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Volumn 9, Issue 10, 2010, Pages 4927-4939

Analysis of low abundance membrane-associated proteins from rat pancreatic zymogen granules

Author keywords

2D gel electrophoresis; exocrine pancreas; membrane associated proteins; organelle biogenesis; tandem mass spectrometry; zymogen granules

Indexed keywords

CALNEXIN; CHYMASE; CYCLOPHILIN B; HYBRID PROTEIN; MEMBRANE PROTEIN; PROTEIN YFP; UNCLASSIFIED DRUG; ZYMOGEN GRANULE;

EID: 77957346850     PISSN: 15353893     EISSN: 15353907     Source Type: Journal    
DOI: 10.1021/pr100052q     Document Type: Article
Times cited : (15)

References (83)
  • 1
    • 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, G.; Laine, J.; Lebel, D. Reconstitution in vitro of the pH-dependent aggregation of pancreatic zymogens en route to the secretory granule: implication of GP-2 Biochem. J. 1993, 291 (Pt 1) 289-96
    • (1993) Biochem. J. , vol.291 , Issue.PART 1 , pp. 289-296
    • Leblond, F.A.1    Viau, G.2    Laine, J.3    Lebel, D.4
  • 2
    • 0027730475 scopus 로고
    • Regulated secretory proteins in the exocrine pancreas aggregate under conditions that mimic the trans-Golgi network
    • Freedman, S. D.; Scheele, G. A. Regulated secretory proteins in the exocrine pancreas aggregate under conditions that mimic the trans-Golgi network Biochem. Biophys. Res. Commun. 1993, 197 (2) 992-9
    • (1993) Biochem. Biophys. Res. Commun. , vol.197 , Issue.2 , pp. 992-999
    • Freedman, S.D.1    Scheele, G.A.2
  • 3
    • 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.; Kicska, G. A.; Rindler, M. J. Secretory granule content proteins and the luminal domains of granule membrane proteins aggregate in vitro at mildly acidic pH J. Biol. Chem. 1996, 271 (1) 48-55
    • (1996) J. Biol. Chem. , vol.271 , Issue.1 , pp. 48-55
    • Colomer, V.1    Kicska, G.A.2    Rindler, M.J.3
  • 4
    • 0031948922 scopus 로고    scopus 로고
    • In vitro condensation-sorting of enzyme proteins isolated from rat pancreatic acinar cells
    • Dartsch, H.; Kleene, R.; Kern, H. F. In vitro condensation-sorting of enzyme proteins isolated from rat pancreatic acinar cells Eur. J. Cell Biol. 1998, 75, 211-22
    • (1998) Eur. J. Cell Biol. , vol.75 , pp. 211-222
    • Dartsch, H.1    Kleene, R.2    Kern, H.F.3
  • 5
    • 0032526224 scopus 로고    scopus 로고
    • Sorting and storage during secretory granule biogenesis: Looking backward and looking forward
    • Arvan, P.; Castle, D. Sorting and storage during secretory granule biogenesis: looking backward and looking forward Biochem. J. 1998, 332 (Pt 3) 593-610
    • (1998) Biochem. J. , vol.332 , Issue.PART 3 , pp. 593-610
    • Arvan, P.1    Castle, D.2
  • 7
    • 0035280141 scopus 로고    scopus 로고
    • Secretory granule biogenesis: Rafting to the SNARE
    • Tooze, S. A.; Martens, G. J. M.; Huttner, W. B. Secretory granule biogenesis: rafting to the SNARE Trends Cell Biol. 2001, 11 (3) 116-22
    • (2001) Trends Cell Biol. , vol.11 , Issue.3 , pp. 116-122
    • Tooze, S.A.1    Martens, G.J.M.2    Huttner, W.B.3
  • 8
    • 0036157849 scopus 로고    scopus 로고
    • The regulation of exocytosis in the pancreatic acinar cell
    • Wasle, B.; Edwardson, J. M. The regulation of exocytosis in the pancreatic acinar cell Cell Signal. 2002, 14 (3) 191-7
    • (2002) Cell Signal. , vol.14 , Issue.3 , pp. 191-197
    • Wasle, B.1    Edwardson, J.M.2
  • 9
    • 33746894711 scopus 로고    scopus 로고
    • Regulation of pancreatic acinar cell function
    • Williams, J. A. Regulation of pancreatic acinar cell function Curr. Opin. Gastroenterol. 2006, 22 (5) 498-504
    • (2006) Curr. Opin. Gastroenterol. , vol.22 , Issue.5 , pp. 498-504
    • Williams, J.A.1
  • 10
    • 68949206485 scopus 로고    scopus 로고
    • The pancreatic zymogen granule membrane protein, GP2, binds Escherichia coli Type 1 fimbriae
    • Yu, S.; Lowe, A. W. The pancreatic zymogen granule membrane protein, GP2, binds Escherichia coli Type 1 fimbriae BMC Gastroenterol. 2009, 9, 58
    • (2009) BMC Gastroenterol. , vol.9 , pp. 58
    • Yu, S.1    Lowe, A.W.2
  • 12
    • 7444264196 scopus 로고    scopus 로고
    • Membrane targeting in secretion
    • Schrader, M. Membrane targeting in secretion Subcell. Biochem. 2004, 37, 391-421
    • (2004) Subcell. Biochem. , vol.37 , pp. 391-421
    • Schrader, M.1
