메뉴 건너뛰기




Volumn 145, Issue 8, 2004, Pages 3840-3849

Aggregation and lack of secretion of most newly synthesized proinsulin in non-β-cell lines

Author keywords

[No Author keywords available]

Indexed keywords

BAFILOMYCIN; CALRETICULIN; CHAPERONE; CHLOROQUINE; LUBROL; PROINSULIN; PROLACTIN;

EID: 3843093823     PISSN: 00137227     EISSN: None     Source Type: Journal    
DOI: 10.1210/en.2003-1512     Document Type: Article
Times cited : (15)

References (72)
  • 1
    • 0032054714 scopus 로고    scopus 로고
    • The role of assembly in insulin's biosynthesis
    • Dodson G, Steiner D 1998 The role of assembly in insulin's biosynthesis. Curr Opin Struct Biol 8:189-194
    • (1998) Curr Opin Struct Biol , vol.8 , pp. 189-194
    • Dodson, G.1    Steiner, D.2
  • 2
    • 0028927425 scopus 로고
    • In vivo iodination of a misfolded proinsulin reveals colocalized signals for Bip binding and for degradation in the ER
    • Schmitz A, Maintz M, Kehle T, Herzog V 1995 In vivo iodination of a misfolded proinsulin reveals colocalized signals for Bip binding and for degradation in the ER. EMBO J 14:1091-1098
    • (1995) EMBO J , vol.14 , pp. 1091-1098
    • Schmitz, A.1    Maintz, M.2    Kehle, T.3    Herzog, V.4
  • 3
    • 0029133141 scopus 로고
    • Intracellular transport of proinsulin in pancreatic beta-cells. Structural maturation probed by disulfide accessibility
    • Huang XF, Arvan P 1995 Intracellular transport of proinsulin in pancreatic beta-cells. Structural maturation probed by disulfide accessibility. J Biol Chem 270:20417-20423
    • (1995) J Biol Chem , vol.270 , pp. 20417-20423
    • Huang, X.F.1    Arvan, P.2
  • 4
    • 0017808254 scopus 로고
    • Role of zinc and calcium in the formation and storage of insulin in the pancreatic β-cell
    • Howell SL, Tyhurst M, Duvefelt H, Andersson A, Hellerstrom C 1978 Role of zinc and calcium in the formation and storage of insulin in the pancreatic β-cell. Cell Tissue Res 188:107-118
    • (1978) Cell Tissue Res , vol.188 , pp. 107-118
    • Howell, S.L.1    Tyhurst, M.2    Duvefelt, H.3    Andersson, A.4    Hellerstrom, C.5
  • 5
    • 0022979193 scopus 로고
    • Conversion of proinsulin to insulin occurs coordinately with acidification of maturing secretory vesicles
    • Orci I, Ravazzola M, Amherdt M, Madsen O, Perrelet A, Vassalli JD, Anderson RG 1986 Conversion of proinsulin to insulin occurs coordinately with acidification of maturing secretory vesicles. J Cell Biol 103:2273-2281
    • (1986) J Cell Biol , vol.103 , pp. 2273-2281
    • Orci, I.1    Ravazzola, M.2    Amherdt, M.3    Madsen, O.4    Perrelet, A.5    Vassalli, J.D.6    Anderson, R.G.7
  • 6
    • 0023645960 scopus 로고
    • Studies on the molecular organization of rat insulin secretory granules
    • Michael J, Carroll R, Swift HH, Steiner DF 1987 Studies on the molecular organization of rat insulin secretory granules. J Biol Chem 262:16531-16535
    • (1987) J Biol Chem , vol.262 , pp. 16531-16535
    • Michael, J.1    Carroll, R.2    Swift, H.H.3    Steiner, D.F.4
  • 7
    • 0031171411 scopus 로고    scopus 로고
    • Constant delivery of proinsulin by encapsulation of transfected cells
    • Taniguchi H, Fukao K, Nakauchi H 1997 Constant delivery of proinsulin by encapsulation of transfected cells. J Surg Res 70:41-45
    • (1997) J Surg Res , vol.70 , pp. 41-45
    • Taniguchi, H.1    Fukao, K.2    Nakauchi, H.3
  • 8
    • 0030946203 scopus 로고    scopus 로고
    • Hepatic insulin gene expression as treatment for type 1 diabetes mellitus in rats
