메뉴 건너뛰기




Volumn 73, Issue 3, 1997, Pages 205-214

A novel pancreas-specific serpin (ZG-46p) localises to the soluble and membrane fraction of the Golgi complex and the zymogen granules of acinar cells

Author keywords

Golgi complex; Rat pancreas; Serpin; Sorting; Zymogen granule

Indexed keywords

ANTITHROMBIN III; COMPLEMENTARY DNA; GLYCOSYLATED PROTEIN; MEMBRANE PROTEIN; MESSENGER RNA; SERINE PROTEINASE INHIBITOR; TRYPSIN INHIBITOR; ZYMOGEN GRANULE;

EID: 0030762580     PISSN: 01719335     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (11)

References (42)
  • 1
    • 0027639817 scopus 로고
    • Biogenesis of constitutive secretory vesicles, secretory granules and synaptic vesicles
    • Bauerfeind, R., W. B. Huttner: Biogenesis of constitutive secretory vesicles, secretory granules and synaptic vesicles. Curr. Opin. Cell Biol. 5, 628-635 (1993).
    • (1993) Curr. Opin. Cell Biol. , vol.5 , pp. 628-635
    • Bauerfeind, R.1    Huttner, W.B.2
  • 2
    • 0025857159 scopus 로고
    • Ultrastructural localization of GP2 in acinar cells of pancreas: Presence of GP2 in endocytic and exocytic compartments
    • Beaudoin, A. R., P. St.-Jean, G. Grondin: Ultrastructural localization of GP2 in acinar cells of pancreas: presence of GP2 in endocytic and exocytic compartments. J. Histochem. Cytochem. 39, 575-585 (1991).
    • (1991) J. Histochem. Cytochem. , vol.39 , pp. 575-585
    • Beaudoin, A.R.1    St.-Jean, P.2    Grondin, G.3
  • 3
    • 0019887744 scopus 로고
    • Phase separation of integral membrane proteins in Triton X-114
    • Bordier, C.: Phase separation of integral membrane proteins in Triton X-114. J. Biol. Chem. 256, 1604-1607 (1981).
    • (1981) J. Biol. Chem. , vol.256 , pp. 1604-1607
    • Bordier, C.1
  • 4
    • 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., K. Lal, T. C. Hoops, 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, 3711-3719 (1994).
    • (1994) EMBO J , vol.13 , pp. 3711-3719
    • Colomer, V.1    Lal, K.2    Hoops, T.C.3    Rindler, M.J.4
  • 5
    • 0028587882 scopus 로고
    • cDNA cloning and characterization of a novel 16 kDa protein located in zymogen granules of rat pancreas and goblet cells of the gut
    • Cronshagen, U., P. Voland, H. F. Kern: cDNA cloning and characterization of a novel 16 kDa protein located in zymogen granules of rat pancreas and goblet cells of the gut. Eur. J. Cell Biol. 65, 366-377 (1994).
    • (1994) Eur. J. Cell Biol. , vol.65 , pp. 366-377
    • Cronshagen, U.1    Voland, P.2    Kern, H.F.3
  • 6
    • 0026709706 scopus 로고
    • The major zymogen granule membrane protein GP-2 in the rat pancreas is not involved in granule formation
    • Dittié, A., 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, 243-258 (1992).
    • (1992) Eur. J. Cell Biol. , vol.58 , pp. 243-258
    • Dittié, A.1    Kern, H.F.2
  • 7
    • 0019769965 scopus 로고
    • The Golgi apparatus (complex) -(1954-1981) - From artifact to centerstage
    • Farquhar, M. G., G. E. Palade: The Golgi apparatus (complex) -(1954-1981) - from artifact to centerstage. J. Cell Biol. 91, 77s-103s (1981).