  • 13
    • 66149085220 scopus 로고    scopus 로고
    • New insights into the mechanisms of pancreatitis
    • Gaisano, H. Y.; Gorelick, F. S. New insights into the mechanisms of pancreatitis Gastroenterology 2009, 136 (7) 2040-4
    • (2009) Gastroenterology , vol.136 , Issue.7 , pp. 2040-2044
    • Gaisano, H.Y.1    Gorelick, F.S.2
  • 14
    • 34548164149 scopus 로고    scopus 로고
    • Proteomic Analysis of Pancreatic Zymogen Granules: Identification of New Granule Proteins
    • Rindler, M. J.; Xu, C. F.; Gumper, I.; Smith, N. N.; Neubert, T. A. Proteomic Analysis of Pancreatic Zymogen Granules: Identification of New Granule Proteins J. Proteome Res. 2007, 6, 2978-92
    • (2007) J. Proteome Res. , vol.6 , pp. 2978-2992
    • Rindler, M.J.1    Xu, C.F.2    Gumper, I.3    Smith, N.N.4    Neubert, T.A.5
  • 16
    • 0033934448 scopus 로고    scopus 로고
    • A submembranous matrix of proteoglycans on zymogen granule membranes is involved in granule formation in rat pancreatic acinar cells
    • Schmidt, K.; Dartsch, H.; Linder, D.; Kern, H.; Kleene, R. A submembranous matrix of proteoglycans on zymogen granule membranes is involved in granule formation in rat pancreatic acinar cells J. Cell Sci. 2000, 113 (Pt 12) 2233-42
    • (2000) J. Cell Sci. , vol.113 , Issue.PART 12 , pp. 2233-2242
    • Schmidt, K.1    Dartsch, H.2    Linder, D.3    Kern, H.4    Kleene, R.5
  • 17
    • 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
    • Schmidt, K.; Schrader, M.; Kern, H. F.; Kleene, R. 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. 2001, 276, 14315-23
    • (2001) J. Biol. Chem. , vol.276 , pp. 14315-14323
    • Schmidt, K.1    Schrader, M.2    Kern, H.F.3    Kleene, R.4
  • 19
    • 43149088924 scopus 로고    scopus 로고
    • Rab8 is involved in zymogen granule formation in pancreatic acinar AR42J cells
    • Faust, F.; Gomez-Lazaro, M.; Borta, H.; Agricola, B.; Schrader, M. Rab8 is involved in zymogen granule formation in pancreatic acinar AR42J cells Traffic 2008, 9 (6) 964-79
    • (2008) Traffic , vol.9 , Issue.6 , pp. 964-979
    • Faust, F.1    Gomez-Lazaro, M.2    Borta, H.3    Agricola, B.4    Schrader, M.5
  • 20
    • 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.; Voland, P.; Kern, H. F. 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. 1994, 65 (2) 366-77
    • (1994) Eur. J. Cell Biol. , vol.65 , Issue.2 , pp. 366-377
    • Cronshagen, U.1    Voland, P.2    Kern, H.F.3
  • 21
    • 0028343964 scopus 로고
    • Chicken antibodies to rabbit muscle actin with a restricted repertoire of F-actin recognition
    • Schrader, M.; Temm-Grove, C. J.; Lessard, J. L.; Jockusch, B. M. Chicken antibodies to rabbit muscle actin with a restricted repertoire of F-actin recognition Eur. J. Cell Biol. 1994, 63 (2) 326-35
    • (1994) Eur. J. Cell Biol. , vol.63 , Issue.2 , pp. 326-335
    • Schrader, M.1    Temm-Grove, C.J.2    Lessard, J.L.3    Jockusch, B.M.4
  • 22
    • 0031807109 scopus 로고    scopus 로고
    • Use of thiourea to increase the solubility of membrane proteins in two-dimensional electrophoresis
    • DOI 10.1002/elps.1150190526
    • Rabilloud, T. Use of thiourea to increase the solubility of membrane proteins in two-dimensional electrophoresis Electrophoresis 1998, 19 (5) 758-60 (Pubitemid 28236679)
    • (1998) Electrophoresis , vol.19 , Issue.5 , pp. 758-760
    • Rabilloud, T.1
  • 23
    • 0033662168 scopus 로고    scopus 로고
    • A modified silver staining protocol for visualization of proteins compatible with matrix-assisted laser desorption/ionization and electrospray ionization-mass spectrometry
    • Yan, J. X.; Wait, R.; Berkelman, T.; Harry, R. A.; Westbrook, J. A.; Wheeler, C. H.; Dunn, M. J. A modified silver staining protocol for visualization of proteins compatible with matrix-assisted laser desorption/ionization and electrospray ionization-mass spectrometry Electrophoresis 2000, 21 (17) 3666-72
    • (2000) Electrophoresis , vol.21 , Issue.17 , pp. 3666-3672
    • Yan, J.X.1    Wait, R.2    Berkelman, T.3    Harry, R.A.4    Westbrook, J.A.5    Wheeler, C.H.6    Dunn, M.J.7
  • 24
    • 0018356117 scopus 로고
    • Preparation of collagen substrates for cell attachment: Effect of collagen concentration and phosphate buffer