    • Muzzin P, Eisensmith RC, Copeland KC, Woo SL 1997 Hepatic insulin gene expression as treatment for type 1 diabetes mellitus in rats. Mol Endocrinol 11:833-837
    • (1997) Mol Endocrinol , vol.11 , pp. 833-837
    • Muzzin, P.1    Eisensmith, R.C.2    Copeland, K.C.3    Woo, S.L.4
  • 9
    • 0027963253 scopus 로고
    • Insulin-releasing pituitary cells as a model for somatic cell gene therapy in diabetes mellitus
    • Stewart C, Taylor NA, Green IC, Docherty K, Bailey CJ 1994 Insulin-releasing pituitary cells as a model for somatic cell gene therapy in diabetes mellitus. J Endocrinol 142:339-343
    • (1994) J Endocrinol , vol.142 , pp. 339-343
    • Stewart, C.1    Taylor, N.A.2    Green, I.C.3    Docherty, K.4    Bailey, C.J.5
  • 10
    • 0032973065 scopus 로고    scopus 로고
    • Engineering cultured insulin-secreting pancreatic B-cell lines
    • McClenaghan NH, Flatt PR 1999 Engineering cultured insulin-secreting pancreatic B-cell lines. J Mol Med 77:235-243
    • (1999) J Mol Med , vol.77 , pp. 235-243
    • McClenaghan, N.H.1    Flatt, P.R.2
  • 11
    • 0033584967 scopus 로고    scopus 로고
    • Differentiation-induced insulin secretion from nonendocrine cells with engineered human proinsulin cDNA
    • Yamasaki K, Sasaki T, Nemoto M, Eto Y, Tajima N 1999 Differentiation- induced insulin secretion from nonendocrine cells with engineered human proinsulin cDNA. Biochem Biophys Res Commun 265:361-365
    • (1999) Biochem Biophys Res Commun , vol.265 , pp. 361-365
    • Yamasaki, K.1    Sasaki, T.2    Nemoto, M.3    Eto, Y.4    Tajima, N.5
  • 14
    • 0035043950 scopus 로고    scopus 로고
    • Regulated secretion of proinsulin/insulin from human hepatoma cells transduced by recombinant adeno-associated virus
    • Yang YW, Hsieh YC 2001 Regulated secretion of proinsulin/insulin from human hepatoma cells transduced by recombinant adeno-associated virus. Biotechnol Appl Biochem 33:133-140
    • (2001) Biotechnol Appl Biochem , vol.33 , pp. 133-140
    • Yang, Y.W.1    Hsieh, Y.C.2
  • 15
    • 0033536557 scopus 로고    scopus 로고
    • Stable transfection of rat preproinsulin II gene into rat hematopoietic stem cells via recombinant adeno-associated virus
    • Shah R, Jindal RM 1999 Stable transfection of rat preproinsulin II gene into rat hematopoietic stem cells via recombinant adeno-associated virus. Life Sci 65:2041-2047
    • (1999) Life Sci , vol.65 , pp. 2041-2047
    • Shah, R.1    Jindal, R.M.2
  • 16
    • 0031730473 scopus 로고    scopus 로고
    • Adenovirus-mediated transfer of a modified human proinsulin gene reverses hyperglycemia in diabetic mice
    • Short DK, Okada S, Yamauchi K, Pessin JE 1998 Adenovirus-mediated transfer of a modified human proinsulin gene reverses hyperglycemia in diabetic mice. Am J Physiol 275:E748-E756
    • (1998) Am J Physiol , vol.275
    • Short, D.K.1    Okada, S.2    Yamauchi, K.3    Pessin, J.E.4
  • 17
    • 0028963345 scopus 로고
    • Gene therapy for diabetes mellitus in rats by hepatic expression of insulin
    • Kolodka TM, Finegold M, Moss L, Woo SL 1995 Gene therapy for diabetes mellitus in rats by hepatic expression of insulin. Proc Natl Acad Sci USA 92:3293-3297
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 3293-3297
    • Kolodka, T.M.1    Finegold, M.2    Moss, L.3    Woo, S.L.4
  • 20
    • 0033847742 scopus 로고    scopus 로고
    • Processing and release of human proinsulin-cleavage products into culture media by different engineered non-endocrine cells: A specific assessment by capillary electrophoresis
