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Volumn 322, Issue 1, 2004, Pages 320-325

Effects of GP2 expression on secretion and endocytosis in pancreatic AR4-2J cells

Author keywords

Endocytosis; Exocrine; GP2; Membrane protein; Pancreas; Secretion; Secretory granule; Secretory pathway

Indexed keywords

AMYLASE; CHOLECYSTOKININ OCTAPEPTIDE; GP2 PROTEIN; MEMBRANE PROTEIN; UNCLASSIFIED DRUG;

EID: 4143053547     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbrc.2004.07.120     Document Type: Article
Times cited : (8)

References (29)
  • 1
    • 0016785996 scopus 로고
    • Intracellular aspects of the process of protein secretion
    • G.E. Palade Intracellular aspects of the process of protein secretion Science 189 1975 347 358
    • (1975) Science , vol.189 , pp. 347-358
    • Palade, G.E.1
  • 2
    • 0015514156 scopus 로고
    • Comparative analysis of zymogen granule membrane polypeptides
    • R.J. MacDonald, and R.A. Ronzio Comparative analysis of zymogen granule membrane polypeptides Biochem. Biophys. Res. Commun. 49 1972 377 382
    • (1972) Biochem. Biophys. Res. Commun. , vol.49 , pp. 377-382
    • MacDonald1    Ronzio, R.A.R.J.2
  • 4
    • 0025727369 scopus 로고
    • A single gene encodes membrane-bound and free forms of GP-2, the major glycoprotein in pancreatic secretory (zymogen) granule membranes
    • S.-I. Fukuoka, S.D. Freedman, and G.A. Scheele 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 1991 2898 2902
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 2898-2902
    • Fukuoka, S.-I.1    Freedman2    Scheele, G.A.S.D.3
  • 5
    • 0030062155 scopus 로고    scopus 로고
    • Polarized secretion of a GPI-anchored exocrine granule protein by apical membrane-restricted proteolysis
    • B.A. Fritz, and A.W. Lowe Polarized secretion of a GPI-anchored exocrine granule protein by apical membrane-restricted proteolysis Am. J. Physiol. 270 1996 G176 G183
    • (1996) Am. J. Physiol. , vol.270
    • Fritz1    Lowe, A.W.B.A.2
  • 6
    • 0025909610 scopus 로고
    • Isolation of the cDNA encoding glycoprotein-2 (GP-2), the major zymogen granule membrane protein
    • T.C. Hoops, and M.J. Rindler Isolation of the cDNA encoding glycoprotein-2 (GP-2), the major zymogen granule membrane protein J. Biol. Chem. 266 1991 4257 4263
    • (1991) J. Biol. Chem. , vol.266 , pp. 4257-4263
    • Hoops1    Rindler, M.J.T.C.2
  • 7
    • 0035957985 scopus 로고    scopus 로고
    • Regulated apical secretion of zymogens in rat pancreas: Involvement of the GPI-anchored glycoprotein GP-2, the lectin ZG16p and cholesterol- glycosphingolipid enriched microdomains
    • K. Schmidt, M. Schrader, H.-F. Kern, and R. Kleene Regulated apical secretion of zymogens in rat pancreas: involvement of the GPI-anchored glycoprotein GP-2, the lectin ZG16p and cholesterol-glycosphingolipid enriched microdomains J. Biol. Chem. 276 2001 14315 14323
    • (2001) J. Biol. Chem. , vol.276 , pp. 14315-14323
    • Schmidt, K.1    Schrader, M.2    Kern3    Kleene, R.H.-F.4
  • 8
    • 0033934448 scopus 로고    scopus 로고
    • A submembranous matrix of proteoglycans on zymogen granule membranes is involved in granule formation in rat pancreatic acinar cells