    • Kleinman, H. K.; McGoodwin, E. B.; Rennard, S. I.; Martin, G. R. Preparation of collagen substrates for cell attachment: effect of collagen concentration and phosphate buffer Anal. Biochem. 1979, 94 (2) 308-12
    • (1979) Anal. Biochem. , vol.94 , Issue.2 , pp. 308-312
    • Kleinman, H.K.1    McGoodwin, E.B.2    Rennard, S.I.3    Martin, G.R.4
  • 26
    • 38449099776 scopus 로고    scopus 로고
    • Cryosectioning and immunolabeling
    • Slot, J. W.; Geuze, H. J. Cryosectioning and immunolabeling Nat. Protoc. 2007, 2 (10) 2480-91
    • (2007) Nat. Protoc. , vol.2 , Issue.10 , pp. 2480-2491
    • Slot, J.W.1    Geuze, H.J.2
  • 27
    • 34548020973 scopus 로고    scopus 로고
    • Correlative light and electron microscopy using immunolabeled resin sections
    • Schwarz, H.; Humbel, B. M. Correlative light and electron microscopy using immunolabeled resin sections Methods Mol. Biol. 2007, 369, 229-56
    • (2007) Methods Mol. Biol. , vol.369 , pp. 229-256
    • Schwarz, H.1    Humbel, B.M.2
  • 28
    • 0020591172 scopus 로고
    • Secretory responses of hypertrophied rat pancreas induced by repeated oral administrations of a synthetic protease inhibitor
    • Yonezawa, H. Secretory responses of hypertrophied rat pancreas induced by repeated oral administrations of a synthetic protease inhibitor Jpn. J. Physiol. 1983, 33 (2) 183-95
    • (1983) Jpn. J. Physiol. , vol.33 , Issue.2 , pp. 183-195
    • Yonezawa, H.1
  • 29
    • 0035875485 scopus 로고    scopus 로고
    • Cholesterol-dependent interaction of syncollin with the membrane of the pancreatic zymogen granule
    • Hodel, A.; An, S. J.; Hansen, N. J.; Lawrence, J.; Wasle, B.; Schrader, M.; Edwardson, J. M. Cholesterol-dependent interaction of syncollin with the membrane of the pancreatic zymogen granule Biochem. J. 2001, 356 (Pt 3) 843-50
    • (2001) Biochem. J. , vol.356 , Issue.PART 3 , pp. 843-850
    • Hodel, A.1    An, S.J.2    Hansen, N.J.3    Lawrence, J.4    Wasle, B.5    Schrader, M.6    Edwardson, J.M.7
  • 30
    • 0036499901 scopus 로고    scopus 로고
    • Interaction of syncollin with GP-2, the major membrane protein of pancreatic zymogen granules, and association with lipid microdomains
    • Kalus, I.; Hodel, A.; Koch, A.; Kleene, R.; Michael Edwardson, J.; Schrader, M. Interaction of syncollin with GP-2, the major membrane protein of pancreatic zymogen granules, and association with lipid microdomains Biochem. J. 2002, 362 (Pt 2) 433-42
    • (2002) Biochem. J. , vol.362 , Issue.PART 2 , pp. 433-442
    • Kalus, I.1    Hodel, A.2    Koch, A.3    Kleene, R.4    Michael Edwardson, J.5    Schrader, M.6
  • 31
    • 0033010364 scopus 로고    scopus 로고
    • Complex formation among rat pancreatic secretory proteins under mild alkaline pH conditions
    • Kleene, R.; Kastner, B.; Rosser, R.; Kern, H. Complex formation among rat pancreatic secretory proteins under mild alkaline pH conditions Digestion 1999, 60 (4) 305-13
    • (1999) Digestion , vol.60 , Issue.4 , pp. 305-313
    • Kleene, R.1    Kastner, B.2    Rosser, R.3    Kern, H.4
  • 32
    • 0032587136 scopus 로고    scopus 로고
    • The secretory lectin ZG16p mediates sorting of enzyme proteins to the zymogen granule membrane in pancreatic acinar cells
    • Kleene, R.; Dartsch, H.; Kern, H. F. The secretory lectin ZG16p mediates sorting of enzyme proteins to the zymogen granule membrane in pancreatic acinar cells Eur. J. Cell Biol. 1999, 78, 79-90
    • (1999) Eur. J. Cell Biol. , vol.78 , pp. 79-90
    • Kleene, R.1    Dartsch, H.2    Kern, H.F.3
  • 33
    • 0030872595 scopus 로고    scopus 로고
    • The secretory granule protein syncollin binds to syntaxin in a Ca2(+)- sensitive manner
    • Edwardson, J. M.; An, S.; Jahn, R. The secretory granule protein syncollin binds to syntaxin in a Ca2(+)- sensitive manner Cell 1997, 90 (2) 325-33
    • (1997) Cell , vol.90 , Issue.2 , pp. 325-333
    • Edwardson, J.M.1    An, S.2    Jahn, R.3
  • 34
    • 0028229078 scopus 로고
    • Interaction of heparin with rat mast cell protease 1
    • Pejler, G.; Maccarana, M. Interaction of heparin with rat mast cell protease 1 J. Biol. Chem. 1994, 269 (20) 14451-6 (Pubitemid 24193997)
    • (1994) Journal of Biological Chemistry , vol.269 , Issue.20 , pp. 14451-14456
    • Pejler, G.1    Maccarana, M.2
  • 35
    • 0033554430 scopus 로고    scopus 로고
    • Mechanism by which heparin proteoglycan modulates mast cell chymase activity