    • Arcelloni C, Falqui L, Martinenghi S, Stabilini A, Pontiroli AE, Paroni R 2000 Processing and release of human proinsulin-cleavage products into culture media by different engineered non-endocrine cells: a specific assessment by capillary electrophoresis. J Endocrinol 166:437-445
    • (2000) J Endocrinol , vol.166 , pp. 437-445
    • Arcelloni, C.1    Falqui, L.2    Martinenghi, S.3    Stabilini, A.4    Pontiroli, A.E.5    Paroni, R.6
  • 21
    • 0033504139 scopus 로고    scopus 로고
    • Human proinsulin gene-transfected Chinese hamster ovary cells secrete immunoreactive insulin
    • Sato Y, Nio Y, Omori H, Inoue Y, Hirahara N, Sasaki S, Tamura K 1999 Human proinsulin gene-transfected Chinese hamster ovary cells secrete immunoreactive insulin. In Vivo 13:535-540
    • (1999) In Vivo , vol.13 , pp. 535-540
    • Sato, Y.1    Nio, Y.2    Omori, H.3    Inoue, Y.4    Hirahara, N.5    Sasaki, S.6    Tamura, K.7
  • 22
    • 0029922307 scopus 로고    scopus 로고
    • Synthesis and processing of genetically modified human proinsulin by rat myoblast primary cultures
    • Simonson GD, Groskreutz DJ, Gorman CM, MacDonald MJ 1996 Synthesis and processing of genetically modified human proinsulin by rat myoblast primary cultures. Hum Gene Ther 7:71-78
    • (1996) Hum Gene Ther , vol.7 , pp. 71-78
    • Simonson, G.D.1    Groskreutz, D.J.2    Gorman, C.M.3    MacDonald, M.J.4
  • 24
    • 0035491791 scopus 로고    scopus 로고
    • Gene and cell-replacement therapy in the treatment of type 1 diabetes: How nigh must the standards be set?
    • Halban PA, Kahn SE, Lernmark A, Rhodes CJ 2001 Gene and cell-replacement therapy in the treatment of type 1 diabetes: how nigh must the standards be set? Diabetes 50:2181-2191
    • (2001) Diabetes , vol.50 , pp. 2181-2191
    • Halban, P.A.1    Kahn, S.E.2    Lernmark, A.3    Rhodes, C.J.4
  • 25
    • 0036633140 scopus 로고    scopus 로고
    • Human liver-derived cells stably modified for regulated proinsulin secretion function as bioimplants in vivo
    • Chen X, Patil JG, Lok SH, Kon OL 2002 Human liver-derived cells stably modified for regulated proinsulin secretion function as bioimplants in vivo. J Gene Med 4:447-458
    • (2002) J Gene Med , vol.4 , pp. 447-458
    • Chen, X.1    Patil, J.G.2    Lok, S.H.3    Kon, O.L.4
  • 27
    • 0023084134 scopus 로고
    • Use of eukaryotic expression technology in the functional analysis of cloned genes
    • Cullen BR 1987 Use of eukaryotic expression technology in the functional analysis of cloned genes. Methods Enzymol 152:684-704
    • (1987) Methods Enzymol , vol.152 , pp. 684-704
    • Cullen, B.R.1
  • 28
    • 0024520745 scopus 로고
    • Site-directed mutagenesis by overlap extension using the polymerase chain reaction
    • Ho SN, Hunt HD, Horton RM, Pullen JK, Pease LR 1989 Site-directed mutagenesis by overlap extension using the polymerase chain reaction. Gene 77:51-59
    • (1989) Gene , vol.77 , pp. 51-59
    • Ho, S.N.1    Hunt, H.D.2    Horton, R.M.3    Pullen, J.K.4    Pease, L.R.5
  • 29
    • 0035808327 scopus 로고    scopus 로고
    • Acquisition of Lubrol insolubility, a common step for growth hormone and prolactin in the secretory pathway of neuroendocrine cells
    • Lee MS, Zhu YL, Chang JE, Dannies PS 2001 Acquisition of Lubrol insolubility, a common step for growth hormone and prolactin in the secretory pathway of neuroendocrine cells. J Biol Chem 276:715-721
    • (2001) J Biol Chem , vol.276 , pp. 715-721
    • Lee, M.S.1    Zhu, Y.L.2    Chang, J.E.3    Dannies, P.S.4
  • 31
    • 0033540037 scopus 로고    scopus 로고
