.1    Liang, C.-M.2    Dandekar, S.3    Kranzel, L.S.4
  • 30
    • 0028980174 scopus 로고
    • The Neuro-2a neuroblastoma cell line expresses [Met]-enkephalin and vasopressin mRNA and peptide
    • Bamberger A-M, Pu L-P, Cool DR, Loh YP 1995 The Neuro-2a neuroblastoma cell line expresses [Met]-enkephalin and vasopressin mRNA and peptide. Mol Cell Endocrinol 113:155-163
    • (1995) Mol Cell Endocrinol , vol.113 , pp. 155-163
    • Bamberger, A.-M.1    Pu, L.-P.2    Cool, D.R.3    Loh, Y.P.4
  • 34
    • 0027965348 scopus 로고
    • The family of subtilisin/kexin like pro-protein and prohormone convertases: Divergent or shared functions
    • Seidah NG, Chretien M, Day R 1994 The family of subtilisin/kexin like pro-protein and prohormone convertases: divergent or shared functions. Biochimie 76:197-209
    • (1994) Biochimie , vol.76 , pp. 197-209
    • Seidah, N.G.1    Chretien, M.2    Day, R.3
  • 35
    • 0029787008 scopus 로고    scopus 로고
    • A protease processing site is essential for protein sorting to the regulated pathway
    • Brechler V, Chu WN, BaxterJD, Thibault G, Reudelhuber TL 1996 A protease processing site is essential for protein sorting to the regulated 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    Reudelhuber, T.L.5
  • 36
    • 0027465514 scopus 로고
    • Expression of mutant ELH prohormones in AtT-20 cells: The relationship between prohormone processing and sorting
    • Jung LJ, KreinerT, Scheller RH 1993 Expression of mutant ELH prohormones in AtT-20 cells: the relationship between prohormone processing and sorting. J Cell Biol 121:11-21
    • (1993) J Cell Biol , vol.121 , pp. 11-21
    • Jung, L.J.1    Kreiner, T.2    Scheller, R.H.3
  • 38
    • 0021024216 scopus 로고
    • Expressing a human proinsulin cDNa in a mouse ACTH-secreting cell. Intracellular storage, proteolytic processing, and secretion on stimulation
    • Moore H-PH, Walker ML, 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.H.1    Walker, M.L.2    Lee, F.3    Kelly, R.B.4
  • 39
    • 0030974124 scopus 로고    scopus 로고
    • fat mouse associated with carboxypeptidase e mutation
    • fat mouse associated with 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.