    • (1981) J. Cell Biol. , vol.91
    • Farquhar, M.G.1    Palade, G.E.2
  • 8
    • 0027730475 scopus 로고
    • Regulated secretory proteins in the exocrine pancreas aggregate under conditions that mimic the trans-Golgi network
    • Freedman, S.D., G. A. Scheele: Regulated secretory proteins in the exocrine pancreas aggregate under conditions that mimic the trans-Golgi network. Biochem. Biophys. Res. Commun. 197, 992-999 (1993).
    • (1993) Biochem. Biophys. Res. Commun. , vol.197 , pp. 992-999
    • Freedman, S.D.1    Scheele, G.A.2
  • 9
    • 0027376899 scopus 로고
    • Reversible pH-induced homophilic binding of GP2, a glycosyl-phosphatidylinositol-anchored protein in pancreatic zymogen granule membranes
    • Freedman, S. D., 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, 229-238 (1993).
    • (1993) Eur. J. Cell Biol. , vol.61 , pp. 229-238
    • Freedman, S.D.1    Scheele, G.A.2
  • 10
    • 0022919511 scopus 로고
    • Localization of pancreatic enzyme secretion-stimulating activity and trypsin inhibitory activity in zymogen granule of the rat pancreas
    • Fukuoka, S. J., H. Kawajiri, T. Fushiki, K. Takahashi, K. Iwai: Localization of pancreatic enzyme secretion-stimulating activity and trypsin inhibitory activity in zymogen granule of the rat pancreas. Biochim. Biophys. Acta 884, 18-24 (1986).
    • (1986) Biochim. Biophys. Acta , vol.884 , pp. 18-24
    • Fukuoka, S.J.1    Kawajiri, H.2    Fushiki, T.3    Takahashi, K.4    Iwai, K.5
  • 11
    • 0025727369 scopus 로고
    • A single gene encodes membrane bound and free forms of GP2, the major glycoprotein in pancreatic secretory (zymogen) granule membranes
    • Fukuoka, S. J., S. D. Freedman, G. A. Scheele: A single gene encodes membrane bound and free forms of GP2, the major glycoprotein in pancreatic secretory (zymogen) granule membranes. Proc. Natl. Acad. Sci. USA 88, 2898-2902 (1991).
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 2898-2902
    • Fukuoka, S.J.1    Freedman, S.D.2    Scheele, G.A.3
  • 12
    • 0001851123 scopus 로고
    • Differentiation and development of the pancreas in animals
    • V. L. W. Go, E. P. DiMagno, J. D. Gardner; E. Lebenthal, H. A. Reber, G. A. Scheele (eds.): Raven Press, New York
    • Githens, S.: Differentiation and development of the pancreas in animals. In: V. L. W. Go, E. P. DiMagno, J. D. Gardner; E. Lebenthal, H. A. Reber, G. A. Scheele (eds.): The Pancreas. Biology, Pathobiology and Diseases. pp. 21-56. Raven Press, New York 1993.
    • (1993) The Pancreas. Biology, Pathobiology and Diseases , pp. 21-56
    • Githens, S.1
  • 13
    • 0020606737 scopus 로고
    • Comparison of secretory protein and membrane composition of secretory granules from normal and neoplastic pancreatic acinar cells of rats
    • Hansen, L. J., M. K. Reddy, J. K. Reddy: Comparison of secretory protein and membrane composition of secretory granules from normal and neoplastic pancreatic acinar cells of rats. Proc. Natl. Acad. Sci. USA 80, 4379-4383 (1983).
    • (1983) Proc. Natl. Acad. Sci. USA , vol.80 , pp. 4379-4383
    • Hansen, L.J.1    Reddy, M.K.2    Reddy, J.K.3
  • 14
    • 0003448569 scopus 로고
    • Cold Spring Harbor Laboratory Press. Cold Spring Harbor, New York
    • Harlow, E., D. Lane: Antibodies: A Laboratory Manual. Cold Spring Harbor Laboratory Press. Cold Spring Harbor, New York 1988.