    • Mitochondrial glutamate acts as a messenger in glucose-induced insulin exocytosis
    • Maechler P, Wollheim CB 1999 Mitochondrial glutamate acts as a messenger in glucose-induced insulin exocytosis. Nature 402:685-689
    • (1999) Nature , vol.402 , pp. 685-689
    • Maechler, P.1    Wollheim, C.B.2
  • 32
    • 0025010510 scopus 로고
    • Prolactin and insulin are targeted to the regulated pathway in GH4C1 cells, but their storage is differentially regulated
    • Reaves BJ, Van Itallie CM, Moore HH, Dannies PS 1990 Prolactin and insulin are targeted to the regulated pathway in GH4C1 cells, but their storage is differentially regulated. Mol Endocrinol 4:1017-1026
    • (1990) Mol Endocrinol , vol.4 , pp. 1017-1026
    • Reaves, B.J.1    Van Itallie, C.M.2    Moore, H.H.3    Dannies, P.S.4
  • 33
    • 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, 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
  • 34
    • 0022969534 scopus 로고
    • Hormonal induction of secretory granules in a pituitary tumor cell line
    • Scammell JG, Burrage TG, Dannies PS 1986 Hormonal induction of secretory granules in a pituitary tumor cell line. Endocrinology 119:1543-1548
    • (1986) Endocrinology , vol.119 , pp. 1543-1548
    • Scammell, J.G.1    Burrage, T.G.2    Dannies, P.S.3
  • 35
    • 0022404854 scopus 로고
    • Comparison of patterns of prolactin release in GH4C1 cells and primary pituitary cultures
    • Delbeke D, Kojima I, Dannies PS 1985 Comparison of patterns of prolactin release in GH4C1 cells and primary pituitary cultures. Mol Cell Endocrinol 43:15-22
    • (1985) Mol Cell Endocrinol , vol.43 , pp. 15-22
    • Delbeke, D.1    Kojima, I.2    Dannies, P.S.3
  • 36
    • 0027965348 scopus 로고
    • The family of subtilisin/kexin like pro-protein and pro-hormone convertases: Divergent or shared functions
    • Paris
    • Seidah NG, Chretien M, Day R 1994 The family of subtilisin/kexin like pro-protein and pro-hormone convertases: divergent or shared functions. Biochimie (Paris) 76:197-209
    • (1994) Biochimie , vol.76 , pp. 197-209
    • Seidah, N.G.1    Chretien, M.2    Day, R.3
  • 37
    • 0034088234 scopus 로고    scopus 로고
    • Proinsulin endoproteolysis confers enhanced targeting of processed insulin to the regulated secretory pathway
    • Kuliawat R, Prabakaran D, Arvan P 2000 Proinsulin endoproteolysis confers enhanced targeting of processed insulin to the regulated secretory pathway. Mol Biol Cell 11:1959-1972
    • (2000) Mol Biol Cell , vol.11 , pp. 1959-1972
    • Kuliawat, R.1    Prabakaran, D.2    Arvan, P.3
  • 38
    • 0020568549 scopus 로고
    • A subclass of proteins and sulfated macromolecules secreted by AtT-20 (mouse pituitary tumor) cells is sorted with adrenocorticotropin into dense secretory granules
    • Moore HP, Gumbiner B, Kelly RB 1983 A subclass of proteins and sulfated macromolecules secreted by AtT-20 (mouse pituitary tumor) cells is sorted with adrenocorticotropin into dense secretory granules. J Cell Biol 97:810-817
    • (1983) J Cell Biol , vol.97 , pp. 810-817
    • Moore, H.P.1    Gumbiner, B.2    Kelly, R.B.3
  • 39
    • 0021359618 scopus 로고
    • Peptide α-amidation activity in mouse anterior pituitary AtT-20 cell granules: Properties and secretion
    • Mains RE, Glembotski CC, Eipper BA 1984 Peptide α-amidation activity in mouse anterior pituitary AtT-20 cell granules: properties and secretion. Endocrinology 114:1522-1530
    • (1984) Endocrinology , vol.114 , pp. 1522-1530
    • Mains, R.E.1    Glembotski, C.C.2    Eipper, B.A.3