    • K. Schmidt, H. Dartsch, D. Linder, H.-F. Kern, and R. Kleene A submembranous matrix of proteoglycans on zymogen granule membranes is involved in granule formation in rat pancreatic acinar cells J. Cell Sci. 113 2000 2233 2242
    • (2000) J. Cell Sci. , vol.113 , pp. 2233-2242
    • Schmidt, K.1    Dartsch, H.2    Linder, D.3    Kern4    Kleene, R.H.-F.5
  • 9
    • 0036499901 scopus 로고    scopus 로고
    • Interaction of syncollin with GP-2, the major membrane protein of pancreatic zymogen granules, and association with lipid microdomains
    • I. Kalus, A. Hodel, A. Koch, R. Kleene, J.M. Edwardson, and M. Schrader Interaction of syncollin with GP-2, the major membrane protein of pancreatic zymogen granules, and association with lipid microdomains Biochem. J. 362 2002 433 442
    • (2002) Biochem. J. , vol.362 , pp. 433-442
    • Kalus, I.1    Hodel, A.2    Koch, A.3    Kleene, R.4    Edwardson5    Schrader, M.J.M.6
  • 10
    • 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
    • V. Colomer, K. Lai, T.C. Hoops, and M.J. Rindler 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 1994 3711 3719
    • (1994) EMBO J. , vol.13 , pp. 3711-3719
    • Colomer, V.1    Lai, K.2    Hoops3    Rindler, M.J.T.C.4
  • 11
    • 0026570855 scopus 로고
    • GP-2/THP gene family encodes self-binding glycosylphosphatidylinositol- anchored proteins in apical secretory compartments of pancreas and kidney
    • S.-I. Fukuoka, S.D. Freedman, H. Yu, V.P. Sukhatme, and G.A. Scheele GP-2/THP gene family encodes self-binding glycosylphosphatidylinositol-anchored proteins in apical secretory compartments of pancreas and kidney Proc. Natl. Acad. Sci. USA 89 1992 1189 1193
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 1189-1193
    • Fukuoka, S.-I.1    Freedman, S.D.2    Yu, H.3    Sukhatme4    Scheele, G.A.V.P.5
  • 12
    • 0026934792 scopus 로고
    • Specific interactions of pancreatic amylase at acidic pH. Amylase and the major protein of the zymogen granule membrane (GP-2) bind to immobilized or polymerized amylase
    • M. Jacob, J. Laine, and D. LeBel Specific interactions of pancreatic amylase at acidic pH. Amylase and the major protein of the zymogen granule membrane (GP-2) bind to immobilized or polymerized amylase Biochem. Cell Biol. 70 1992 1105 1114
    • (1992) Biochem. Cell Biol. , vol.70 , pp. 1105-1114
    • Jacob, M.1    Laine2    Lebel, D.J.3
  • 13
    • 0027376899 scopus 로고
    • Reversible pH-induced homophilic binding of GP2, a glycosyl- phosphatidylinositol-anchored protein in pancreatic zymogen granule membranes
    • S.D. Freedman, and G.A. Scheele Reversible pH-induced homophilic binding of GP2, a glycosyl-phosphatidylinositol-anchored protein in pancreatic zymogen granule membranes Eur. J. Cell Biol. 61 1993 229 238
    • (1993) Eur. J. Cell Biol. , vol.61 , pp. 229-238
    • Freedman1    Scheele, G.A.S.D.2
  • 14
    • 0027412124 scopus 로고
    • Reconstitution in vitro of the pH-dependent aggregation of pancreatic zymogens en route to the secretory granule: Implication of GP-2
    • F.A. Leblond, G. Viau, J. Laine, and D. LeBel Reconstitution in vitro of the pH-dependent aggregation of pancreatic zymogens en route to the secretory granule: implication of GP-2 Biochem. J. 291 1993 289 296
    • (1993) Biochem. J. , vol.291 , pp. 289-296
    • Leblond, F.A.1    Viau, G.2    Laine3    Lebel, D.J.4
  • 15