    • Pejler, G.; Sadler, J. E. Mechanism by which heparin proteoglycan modulates mast cell chymase activity Biochemistry 1999, 38 (37) 12187-95
    • (1999) Biochemistry , vol.38 , Issue.37 , pp. 12187-12195
    • Pejler, G.1    Sadler, J.E.2
  • 36
    • 0028882013 scopus 로고
    • Regulation of rat mast cell protease 1 activity. Protease inhibition is prevented by heparin proteoglycan
    • Pejler, G.; Berg, L. Regulation of rat mast cell protease 1 activity. Protease inhibition is prevented by heparin proteoglycan Eur. J. Biochem. 1995, 233 (1) 192-9
    • (1995) Eur. J. Biochem. , vol.233 , Issue.1 , pp. 192-199
    • Pejler, G.1    Berg, L.2
  • 37
    • 58149287751 scopus 로고    scopus 로고
    • Global topology analysis of pancreatic zymogen granule membrane proteins
    • Chen, X.; Ulintz, P. J.; Simon, E. S.; Williams, J. A.; Andrews, P. C. Global topology analysis of pancreatic zymogen granule membrane proteins Mol. Cell. Proteomics 2008, 7 (12) 2323-36
    • (2008) Mol. Cell. Proteomics , vol.7 , Issue.12 , pp. 2323-2336
    • Chen, X.1    Ulintz, P.J.2    Simon, E.S.3    Williams, J.A.4    Andrews, P.C.5
  • 38
    • 0025287491 scopus 로고
    • Molecular cloning of a complementary DNA to rat cyclophilin-like protein mRNA
    • Iwai, N.; Inagami, T. Molecular cloning of a complementary DNA to rat cyclophilin-like protein mRNA Kidney Int. 1990, 37 (6) 1460-5
    • (1990) Kidney Int. , vol.37 , Issue.6 , pp. 1460-1465
    • Iwai, N.1    Inagami, T.2
  • 40
    • 73449125521 scopus 로고    scopus 로고
    • Proteomic identification of multitasking proteins in unexpected locations complicates drug targeting
    • Butler, G. S.; Overall, C. M. Proteomic identification of multitasking proteins in unexpected locations complicates drug targeting Nat. Rev. Drug Discovery 2009, 8 (12) 935-48
    • (2009) Nat. Rev. Drug Discovery , vol.8 , Issue.12 , pp. 935-948
    • Butler, G.S.1    Overall, C.M.2
  • 41
    • 0037177882 scopus 로고    scopus 로고
    • Charcot-Leyden crystal protein (galectin-10) is not a dual function galectin with lysophospholipase activity but binds a lysophospholipase inhibitor in a novel structural fashion
    • Ackerman, S. J.; Liu, L.; Kwatia, M. A.; Savage, M. P.; Leonidas, D. D.; Swaminathan, G. J.; Acharya, K. R. Charcot-Leyden crystal protein (galectin-10) is not a dual function galectin with lysophospholipase activity but binds a lysophospholipase inhibitor in a novel structural fashion J. Biol. Chem. 2002, 277 (17) 14859-68
    • (2002) J. Biol. Chem. , vol.277 , Issue.17 , pp. 14859-14868
    • Ackerman, S.J.1    Liu, L.2    Kwatia, M.A.3    Savage, M.P.4    Leonidas, D.D.5    Swaminathan, G.J.6    Acharya, K.R.7
  • 42
    • 0035968445 scopus 로고    scopus 로고
    • Bile salt-dependent lipase: Its pathophysiological implications
    • Lombardo, D. Bile salt-dependent lipase: its pathophysiological implications Biochim. Biophys. Acta 2001, 1533 (1) 1-28
    • (2001) Biochim. Biophys. Acta , vol.1533 , Issue.1 , pp. 1-28
    • Lombardo, D.1
  • 43
    • 0018877342 scopus 로고
    • Studies on the substrate specificity of a carboxyl ester hydrolase from human pancreatic juice. I. Action on carboxyl esters, glycerides and phospholipids
    • Lombardo, D.; Fauvel, J.; Guy, O. Studies on the substrate specificity of a carboxyl ester hydrolase from human pancreatic juice. I. Action on carboxyl esters, glycerides and phospholipids Biochim. Biophys. Acta 1980, 611 (1) 136-46 (Pubitemid 10168188)
    • (1980) Biochimica et Biophysica Acta , vol.611 , Issue.1 , pp. 136-146
    • Lombardo, D.1    Fauvel, J.2    Guy, O.3
  • 44
    • 0028825918 scopus 로고
    • Association of bile-salt-dependent lipase with membranes of human pancreatic microsomes
    • Bruneau, N.; de la Porte, P. L.; Sbarra, V.; Lombardo, D. Association of bile-salt-dependent lipase with membranes of human pancreatic microsomes Eur. J. Biochem. 1995, 233 (1) 209-18
    • (1995) Eur. J. Biochem. , vol.233 , Issue.1 , pp. 209-218
    • Bruneau, N.1    De La Porte, P.L.2    Sbarra, V.3    Lombardo, D.4
  • 45
    • 0029025326 scopus 로고
    • Chaperone function of a Grp 94-related protein for folding and transport of the pancreatic bile salt-dependent lipase
    • Bruneau, N.; Lombardo, D. Chaperone function of a Grp 94-related protein for folding and transport of the pancreatic bile salt-dependent lipase J. Biol. Chem. 1995, 270 (22) 13524-33