  • 40
    • 0014892983 scopus 로고
    • Control of enzyme levels in animal tissues
    • Schimke RT, Doyle D 1970 Control of enzyme levels in animal tissues. Annu Rev Biochem 39:929-976
    • (1970) Annu Rev Biochem , vol.39 , pp. 929-976
    • Schimke, R.T.1    Doyle, D.2
  • 41
    • 0015500963 scopus 로고
    • Compartmentation of free valine and its relation to protein turnover in perfused rat liver
    • Mortimore GE, Woodside KH, Henry JE 1972 Compartmentation of free valine and its relation to protein turnover in perfused rat liver. J Biol Chem 247:2776-2784
    • (1972) J Biol Chem , vol.247 , pp. 2776-2784
    • Mortimore, G.E.1    Woodside, K.H.2    Henry, J.E.3
  • 42
    • 0015240153 scopus 로고
    • Reutilization of amino acids in protein synthesis in HeLa cells
    • Righetti P, Little EP, Wolf G 1971 Reutilization of amino acids in protein synthesis in HeLa cells. J Biol Chem 246:5724-5732
    • (1971) J Biol Chem , vol.246 , pp. 5724-5732
    • Righetti, P.1    Little, E.P.2    Wolf, G.3
  • 45
    • 0000689386 scopus 로고
    • Familial syndrome of hyperproinsulinemia and hyperinsulinemia with mild diabetes
    • Scriver CR, Beaudet AL, Sly WS, Valle D, eds. New York: McGraw-Hill, Inc.
    • Steiner DF, Tager HS, Nanjo K, Chan SJ, Rubenstein AH 1995 Familial syndrome of hyperproinsulinemia and hyperinsulinemia with mild diabetes. In: Scriver CR, Beaudet AL, Sly WS, Valle D, eds. The metabolic and molecular bases of inherited disease. Vol 1. New York: McGraw-Hill, Inc.; 897-904
    • (1995) The Metabolic and Molecular Bases of Inherited Disease , vol.1 , pp. 897-904
    • Steiner, D.F.1    Tager, H.S.2    Nanjo, K.3    Chan, S.J.4    Rubenstein, A.H.5
  • 46
  • 47
    • 0036828020 scopus 로고    scopus 로고
    • Prolonged retention after aggregation into secretory granules of R183H-growth hormone, a mutant that causes autosomal growth hormone deficiency type II
    • Zhu YL, Conway-Campbell BL, Waters MJ, Dannies PS 2002 Prolonged retention after aggregation into secretory granules of R183H-growth hormone, a mutant that causes autosomal growth hormone deficiency type II. Endocrinology 1443:4243-4248
    • (2002) Endocrinology , vol.1443 , pp. 4243-4248
    • Zhu, Y.L.1    Conway-Campbell, B.L.2    Waters, M.J.3    Dannies, P.S.4
  • 48
    • 0034671727 scopus 로고    scopus 로고
    • Subunit structure of a mammalian ER/Golgi SNARE complex
    • Xu D, Joglekar AP, Williams AL, Hay JC 2000 Subunit structure of a mammalian ER/Golgi SNARE complex. J Biol Chem 275:39631-39639
    • (2000) J Biol Chem , vol.275 , pp. 39631-39639
    • Xu, D.1    Joglekar, A.P.2    Williams, A.L.3    Hay, J.C.4
  • 49
    • 0031773999 scopus 로고    scopus 로고
    • TGN38 cycles via the basolateral membrane of polarized Caco-2 cells
    • Reaves BJ, Roquemore EP, Luzio JP, Banting G 1998 TGN38 cycles via the basolateral membrane of polarized Caco-2 cells. Mol Membr Biol 15:133-139
    • (1998) Mol Membr Biol , vol.15 , pp. 133-139
    • Reaves, B.J.1    Roquemore, E.P.2    Luzio, J.P.3    Banting, G.4
  • 50
    • 0031670728 scopus 로고    scopus 로고
    • Lumenal and transmembrane domains play a role in sorting type I membrane proteins on endocytic pathways
    • Reaves BJ, Banting G, Luzio JP 1998 Lumenal and transmembrane domains play a role in sorting type I membrane proteins on endocytic pathways. Mol Biol Cell 9:1107-1122
    • (1998) Mol Biol Cell , vol.9 , pp. 1107-1122
    • Reaves, B.J.1    Banting, G.2    Luzio, J.P.3
  • 52
    • 0024278677 scopus 로고