    • (1988) Antibodies: A Laboratory Manual
    • Harlow, E.1    Lane, D.2
  • 15
    • 0022377582 scopus 로고
    • Membrane detachment and release of the major membrane glycoprotein of secretory granules in rat pancreatic exocrine cells
    • Havinga, J. R., J. W. Slot, G. J. Strous: Membrane detachment and release of the major membrane glycoprotein of secretory granules in rat pancreatic exocrine cells. Eur. J. Cell Biol. 39, 70-76 (1985).
    • (1985) Eur. J. Cell Biol. , vol.39 , pp. 70-76
    • Havinga, J.R.1    Slot, J.W.2    Strous, G.J.3
  • 16
    • 0027377051 scopus 로고
    • Incorporation of the pancreatic membrane protein GP2 into secretory granules in exocrine but not endocrine cells
    • Hoops, T. C., J. Ivanov, Z. Cui, V. Colomer-Gould, M. J. Rindler: Incorporation of the pancreatic membrane protein GP2 into secretory granules in exocrine but not endocrine cells. J. Biol. Chem. 268, 25694-25705 (1993).
    • (1993) J. Biol. Chem. , vol.268 , pp. 25694-25705
    • Hoops, T.C.1    Ivanov, J.2    Cui, Z.3    Colomer-Gould, V.4    Rindler, M.J.5
  • 17
    • 0024423930 scopus 로고
    • Implication of the three-dimensional structure of α1-antitrypsin for structure and function of serpins
    • Huber, R., R. W. Carrell: Implication of the three-dimensional structure of α1-antitrypsin for structure and function of serpins. Biochemistry 28, 8951-8966 (1989).
    • (1989) Biochemistry , vol.28 , pp. 8951-8966
    • Huber, R.1    Carrell, R.W.2
  • 18
    • 0026085275 scopus 로고
    • The granin (chromogranin/secrctogranin) family
    • Huttner, W. B., H. H. Gerdes, P. Rosa: The granin (chromogranin/secrctogranin) family. Trends Biochem. Sci. 126, 27-30 (1991).
    • (1991) Trends Biochem. Sci. , vol.126 , pp. 27-30
    • Huttner, W.B.1    Gerdes, H.H.2    Rosa, P.3
  • 19
    • 0023645161 scopus 로고
    • Purification and sequencing of a trypsin-sensitive cholecystokinin-releasing peptide from rat pancreatic juice
    • Iwai, K., S.-I. Fukuoka, T. Fushiki, M. Tsujikawa, M. Hirose, S. Tsunasawa, F. Sakiyama: Purification and sequencing of a trypsin-sensitive cholecystokinin-releasing peptide from rat pancreatic juice. J. Biol. Chem. 262, 8956-8959 (1987).
    • (1987) J. Biol. Chem. , vol.262 , pp. 8956-8959
    • Iwai, K.1    Fukuoka, S.-I.2    Fushiki, T.3    Tsujikawa, M.4    Hirose, M.5    Tsunasawa, S.6    Sakiyama, F.7
  • 20
    • 0026934792 scopus 로고
    • Specific interactions of pancreatic amylase at acidic pH. Amylase and the major protein of the zymogen granule membrane (GP2) bind to immobilized or polymerized amylase
    • Jacob, M., J. Lainé, D. LeBel: Specific interactions of pancreatic amylase at acidic pH. Amylase and the major protein of the zymogen granule membrane (GP2) bind to immobilized or polymerized amylase. Biochem. Cell Biol. 70, 1105-1114 (1992).
    • (1992) Biochem. Cell Biol. , vol.70 , pp. 1105-1114
    • Jacob, M.1    Lainé, J.2    LeBel, D.3
  • 21
    • 0018356117 scopus 로고
    • Preparation of collagen substrates for cell attachment; Effect of collagen concentration and phosphate buffer
    • Kleinmann, H. K., E. B. McGoodwin, S. I. Rennard, G. R. Martin: Preparation of collagen substrates for cell attachment; Effect of collagen concentration and phosphate buffer. Anal. Biochem. 94, 308-312 (1979).