    • (1995) J. Biol. Chem. , vol.270 , Issue.22 , pp. 13524-13533
    • Bruneau, N.1    Lombardo, D.2
  • 46
    • 0025045118 scopus 로고
    • Protein disulfide-isomerase in rat exocrine pancreatic cells is exported from the endoplasmic reticulum despite possessing the retention signal
    • Yoshimori, T.; Semba, T.; Takemoto, H.; Akagi, S.; Yamamoto, A.; Tashiro, Y. Protein disulfide-isomerase in rat exocrine pancreatic cells is exported from the endoplasmic reticulum despite possessing the retention signal J. Biol. Chem. 1990, 265 (26) 15984-90
    • (1990) J. Biol. Chem. , vol.265 , Issue.26 , pp. 15984-15990
    • Yoshimori, T.1    Semba, T.2    Takemoto, H.3    Akagi, S.4    Yamamoto, A.5    Tashiro, Y.6
  • 47
    • 0034658094 scopus 로고    scopus 로고
    • Roles of molecular chaperones in pancreatic secretion and their involvement in intestinal absorption
    • Bruneau, N.; Lombardo, D.; Levy, E.; Bendayan, M. Roles of molecular chaperones in pancreatic secretion and their involvement in intestinal absorption Microsc. Res. Tech. 2000, 49 (4) 329-45
    • (2000) Microsc. Res. Tech. , vol.49 , Issue.4 , pp. 329-345
    • Bruneau, N.1    Lombardo, D.2    Levy, E.3    Bendayan, M.4
  • 48
    • 0021961927 scopus 로고
    • Glucocorticoids increase amylase mRNA levels, secretory organelles, and secretion in pancreatic acinar AR42J cells
    • Logsdon, C. D.; Moessner, J.; Williams, J. A.; Goldfine, I. D. Glucocorticoids increase amylase mRNA levels, secretory organelles, and secretion in pancreatic acinar AR42J cells J. Cell Biol. 1985, 100 (4) 1200-8
    • (1985) J. Cell Biol. , vol.100 , Issue.4 , pp. 1200-1208
    • Logsdon, C.D.1    Moessner, J.2    Williams, J.A.3    Goldfine, I.D.4
  • 49
    • 4143053547 scopus 로고    scopus 로고
    • Effects of GP2 expression on secretion and endocytosis in pancreatic AR4-2J cells
    • Yu, S.; Hao, Y.; Lowe, A. W. Effects of GP2 expression on secretion and endocytosis in pancreatic AR4-2J cells Biochem. Biophys. Res. Commun. 2004, 322 (1) 320-5
    • (2004) Biochem. Biophys. Res. Commun. , vol.322 , Issue.1 , pp. 320-325
    • Yu, S.1    Hao, Y.2    Lowe, A.W.3
  • 51
    • 0037324287 scopus 로고    scopus 로고
    • Mast cell chymase induces smooth muscle cell apoptosis by a mechanism involving fibronectin degradation and disruption of focal adhesions
    • Leskinen, M. J.; Lindstedt, K. A.; Wang, Y.; Kovanen, P. T. Mast cell chymase induces smooth muscle cell apoptosis by a mechanism involving fibronectin degradation and disruption of focal adhesions Arterioscler. Thromb. Vasc. Biol. 2003, 23 (2) 238-43
    • (2003) Arterioscler. Thromb. Vasc. Biol. , vol.23 , Issue.2 , pp. 238-243
    • Leskinen, M.J.1    Lindstedt, K.A.2    Wang, Y.3    Kovanen, P.T.4
  • 52
    • 0027363385 scopus 로고
    • Peptidylproline cis-trans-isomerases: Immunophilins
    • Galat, A. Peptidylproline cis-trans-isomerases: immunophilins Eur. J. Biochem. 1993, 216 (3) 689-707
    • (1993) Eur. J. Biochem. , vol.216 , Issue.3 , pp. 689-707
    • Galat, A.1
  • 53
    • 22244464562 scopus 로고    scopus 로고
    • The cyclophilins
    • Wang, P.; Heitman, J. The cyclophilins Genome Biol. 2005, 6 (7) 226
    • (2005) Genome Biol. , vol.6 , Issue.7 , pp. 226
    • Wang, P.1    Heitman, J.2
  • 54
    • 0024959449 scopus 로고
    • Cyclophilin and peptidyl-prolyl cis-trans isomerase are probably identical proteins
    • Fischer, G.; Wittmann-Liebold, B.; Lang, K.; Kiefhaber, T.; Schmid, F. X. Cyclophilin and peptidyl-prolyl cis-trans isomerase are probably identical proteins Nature 1989, 337 (6206) 476-8
    • (1989) Nature , vol.337 , Issue.6206 , pp. 476-478
    • Fischer, G.1    Wittmann-Liebold, B.2    Lang, K.3    Kiefhaber, T.4    Schmid, F.X.5
  • 55
    • 0024959451 scopus 로고
    • Peptidyl-prolyl cis-trans isomerase is the cyclosporin A-binding protein cyclophilin
    • Takahashi, N.; Hayano, T.; Suzuki, M. Peptidyl-prolyl cis-trans isomerase is the cyclosporin A-binding protein cyclophilin Nature 1989, 337 (6206) 473-5
    • (1989) Nature , vol.337 , Issue.6206 , pp. 473-475
    • Takahashi, N.1    Hayano, T.2    Suzuki, M.3
  • 56
    • 0028227015 scopus 로고
    • Cyclophilin B trafficking through the secretory pathway is altered by binding of cyclosporin A