    • The role of a low pH intracellular compartment in the processing, storage, and secretion of ACTH and endorphin
    • Mains RE, May V 1988 The role of a low pH intracellular compartment in the processing, storage, and secretion of ACTH and endorphin. J Biol Chem 263:7887-7894
    • (1988) J Biol Chem , vol.263 , pp. 7887-7894
    • Mains, R.E.1    May, V.2
  • 53
    • 0038351954 scopus 로고    scopus 로고
    • Role of the connecting peptide in insulin biosynthesis
    • Liu M, Ramos-Castaneda J, Arvan P 2003 Role of the connecting peptide in insulin biosynthesis. J Biol Chem 278:14798-14805
    • (2003) J Biol Chem , vol.278 , pp. 14798-14805
    • Liu, M.1    Ramos-Castaneda, J.2    Arvan, P.3
  • 54
    • 0030917424 scopus 로고    scopus 로고
    • Proinsulin conversion in GH3 cells after coexpression of human proinsulin with the endoproteases PC2 and/or PC3
    • Kaufmann JE, Irminger JC, Mungall J, Halban PA 1997 Proinsulin conversion in GH3 cells after coexpression of human proinsulin with the endoproteases PC2 and/or PC3. Diabetes 46:978-982
    • (1997) Diabetes , vol.46 , pp. 978-982
    • Kaufmann, J.E.1    Irminger, J.C.2    Mungall, J.3    Halban, P.A.4
  • 55
    • 0029088733 scopus 로고
    • Sequence requirements for proinsulin processing at the B-chain/C-peptide junction
    • Kaufmann JE, Irminger JC, Halban PA 1995 Sequence requirements for proinsulin processing at the B-chain/C-peptide junction. Biochem J 310:869-874
    • (1995) Biochem J , vol.310 , pp. 869-874
    • Kaufmann, J.E.1    Irminger, J.C.2    Halban, P.A.3
  • 56
    • 0025786795 scopus 로고
    • Intracellular transport and sorting of mutant human proinsulins that fail to form hexamers
    • Quinn D, Orci L, Ravazzola M, Moore HP 1991 Intracellular transport and sorting of mutant human proinsulins that fail to form hexamers. J Cell Biol 113:987-996
    • (1991) J Cell Biol , vol.113 , pp. 987-996
    • Quinn, D.1    Orci, L.2    Ravazzola, M.3    Moore, H.P.4
  • 57
    • 0024346927 scopus 로고
    • A major C-peptide deletion prevents secretion of a mutant human proinsulin from transfected monkey kidney cells
    • Shakur Y, Shennan KI, Taylor NA, Docherty K 1989 A major C-peptide deletion prevents secretion of a mutant human proinsulin from transfected monkey kidney cells. J Mol Endocrinol 3:155-162
    • (1989) J Mol Endocrinol , vol.3 , pp. 155-162
    • Shakur, Y.1    Shennan, K.I.2    Taylor, N.A.3    Docherty, K.4
  • 58
    • 0027957282 scopus 로고
    • Human proinsulin conversion in the regulated and the constitutive pathways of transfected AtT20 cells
    • Irminger JC, Vollenweider FM, Neerman-Arbez M, Halban PA 1994 Human proinsulin conversion in the regulated and the constitutive pathways of transfected AtT20 cells. J Biol Chem 269:1756-1762
    • (1994) J Biol Chem , vol.269 , pp. 1756-1762
    • Irminger, J.C.1    Vollenweider, F.M.2    Neerman-Arbez, M.3    Halban, P.A.4
  • 60
    • 0024368808 scopus 로고
    • Partial diversion of a mutant proinsulin (B10 aspartic acid) from the regulated to the constitutive secretory pathway in transfected AtT-20 cells
    • Gross DJ, Halban PA, Kahn CR, Weir GC, Villa-Komaroff L 1989 Partial diversion of a mutant proinsulin (B10 aspartic acid) from the regulated to the constitutive secretory pathway in transfected AtT-20 cells. Proc Natl Acad Sci USA 86:4107-4111
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 4107-4111
    • Gross, D.J.1    Halban, P.A.2    Kahn, C.R.3    Weir, G.C.4    Villa-Komaroff, L.5
  • 61
    • 0035808328 scopus 로고    scopus 로고