    • (1979) Anal. Biochem. , vol.94 , pp. 308-312
    • Kleinmann, H.K.1    McGoodwin, E.B.2    Rennard, S.I.3    Martin, G.R.4
  • 22
    • 0023811466 scopus 로고
    • The major protein of zymogen granule membranes (GP-2) is anchored via covalent bonds to phosphatidylinositol
    • LeBel, D., M. Beattie: The major protein of zymogen granule membranes (GP-2) is anchored via covalent bonds to phosphatidylinositol. Biochem. Biophys. Res. Commun. 154, 818-823 (1988).
    • (1988) Biochem. Biophys. Res. Commun. , vol.154 , pp. 818-823
    • LeBel, D.1    Beattie, M.2
  • 23
    • 0021961927 scopus 로고
    • Glucocorticoids increase amylase, secretory organelles, and secretion in pancreatic acinar AR42J cells
    • Logsdon, C. D., J. Moessner, J. A. Williams, I. D. Goldfine: Glucocorticoids increase amylase, secretory organelles, and secretion in pancreatic acinar AR42J cells. J. Cell Biol. 100, 1200-1208 (1985).
    • (1985) J. Cell Biol. , vol.100 , pp. 1200-1208
    • Logsdon, C.D.1    Moessner, J.2    Williams, J.A.3    Goldfine, I.D.4
  • 24
    • 0023663868 scopus 로고
    • The trans-most cisternae of the Golgi complex: A compartment for sorting of secretory and plasma membrane proteins
    • Orci, L. M., M. Ravazzola, M. Amherdt, A. Perrelet, S. K. Powell, D. L. Quinn, H. P. H. Moore: The trans-most cisternae of the Golgi complex: a compartment for sorting of secretory and plasma membrane proteins. Cell 51, 1039-1049 (1987).
    • (1987) Cell , vol.51 , pp. 1039-1049
    • Orci, L.M.1    Ravazzola, M.2    Amherdt, M.3    Perrelet, A.4    Powell, S.K.5    Quinn, D.L.6    Moore, H.P.H.7
  • 25
    • 0344601186 scopus 로고
    • The use of two-dimensional gel electrophoresis and high-performance liquid chromatography for the analysis of pancreatic juice
    • V. L. W. Go, E. P. DiMagno, J. D. Gardner; E. Lebenthal, H. A. Reber, G. A. Scheele (eds.): Raven Press. New York
    • Padfield, P. J., G. A. Scheele: The use of two-dimensional gel electrophoresis and high-performance liquid chromatography for the analysis of pancreatic juice. In: V. L. W. Go, E. P. DiMagno, J. D. Gardner; E. Lebenthal, H. A. Reber, G. A. Scheele (eds.): The Pancreas Biology, Pathobiology and Diseases. pp. 265-274. Raven Press. New York 1993.
    • (1993) The Pancreas Biology, Pathobiology and Diseases , pp. 265-274
    • Padfield, P.J.1    Scheele, G.A.2
  • 26
    • 0026731817 scopus 로고
    • Chromogranin B (secretogranin I), a secretory protein of the regulated pathway, is also present in a tightly membrane-associated form in PC12 cells
    • Pimplikar, S. W., W. B. Huttner: Chromogranin B (secretogranin I), a secretory protein of the regulated pathway, is also present in a tightly membrane-associated form in PC12 cells. J. Biol. Chem. 267, 4110-4118 (1992).
    • (1992) J. Biol. Chem. , vol.267 , pp. 4110-4118
    • Pimplikar, S.W.1    Huttner, W.B.2
  • 27
    • 0028206262 scopus 로고
    • The serpin superfamily of proteinase inhibitors: Structure, function, and regulation
    • Potempa, J., E. Korzus, J. Travis: The serpin superfamily of proteinase inhibitors: structure, function, and regulation. J. Biol. Chem. 269, 15957-15960 (1994).
