메뉴 건너뛰기




Volumn 111, Issue 17, 1998, Pages 2665-2679

Participation of GRP94-related protein in secretion of pancreatic bile salt-dependent lipase and in its internalization by the intestinal epithelium

Author keywords

Glucose regulated protein 94; Immunocytochemistry; Pancreatic bile salt dependent lipase

Indexed keywords

MESSENGER RNA; PANCREAS ENZYME; TRIACYLGLYCEROL LIPASE;

EID: 0031696368     PISSN: 00219533     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (54)

References (49)
  • 1
    • 0023803362 scopus 로고
    • Purification of pancreatic carboxylic-ester hydrolase by immunoaffinity and its application to the human bile-salt-stimulated lipase
    • Abouakil, N., Rogalska, E., Bonicel, J. and Lomhardo, D. (1988). Purification of pancreatic carboxylic-ester hydrolase by immunoaffinity and its application to the human bile-salt-stimulated lipase. Biochim. Biophys. Acta. 961, 299-308.
    • (1988) Biochim. Biophys. Acta. , vol.961 , pp. 299-308
    • Abouakil, N.1    Rogalska, E.2    Bonicel, J.3    Lomhardo, D.4
  • 2
    • 0027425512 scopus 로고
    • Bile salt-dependent lipase biosynthesis in rat pancreatic AR 4-2J cells: Essential requirement of linked oligosaccharide for secretion and expression of a fully active enzyme
    • Abouakil, N., Mas, E, Bruneau, N., Benajiba, A. and Lomburdo, D. (1993). Bile salt-dependent lipase biosynthesis in rat pancreatic AR 4-2J cells: essential requirement of linked oligosaccharide for secretion and expression of a fully active enzyme. J. Biol. Chem. 268, 25755-25763.
    • (1993) J. Biol. Chem. , vol.268 , pp. 25755-25763
    • Abouakil, N.1    Mas, E.2    Bruneau, N.3    Benajiba, A.4    Lomburdo, D.5
  • 3
    • 0028869404 scopus 로고
    • Colloidal gold post-embedding immunocytochemistry
    • Bendayan, M. (1995). Colloidal gold post-embedding immunocytochemistry. Prog. Histochem, Cytochem. 29, 1-163.
    • (1995) Prog. Histochem, Cytochem. , vol.29 , pp. 1-163
    • Bendayan, M.1
  • 4
    • 0018835510 scopus 로고
    • Quantitative immunocytochimical localization of pancreatic secretory proteins in subcellular compartments of the rat acinar cell
    • Bendayan, M., Ruth, J., Perrelet, A. and Orci, L. (1980). Quantitative immunocytochimical localization of pancreatic secretory proteins in subcellular compartments of the rat acinar cell. J. Histochem. Cytochem. 28, 149-160.
    • (1980) J. Histochem. Cytochem. , vol.28 , pp. 149-160
    • Bendayan, M.1    Ruth, J.2    Perrelet, A.3    Orci, L.4
  • 6
    • 0024346868 scopus 로고
    • Heparin-modulated binding of pancreatic lipase and uptake of nydrolysed triglycerides in the intestine
    • Bosner, M. S., Gulick, T., Riley, D. J. S., Spilburg, C. A. and Lange, L. G. (1989). Heparin-modulated binding of pancreatic lipase and uptake of nydrolysed triglycerides in the intestine. J. Biol. Chem. 264, 20261-20264.
    • (1989) J. Biol. Chem. , vol.264 , pp. 20261-20264
    • Bosner, M.S.1    Gulick, T.2    Riley, D.J.S.3    Spilburg, C.A.4    Lange, L.G.5
  • 7
    • 0029025326 scopus 로고
    • Chaperon function of a Grp 94-related protein for folding and transport of the pancreatic bile salt-dependent lipase
    • Bruneau, N. and Lombarde, D. (1995). Chaperon function of a Grp 94-related protein for folding and transport of the pancreatic bile salt-dependent lipase. J. Biol. Chem. 270, 13524-13533.
    • (1995) J. Biol. Chem. , vol.270 , pp. 13524-13533
    • Bruneau, N.1    Lombarde, D.2
  • 8
    • 0028825918 scopus 로고