    • 0018584238 scopus 로고
    • Transplantation of azaserine-induced carcinomas of pancreas in rats
    • D.S. Longnecker, H.S. Lilja, J. French, E. Kuhlmann, and W. Noll Transplantation of azaserine-induced carcinomas of pancreas in rats Cancer Lett. 7 1979 197 202
    • (1979) Cancer Lett. , vol.7 , pp. 197-202
    • Longnecker, D.S.1    Lilja, H.S.2    French, J.3    Kuhlmann4    Noll, W.E.5
  • 16
    • 0023230142 scopus 로고
    • Mechanism of glucocorticoid-induced increase in pancreatic amylase gene transcription
    • C.D. Logsdon, K.J. Perot, and A.R. McDonald Mechanism of glucocorticoid-induced increase in pancreatic amylase gene transcription J. Biol. Chem. 262 1987 15765 15769
    • (1987) J. Biol. Chem. , vol.262 , pp. 15765-15769
    • Logsdon, C.D.1    Perot2    McDonald, A.R.K.J.3
  • 17
    • 0023295683 scopus 로고
    • Phasic release of newly synthesized secretory proteins in the unstimulated rat exocrine pancreas
    • P. Arvan, and J.D. Castle Phasic release of newly synthesized secretory proteins in the unstimulated rat exocrine pancreas J. Cell Biol. 104 1987 243 252
    • (1987) J. Cell Biol. , vol.104 , pp. 243-252
    • Arvan1    Castle, J.D.P.2
  • 18
    • 0026709706 scopus 로고
    • The major zymogen granule membrane protein GP-2 in the rat pancreas is not involved in granule formation
    • A. Dittie, and H.-F. Kern The major zymogen granule membrane protein GP-2 in the rat pancreas is not involved in granule formation Eur. J. Cell Biol. 58 1992 243 258
    • (1992) Eur. J. Cell Biol. , vol.58 , pp. 243-258
    • Dittie1    Kern, H.-F.A.2
  • 19
    • 0031883674 scopus 로고    scopus 로고
    • Cleavage of GPI-anchored proteins from the plasma membrane activates apical endocytosis in pancreatic acinar cells
    • S.D. Freedman, H.-F. Kern, and G.A. Scheele Cleavage of GPI-anchored proteins from the plasma membrane activates apical endocytosis in pancreatic acinar cells Eur. J. Cell Biol. 75 1998 163 173
    • (1998) Eur. J. Cell Biol. , vol.75 , pp. 163-173
    • Freedman, S.D.1    Kern2    Scheele, G.A.H.-F.3
  • 20
    • 0034081326 scopus 로고    scopus 로고
    • Mechanisms to explain pancreatic dysfunction in cystic fibrosis
    • S.D. Freedman, P. Blanco, J.C. Shea, and J.G. Alvarez Mechanisms to explain pancreatic dysfunction in cystic fibrosis Med. Clin. North Am. 84 2000 657 664
    • (2000) Med. Clin. North Am. , vol.84 , pp. 657-664
    • Freedman, S.D.1    Blanco, P.2    Shea3    Alvarez, J.G.J.C.4
  • 21
    • 0031932410 scopus 로고    scopus 로고
    • Acinar lumen pH regulates endocytosis, but not exocytosis, at the apical plasma membrane of pancreatic acinar cells
    • S.D. Freedman, H.-F. Kern, and G.A. Scheele Acinar lumen pH regulates endocytosis, but not exocytosis, at the apical plasma membrane of pancreatic acinar cells Eur. J. Cell Biol. 75 1998 153 162
    • (1998) Eur. J. Cell Biol. , vol.75 , pp. 153-162
    • Freedman, S.D.1    Kern2    Scheele, G.A.H.-F.3
  • 22
    • 0034787415 scopus 로고    scopus 로고
    • Pancreatic acinar cell dysfunction in CFTR(-/-) mice is associated with impairments in luminal pH and endocytosis
    • S.D. Freedman, H.F. Kern, and G.A. Scheele Pancreatic acinar cell dysfunction in CFTR(-/-) mice is associated with impairments in luminal pH and endocytosis Gastroenterology 121 2001 950 957