    • Price, E. R.; Jin, M.; Lim, D.; Pati, S.; Walsh, C. T.; McKeon, F. D. Cyclophilin B trafficking through the secretory pathway is altered by binding of cyclosporin A Proc. Natl. Acad. Sci. U.S.A. 1994, 91 (9) 3931-5
    • (1994) Proc. Natl. Acad. Sci. U.S.A. , vol.91 , Issue.9 , pp. 3931-3935
    • Price, E.R.1    Jin, M.2    Lim, D.3    Pati, S.4    Walsh, C.T.5    McKeon, F.D.6
  • 57
    • 0028336648 scopus 로고
    • Peptidyl prolyl cis-trans-isomerase activity associated with the lumen of the endoplasmic reticulum
    • Bose, S.; Freedman, R. B. Peptidyl prolyl cis-trans-isomerase activity associated with the lumen of the endoplasmic reticulum Biochem. J. 1994, 300 (Pt 3) 865-70 (Pubitemid 24180605)
    • (1994) Biochemical Journal , vol.300 , Issue.3 , pp. 865-870
    • Bose, S.1    Freedman, R.B.2
  • 58
    • 0026527418 scopus 로고
    • S-cyclophilin is retained intracellularly via a unique COOH-terminal sequence and colocalizes with the calcium storage protein calreticulin
    • Arber, S.; Krause, K. H.; Caroni, P. s-cyclophilin is retained intracellularly via a unique COOH-terminal sequence and colocalizes with the calcium storage protein calreticulin J. Cell Biol. 1992, 116 (1) 113-25
    • (1992) J. Cell Biol. , vol.116 , Issue.1 , pp. 113-125
    • Arber, S.1    Krause, K.H.2    Caroni, P.3
  • 59
    • 0029869725 scopus 로고    scopus 로고
    • Evidence that human milk isolated cyclophilin B corresponds to a truncated form
    • Mariller, C.; Allain, F.; Kouach, M.; Spik, G. Evidence that human milk isolated cyclophilin B corresponds to a truncated form Biochim. Biophys. Acta 1996, 1293 (1) 31-8
    • (1996) Biochim. Biophys. Acta , vol.1293 , Issue.1 , pp. 31-38
    • Mariller, C.1    Allain, F.2    Kouach, M.3    Spik, G.4
  • 60
    • 0030723208 scopus 로고    scopus 로고
    • A peptidyl-prolyl cis/trans-isomerase (cyclophilin G) in regulated secretory granules
    • Takaki, Y.; Muta, T.; Iwanaga, S. A peptidyl-prolyl cis/trans-isomerase (cyclophilin G) in regulated secretory granules J. Biol. Chem. 1997, 272 (45) 28615-21
    • (1997) J. Biol. Chem. , vol.272 , Issue.45 , pp. 28615-28621
    • Takaki, Y.1    Muta, T.2    Iwanaga, S.3
  • 61
    • 33644634632 scopus 로고    scopus 로고
    • Proteome analysis of glandular parotid and submandibular-sublingual saliva in comparison to whole human saliva by two-dimensional gel electrophoresis
    • Walz, A.; Stuhler, K.; Wattenberg, A.; Hawranke, E.; Meyer, H. E.; Schmalz, G.; Bluggel, M.; Ruhl, S. Proteome analysis of glandular parotid and submandibular-sublingual saliva in comparison to whole human saliva by two-dimensional gel electrophoresis Proteomics 2006, 6 (5) 1631-9
    • (2006) Proteomics , vol.6 , Issue.5 , pp. 1631-1639
    • Walz, A.1    Stuhler, K.2    Wattenberg, A.3    Hawranke, E.4    Meyer, H.E.5    Schmalz, G.6    Bluggel, M.7    Ruhl, S.8
  • 63
    • 0036644582 scopus 로고    scopus 로고
    • Cyclophilins: Unexpected messengers in intercellular communications
    • Bukrinsky, M. I. Cyclophilins: unexpected messengers in intercellular communications Trends Immunol. 2002, 23 (7) 323-5
    • (2002) Trends Immunol. , vol.23 , Issue.7 , pp. 323-325
    • Bukrinsky, M.I.1
  • 64
    • 0030972976 scopus 로고    scopus 로고
    • Native recombinant cyclophilins A, B, and C degrade DNA independently of peptidylprolyl cis-trans-isomerase activity. Potential roles of cyclophilins in apoptosis
    • Montague, J. W.; Hughes, F. M., Jr.; Cidlowski, J. A. Native recombinant cyclophilins A, B, and C degrade DNA independently of peptidylprolyl cis-trans-isomerase activity. Potential roles of cyclophilins in apoptosis J. Biol. Chem. 1997, 272 (10) 6677-84
    • (1997) J. Biol. Chem. , vol.272 , Issue.10 , pp. 6677-6684
    • Montague, J.W.1    Hughes Jr., F.M.2    Cidlowski, J.A.3
  • 65
    • 0028124715 scopus 로고
    • Calcium signalling in T cells stimulated by a cyclophilin B-binding protein
    • Bram, R. J.; Crabtree, G. R. Calcium signalling in T cells stimulated by a cyclophilin B-binding protein Nature 1994, 371 (6495) 355-8
    • (1994) Nature , vol.371 , Issue.6495 , pp. 355-358
    • Bram, R.J.1    Crabtree, G.R.2
  • 66
    • 0141707715 scopus 로고    scopus 로고
    • Peptidylprolyl cis/trans isomerases (immunophilins): Biological diversity - Targets - Functions
    • Galat, A. Peptidylprolyl cis/trans isomerases (immunophilins): biological diversity - targets - functions Curr. Top. Med. Chem. 2003, 3 (12) 1315-47