    • (1994) J. Biol. Chem. , vol.269 , pp. 15957-15960
    • Potempa, J.1    Korzus, E.2    Travis, J.3
  • 28
    • 0023146835 scopus 로고
    • Stimulation of pancreatic secretory process in the rat by low molecular weight proteinase inhibitor
    • Rausch, U., G. Adler, H. Weidenbach, F. Weidenbach, D. Rudolff, J. Koop, H. F. Kern: Stimulation of pancreatic secretory process in the rat by low molecular weight proteinase inhibitor. Cell Tissue Res. 247, 187-193 (1987).
    • (1987) Cell Tissue Res. , vol.247 , pp. 187-193
    • Rausch, U.1    Adler, G.2    Weidenbach, H.3    Weidenbach, F.4    Rudolff, D.5    Koop, J.6    Kern, H.F.7
  • 29
    • 0002884935 scopus 로고
    • Pancreatic secretory enzymes
    • V. L. W. Go, E. P. DiMagno, J. D. Gardner; E. Lebenthal, H. A. Reber, G. A. Scheele (eds.): Raven Press. New York
    • Rinderknecht, H.: Pancreatic secretory enzymes. In: V. L. W. Go, E. P. DiMagno, J. D. Gardner; E. Lebenthal, H. A. Reber, G. A. Scheele (eds.): The Pancreas, Biology, Pathobiology, and Diseases. pp. 219-252. Raven Press. New York 1993.
    • (1993) The Pancreas, Biology, Pathobiology, and Diseases , pp. 219-252
    • Rinderknecht, H.1
  • 30
    • 0025116390 scopus 로고
    • The pancreatic membrane protein GP-2 localizes specifically to secretory granules and is shed into the pancreatic juice as a protein aggregate
    • Rindler, M. J., T. C. Hoops: The pancreatic membrane protein GP-2 localizes specifically to secretory granules and is shed into the pancreatic juice as a protein aggregate. Eur. J. Cell Biol. 53, 154-10 (1990).
    • (1990) Eur. J. Cell Biol. , vol.53 , pp. 154-210
    • Rindler, M.J.1    Hoops, T.C.2
  • 32
    • 0001871689 scopus 로고
    • Regulation of pancreatic gene expression is response to hormones and nutrional substrates
    • V. L. W. Go, E. P. DiMagno, J. D. Gardner: E. Lebenthal, H. A. Reber, G. A. Scheele (eds.): Raven Press. New York
    • Scheele, G. A.: Regulation of pancreatic gene expression is response to hormones and nutrional substrates. In: V. L. W. Go, E. P. DiMagno, J. D. Gardner: E. Lebenthal, H. A. Reber, G. A. Scheele (eds.): The Pancreas. Biology, Pathobiology and Diseases. pp. 103-120. Raven Press. New York 1993.
    • (1993) The Pancreas. Biology, Pathobiology and Diseases , pp. 103-120
    • Scheele, G.A.1
  • 33
    • 0028044809 scopus 로고
    • Role of the GP2/ THP family of GPI-anchored proteins in membrane trafficking during regulated exocrine secretion
    • Scheele, G. A., S. I. Fukuoka, S. D. Freedman: Role of the GP2/ THP family of GPI-anchored proteins in membrane trafficking during regulated exocrine secretion. Pancreas 9, 139-149 (1994).
    • (1994) Pancreas , vol.9 , pp. 139-149
    • Scheele, G.A.1    Fukuoka, S.I.2    Freedman, S.D.3
  • 34
    • 0001029428 scopus 로고
    • Cellular compartmentation, protein processing, and secretion in the exocrine pancreas
    • V. L. W. Go, E. P. DiMagno, J. D. Gardner; E. Lebenthal, H. A. Reber, G. A. Scheele (eds): Raven Press. New York
    • Scheele, G. A., H. F. Kern: Cellular compartmentation, protein processing, and secretion in the exocrine pancreas. In: V. L. W. Go, E. P. DiMagno, J. D. Gardner; E. Lebenthal, H. A. Reber, G. A. Scheele (eds): The Pancreas. Biology, Pathobiology and Diseases. pp. 121-150. Raven Press. New York 1993.