    • (2001) Gastroenterology , vol.121 , pp. 950-957
    • Freedman, S.D.1    Kern2    Scheele, G.A.H.F.3
  • 23
    • 0033543098 scopus 로고    scopus 로고
    • A simple method for constructing E1- and E1/E4-deleted recombinant adenoviral vectors
    • H. Mizuguchi, and M.A. Kay A simple method for constructing E1- and E1/E4-deleted recombinant adenoviral vectors Hum. Gene Ther. 10 1999 2013 2017
    • (1999) Hum. Gene Ther. , vol.10 , pp. 2013-2017
    • Mizuguchi1    Kay, M.A.H.2
  • 24
    • 0021961927 scopus 로고
    • Glucocorticoids increase amylase mRNA levels, secretory organelles, and secretion in pancreatic acinar AR42J cells
    • C.D. Logsdon, J. Mossner, J.A. Williams, and I.D. Goldfine Glucocorticoids increase amylase mRNA levels, secretory organelles, and secretion in pancreatic acinar AR42J cells J. Cell Biol. 100 1985 1200 1208
    • (1985) J. Cell Biol. , vol.100 , pp. 1200-1208
    • Logsdon, C.D.1    Mossner, J.2    Williams3    Goldfine, I.D.J.A.4
  • 25
    • 0036241824 scopus 로고    scopus 로고
    • Processing of the major pancreatic zymogen granule membrane protein, GP2
    • B.A. Fritz, C.S. Poppel, M.W. Fei, and A.W. Lowe Processing of the major pancreatic zymogen granule membrane protein, GP2 Pancreas 24 2002 336 343
    • (2002) Pancreas , vol.24 , pp. 336-343
    • Fritz, B.A.1    Poppel, C.S.2    Fei3    Lowe, A.W.M.W.4
  • 26
    • 0034654035 scopus 로고    scopus 로고
    • Effects of keratin filament disruption on exocrine pancreas-stimulated secretion and susceptibility to injury
    • D.M. Toivola, N.-O. Ku, N. Ghori, A.W. Lowe, S.A. Michie, and M.B. Omary Effects of keratin filament disruption on exocrine pancreas-stimulated secretion and susceptibility to injury Exp. Cell Res. 255 2000 156 170
    • (2000) Exp. Cell Res. , vol.255 , pp. 156-170
    • Toivola, D.M.1    Ku, N.-O.2    Ghori, N.3    Lowe, A.W.4    Michie5    Omary, M.B.S.A.6
  • 27
    • 0041707720 scopus 로고    scopus 로고
    • Intracellular trafficking of a palmitoylated membrane-associated protein component of enveloped vaccinia virus
    • M. Husain, and B. Moss Intracellular trafficking of a palmitoylated membrane-associated protein component of enveloped vaccinia virus J. Virol. 77 2003 9008 9019
    • (2003) J. Virol. , vol.77 , pp. 9008-9019
    • Husain1    Moss, B.M.2
  • 28
    • 0031719218 scopus 로고    scopus 로고
    • New concepts in understanding the pathophysiology of chronic pancreatitis
    • S.D. Freedman New concepts in understanding the pathophysiology of chronic pancreatitis Int. J. Pancreatol. 24 1998 1 8
    • (1998) Int. J. Pancreatol. , vol.24 , pp. 1-8
    • Freedman, S.D.1
  • 29
    • 0028556691 scopus 로고
    • Apical membrane trafficking during regulated pancreatic exocrine secretion - Role of alkaline pH in the acinar lumen and enzymatic cleavage of GP2, a GPI-linked protein
    • S.D. Freedman, H.-F. Kern, and G.A. Scheele Apical membrane trafficking during regulated pancreatic exocrine secretion - role of alkaline pH in the acinar lumen and enzymatic cleavage of GP2, a GPI-linked protein Eur. J. Cell Biol. 65 1994 354 365
    • (1994) Eur. J. Cell Biol. , vol.65 , pp. 354-365
    • Freedman, S.D.1    Kern2    Scheele, G.A.H.-F.3


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