    • Identification of a membrane-associated cysteine protease with possible dual roles in the endoplasmic reticulum and protein storage vacuole
    • Okamoto T, Toyooka K, Minamikawa T 2001 Identification of a membrane-associated cysteine protease with possible dual roles in the endoplasmic reticulum and protein storage vacuole. J Biol Chem 276:742-751
    • (2001) J Biol Chem , vol.276 , pp. 742-751
    • Okamoto, T.1    Toyooka, K.2    Minamikawa, T.3
  • 63
    • 0027501384 scopus 로고
    • Protein degradation by ERp72 from rat and mouse liver endoplasmic reticulum
    • Urade R, Takenaka Y, Kito M 1993 Protein degradation by ERp72 from rat and mouse liver endoplasmic reticulum. J Biol Chem 268:22004-22009
    • (1993) J Biol Chem , vol.268 , pp. 22004-22009
    • Urade, R.1    Takenaka, Y.2    Kito, M.3
  • 64
    • 0037031241 scopus 로고    scopus 로고
    • The inhibition of microsomal triglyceride transfer protein activity in rat hepatoma cells promotes proteasomal and nonproteasomal degradation of apoprotein b100
    • Cardozo C, Wu X, Pan M, Wang H, Fisher EA 2002 The inhibition of microsomal triglyceride transfer protein activity in rat hepatoma cells promotes proteasomal and nonproteasomal degradation of apoprotein b100. Biochemistry 41:10105-10114
    • (2002) Biochemistry , vol.41 , pp. 10105-10114
    • Cardozo, C.1    Wu, X.2    Pan, M.3    Wang, H.4    Fisher, E.A.5
  • 66
    • 0035902492 scopus 로고    scopus 로고
    • Probing the mechanism of insulin fibril formation with insulin mutants
    • Nielsen L, Frokjaer S, Brange J, Uversky VN, Fink AL 2001 Probing the mechanism of insulin fibril formation with insulin mutants. Biochemistry 40:8397-8409
    • (2001) Biochemistry , vol.40 , pp. 8397-8409
    • Nielsen, L.1    Frokjaer, S.2    Brange, J.3    Uversky, V.N.4    Fink, A.L.5
  • 68
    • 0020581761 scopus 로고
    • Low-molecular-weight constituents of isolated insulin-secretory granules. Bivalent cations, adenine nucleotides and inorganic phosphate
    • Hutton JC, Penn EJ, Peshavaria M 1983 Low-molecular-weight constituents of isolated insulin-secretory granules. Bivalent cations, adenine nucleotides and inorganic phosphate. Biochem J 210:297-305
    • (1983) Biochem J , vol.210 , pp. 297-305
    • Hutton, J.C.1    Penn, E.J.2    Peshavaria, M.3
  • 69
    • 0033839040 scopus 로고    scopus 로고
    • Survey of mRNAs encoding zinc transporters and other metal complexing proteins in pancreatic islets of rats from birth to adulthood: Similar patterns in the Sprague-Dawley and Wistar BB strains
    • Clifford KS, MacDonald MJ 2000 Survey of mRNAs encoding zinc transporters and other metal complexing proteins in pancreatic islets of rats from birth to adulthood: similar patterns in the Sprague-Dawley and Wistar BB strains. Diabetes Res Clin Pract 49:77-85
    • (2000) Diabetes Res Clin Pract , vol.49 , pp. 77-85
    • Clifford, K.S.1    MacDonald, M.J.2
  • 72
    • 0343729333 scopus 로고    scopus 로고
    • Colocalization of chaperone cpn60, proinsulin and convertase PC1 within immature secretory granules of insulin-secreting cells suggests a role for cpn60 in insulin processing
    • Arias AE, Velez-Granell CS, Mayer G, Bendayan M 2000 Colocalization of chaperone cpn60, proinsulin and convertase PC1 within immature secretory granules of insulin-secreting cells suggests a role for cpn60 in insulin processing. J Cell Sci 113:2075-2083
    • (2000) J Cell Sci , vol.113 , pp. 2075-2083
    • Arias, A.E.1    Velez-Granell, C.S.2    Mayer, G.3    Bendayan, M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.