    • (2003) Curr. Top. Med. Chem. , vol.3 , Issue.12 , pp. 1315-1347
    • Galat, A.1
  • 67
    • 4143064622 scopus 로고    scopus 로고
    • The combinatorial extension method reveals a sphingolipid binding domain on pancreatic bile salt-dependent lipase: Role in secretion
    • Aubert-Jousset, E.; Garmy, N.; Sbarra, V.; Fantini, J.; Sadoulet, M. O.; Lombardo, D. The combinatorial extension method reveals a sphingolipid binding domain on pancreatic bile salt-dependent lipase: role in secretion Structure 2004, 12 (8) 1437-47
    • (2004) Structure , vol.12 , Issue.8 , pp. 1437-1447
    • Aubert-Jousset, E.1    Garmy, N.2    Sbarra, V.3    Fantini, J.4    Sadoulet, M.O.5    Lombardo, D.6
  • 68
    • 33744512465 scopus 로고    scopus 로고
    • Abnormal sterols in cholesterol-deficiency diseases cause secretory granule malformation and decreased membrane curvature
    • Gondre-Lewis, M. C.; Petrache, H. I.; Wassif, C. A.; Harries, D.; Parsegian, A.; Porter, F. D.; Loh, Y. P. Abnormal sterols in cholesterol-deficiency diseases cause secretory granule malformation and decreased membrane curvature J. Cell Sci. 2006, 119 (Pt 9) 1876-85
    • (2006) J. Cell Sci. , vol.119 , Issue.PART 9 , pp. 1876-1885
    • Gondre-Lewis, M.C.1    Petrache, H.I.2    Wassif, C.A.3    Harries, D.4    Parsegian, A.5    Porter, F.D.6    Loh, Y.P.7
  • 69
    • 0028044809 scopus 로고
    • Role of the GP2/THP family of GPI-anchored proteins in membrane trafficking during regulated exocrine secretion
    • Scheele, G. A.; Fukuoka, S.; Freedman, S. D. Role of the GP2/THP family of GPI-anchored proteins in membrane trafficking during regulated exocrine secretion Pancreas 1994, 9 (2) 139-49
    • (1994) Pancreas , vol.9 , Issue.2 , pp. 139-149
    • Scheele, G.A.1    Fukuoka, S.2    Freedman, S.D.3
  • 70
    • 0031669207 scopus 로고    scopus 로고
    • Ribonuclease-gold labels chondroitin sulphate in guinea pig basophil granules
    • Dvorak, A. M.; Morgan, E. S. Ribonuclease-gold labels chondroitin sulphate in guinea pig basophil granules Histochem. J. 1998, 30 (8) 603-8
    • (1998) Histochem. J. , vol.30 , Issue.8 , pp. 603-608
    • Dvorak, A.M.1    Morgan, E.S.2
  • 71
    • 0031775461 scopus 로고    scopus 로고
    • Ribonuclease-gold labels heparin in human mast cell granules. New use for an ultrastructural enzyme affinity technique
    • Dvorak, A. M.; Morgan, E. S. Ribonuclease-gold labels heparin in human mast cell granules. New use for an ultrastructural enzyme affinity technique J. Histochem. Cytochem. 1998, 46 (6) 695-706
    • (1998) J. Histochem. Cytochem. , vol.46 , Issue.6 , pp. 695-706
    • Dvorak, A.M.1    Morgan, E.S.2
  • 72
    • 0032773587 scopus 로고    scopus 로고
    • Ribonuclease-gold ultrastructural localization of heparin in isolated human lung mast cells stimulated to undergo anaphylactic degranulation and recovery in vitro
    • Dvorak, A. M.; Morgan, E. S. Ribonuclease-gold ultrastructural localization of heparin in isolated human lung mast cells stimulated to undergo anaphylactic degranulation and recovery in vitro Clin.. Exp. Allergy 1999, 29 (8) 1118-28
    • (1999) Clin. Exp. Allergy , vol.29 , Issue.8 , pp. 1118-1128
    • Dvorak, A.M.1    Morgan, E.S.2
  • 73
    • 0032924187 scopus 로고    scopus 로고
    • Ribonuclease-gold labels proteoglycan-containing cytoplasmic granules and ribonucleic acid-containing organelles - A survey
    • Dvorak, A. M.; Morgan, E. S. Ribonuclease-gold labels proteoglycan-containing cytoplasmic granules and ribonucleic acid-containing organelles - a survey Histol. Histopathol. 1999, 14 (2) 597-626
    • (1999) Histol. Histopathol. , vol.14 , Issue.2 , pp. 597-626
    • Dvorak, A.M.1    Morgan, E.S.2
  • 74
    • 4544384802 scopus 로고    scopus 로고
    • Octasaccharide is the minimal length unit required for efficient binding of cyclophilin B to heparin and cell surface heparan sulphate
    • Vanpouille, C.; Denys, A.; Carpentier, M.; Pakula, R.; Mazurier, J.; Allain, F. Octasaccharide is the minimal length unit required for efficient binding of cyclophilin B to heparin and cell surface heparan sulphate Biochem. J. 2004, 382 (Pt 2) 733-40
    • (2004) Biochem. J. , vol.382 , Issue.PART 2 , pp. 733-740
    • Vanpouille, C.1    Denys, A.2    Carpentier, M.3    Pakula, R.4    Mazurier, J.5    Allain, F.6