    • (1993) The Pancreas. Biology, Pathobiology and Diseases , pp. 121-150
    • Scheele, G.A.1    Kern, H.F.2
  • 35
    • 0016688215 scopus 로고
    • Studies on the guinea pig pancreas: Parallel discharge of exocrine enzyme activities
    • Scheele, G. A., G. E. Palade: Studies on the guinea pig pancreas: parallel discharge of exocrine enzyme activities. J. Biol. Chem. 250, 2660-2670 (1975).
    • (1975) J. Biol. Chem. , vol.250 , pp. 2660-2670
    • Scheele, G.A.1    Palade, G.E.2
  • 36
    • 0021750606 scopus 로고
    • Hormonal stimulation in the exocrine pancreas results in coordinate and anticoordinate regulation of protein synthesis
    • Schick, J., H. F. Kern, G. A. Scheele: Hormonal stimulation in the exocrine pancreas results in coordinate and anticoordinate regulation of protein synthesis. J. Cell Biol. 99, 1569-1574 (1984).
    • (1984) J. Cell Biol. , vol.99 , pp. 1569-1574
    • Schick, J.1    Kern, H.F.2    Scheele, G.A.3
  • 37
    • 0029589824 scopus 로고
    • What do dysfunctional serpins tell us about molecular mobility and disease?
    • Stein, P. E., R. W. Carrell: What do dysfunctional serpins tell us about molecular mobility and disease? Nature Struct. Biol. 2, 96-113 (1995).
    • (1995) Nature Struct. Biol. , vol.2 , pp. 96-113
    • Stein, P.E.1    Carrell, R.W.2
  • 38
    • 0023778584 scopus 로고
    • Coupled induction of exocrine proteins and intracellular compartments involved in the secretory pathway in AR4-2J cells by glucocorticoids
    • Swarowsky, B., W. Steinhilber, G. A. Scheele, H. F. Kern: Coupled induction of exocrine proteins and intracellular compartments involved in the secretory pathway in AR4-2J cells by glucocorticoids. Eur. J. Cell Biol. 47, 101-111 (1988).
    • (1988) Eur. J. Cell Biol. , vol.47 , pp. 101-111
    • Swarowsky, B.1    Steinhilber, W.2    Scheele, G.A.3    Kern, H.F.4
  • 39
    • 0023601046 scopus 로고
    • Sorting of progeny corona virus from condensed secretory proteins at the exit from the trans-Golgi network of AtT20 cells
    • Tooze, J., S. A. Tooze, S. D. Fuller: Sorting of progeny corona virus from condensed secretory proteins at the exit from the trans-Golgi network of AtT20 cells. J. Cell Biol. 105, 1215-1226 (1987).
    • (1987) J. Cell Biol. , vol.105 , pp. 1215-1226
    • Tooze, J.1    Tooze, S.A.2    Fuller, S.D.3
  • 41
    • 0023887327 scopus 로고
    • Purification, characterization and amino acid sequencing of two pancreatic secretory trypsin inhibitors in rat pancreatic juice
    • Uda, K., M. Ogawa, T. Shibata: Purification, characterization and amino acid sequencing of two pancreatic secretory trypsin inhibitors in rat pancreatic juice. Biol. Chem. Hoppe-Seyler 369, 55-61 (1988).
    • (1988) Biol. Chem. Hoppe-Seyler , vol.369 , pp. 55-61
    • Uda, K.1    Ogawa, M.2    Shibata, T.3
  • 42
    • 1842377884 scopus 로고
    • Proteinase-Inhibitoren
    • G. Fischer Verlag. Stuttgart
    • Urich, K.: Proteinase-Inhibitoren. In: Vergleichende Biochemie der Tiere pp. 86-94. G. Fischer Verlag. Stuttgart 1990.
    • (1990) Vergleichende Biochemie der Tiere , pp. 86-94
    • Urich, K.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.