  • 76
    • 0037022615 scopus 로고    scopus 로고
    • Interaction with glycosaminoglycans is required for cyclophilin B to trigger integrin-mediated adhesion of peripheral blood T lymphocytes to extracellular matrix
    • Allain, F.; Vanpouille, C.; Carpentier, M.; Slomianny, M. C.; Durieux, S.; Spik, G. Interaction with glycosaminoglycans is required for cyclophilin B to trigger integrin-mediated adhesion of peripheral blood T lymphocytes to extracellular matrix Proc. Natl. Acad. Sci. U.S.A. 2002, 99 (5) 2714-9
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , Issue.5 , pp. 2714-2719
    • Allain, F.1    Vanpouille, C.2    Carpentier, M.3    Slomianny, M.C.4    Durieux, S.5    Spik, G.6
  • 77
    • 0031755878 scopus 로고    scopus 로고
    • Intracellular transport and secretion of salivary proteins
    • Castle, D.; Castle, A. Intracellular transport and secretion of salivary proteins Crit. Rev. Oral Biol. Med. 1998, 9 (1) 4-22
    • (1998) Crit. Rev. Oral Biol. Med. , vol.9 , Issue.1 , pp. 4-22
    • Castle, D.1    Castle, A.2
  • 78
    • 0026594956 scopus 로고
    • Regulated and constitutive secretion. Differential effects of protein synthesis arrest on transport of glycosaminoglycan chains to the two secretory pathways
    • Brion, C.; Miller, S. G.; Moore, H. P. Regulated and constitutive secretion. Differential effects of protein synthesis arrest on transport of glycosaminoglycan chains to the two secretory pathways J. Biol. Chem. 1992, 267 (3) 1477-83
    • (1992) J. Biol. Chem. , vol.267 , Issue.3 , pp. 1477-1483
    • Brion, C.1    Miller, S.G.2    Moore, H.P.3
  • 79
    • 0026525382 scopus 로고
    • Intermediates in the constitutive and regulated secretory pathways released in vitro from semi-intact cells
    • Grimes, M.; Kelly, R. B. Intermediates in the constitutive and regulated secretory pathways released in vitro from semi-intact cells J. Cell Biol. 1992, 117 (3) 539-49
    • (1992) J. Cell Biol. , vol.117 , Issue.3 , pp. 539-549
    • Grimes, M.1    Kelly, R.B.2
  • 80
    • 0031807967 scopus 로고    scopus 로고
    • Regulation and function of mast cell proteases in inflammation
    • Huang, C.; Sali, A.; Stevens, R. L. Regulation and function of mast cell proteases in inflammation J. Clin. Immunol. 1998, 18 (3) 169-83
    • (1998) J. Clin. Immunol. , vol.18 , Issue.3 , pp. 169-183
    • Huang, C.1    Sali, A.2    Stevens, R.L.3
  • 81
    • 0039649450 scopus 로고    scopus 로고
    • Secretory granule proteases in rat mast cells. Cloning of 10 different serine proteases and a carboxypeptidase A from various rat mast cell populations
    • Lutzelschwab, C.; Pejler, G.; Aveskogh, M.; Hellman, L. Secretory granule proteases in rat mast cells. Cloning of 10 different serine proteases and a carboxypeptidase A from various rat mast cell populations J. Exp. Med. 1997, 185 (1) 13-29
    • (1997) J. Exp. Med. , vol.185 , Issue.1 , pp. 13-29
    • Lutzelschwab, C.1    Pejler, G.2    Aveskogh, M.3    Hellman, L.4
  • 82
    • 0029094503 scopus 로고
    • Packaging of proteases and proteoglycans in the granules of mast cells and other hematopoietic cells. A cluster of histidines on mouse mast cell protease 7 regulates its binding to heparin serglycin proteoglycans
    • Matsumoto, R.; Sali, A.; Ghildyal, N.; Karplus, M.; Stevens, R. L. Packaging of proteases and proteoglycans in the granules of mast cells and other hematopoietic cells. A cluster of histidines on mouse mast cell protease 7 regulates its binding to heparin serglycin proteoglycans J. Biol. Chem. 1995, 270 (33) 19524-31
    • (1995) J. Biol. Chem. , vol.270 , Issue.33 , pp. 19524-19531
    • Matsumoto, R.1    Sali, A.2    Ghildyal, N.3    Karplus, M.4    Stevens, R.L.5
  • 83
    • 67349207410 scopus 로고    scopus 로고
    • Serglycin proteoglycan is not implicated in localizing exocrine pancreas enzymes to zymogen granules
    • Niemann, C. U.; Cowland, J. B.; Ralfkiaer, E.; Abrink, M.; Pejler, G.; Borregaard, N. Serglycin proteoglycan is not implicated in localizing exocrine pancreas enzymes to zymogen granules Eur. J. Cell Biol. 2009, 88 (8) 473-9
    • (2009) Eur. J. Cell Biol. , vol.88 , Issue.8 , pp. 473-479
    • Niemann, C.U.1    Cowland, J.B.2    Ralfkiaer, E.3    Abrink, M.4    Pejler, G.5    Borregaard, N.6


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