    • Association of bile salt-dependent lipase to membrane of human pancreatic microsomes
    • Bruneau, N., Lechene de la Porte, P., Sharra, V. and Lombardo, D. (1995). Association of bile salt-dependent lipase to membrane of human pancreatic microsomes. Eur. J. Biochem. 233, 209-218.
    • (1995) Eur. J. Biochem. , vol.233 , pp. 209-218
    • Bruneau, N.1    Lechene de la Porte, P.2    Sharra, V.3    Lombardo, D.4
  • 9
    • 0030833432 scopus 로고    scopus 로고
    • O-Glycosylation of C-terminal tandem repeated sequences regulates the secretion of rat pancreatic bile salt-dependent lipase
    • Bruneau, N., Nganga, A., Fisher, E. and Lombardo, D. (1997). O-Glycosylation of C-terminal tandem repeated sequences regulates the secretion of rat pancreatic bile salt-dependent lipase. J. Biol. Chem. 272, 27353-27361.
    • (1997) J. Biol. Chem. , vol.272 , pp. 27353-27361
    • Bruneau, N.1    Nganga, A.2    Fisher, E.3    Lombardo, D.4
  • 10
    • 0019551730 scopus 로고
    • 'Western Blotting': Electrophoretic transfer of proteins from sodium dodecyl sulfate-polyacrylamide gels to unmodified nitrocellulose an radiographic detection with antibody and radiodinated protein A
    • Burnette, W. N. (1981). 'Western Blotting': Electrophoretic transfer of proteins from sodium dodecyl sulfate-polyacrylamide gels to unmodified nitrocellulose an radiographic detection with antibody and radiodinated protein A. Anal. Biochem. 112, 195-203.
    • (1981) Anal. Biochem. , vol.112 , pp. 195-203
    • Burnette, W.N.1
  • 11
    • 0021211108 scopus 로고
    • Cholesterol absorption in rat intestine: Role of cholesterol esterase and acylcoenzyme A: cholesterol acyltransferase
    • Gallo, L. L. S., Bennett-Clark, S., Myers, S. and Vahouny, G. V. (1984). Cholesterol absorption in rat intestine: role of cholesterol esterase and acylcoenzyme A: cholesterol acyltransferase. J. Lipid Res. 25, 604-612.
    • (1984) J. Lipid Res. , vol.25 , pp. 604-612
    • Gallo, L.L.S.1    Bennett-Clark, S.2    Myers, S.3    Vahouny, G.V.4
  • 12
    • 0003350272 scopus 로고
    • Colloidal gold electron microscopic in situ hybridation: Combination with immunocytochemistry for the study of insulin and amylase secretion
    • Gingras, D. and Bendayan, M. (1995). Colloidal gold electron microscopic in situ hybridation: combination with immunocytochemistry for the study of insulin and amylase secretion. Cell vision 2, 218-224.
    • (1995) Cell Vision , vol.2 , pp. 218-224
    • Gingras, D.1    Bendayan, M.2
  • 13
    • 0023132250 scopus 로고
    • Isolation of full-length putative rat lysophospholipase cDNA using improved methods for mRNA isolation and cDNA cloning
    • Man, J. H., Stratowa, C. and Rutter, W. J. (1987). Isolation of full-length putative rat lysophospholipase cDNA using improved methods for mRNA isolation and cDNA cloning. Biochemistry 26, 1617-1625.
    • (1987) Biochemistry , vol.26 , pp. 1617-1625
    • Man, J.H.1    Stratowa, C.2    Rutter, W.J.3
  • 15
    • 0028205168 scopus 로고
    • Hormonal regulation of protein disulfide isomerase and chaperone synthesis in the rat exocrine pancreas
    • Hensel, G., Aßmann, and Kern, H. F. (1994). Hormonal regulation of protein disulfide isomerase and chaperone synthesis in the rat exocrine pancreas. Eur. J. Cell Biol. 63, 208-218.
    • (1994) Eur. J. Cell Biol. , vol.63 , pp. 208-218
    • Hensel, G.1    Aßmann, A.2    Kern, H.F.3
  • 16
    • 0027943119 scopus 로고
    • Human milk bile salt-stimulated lipase: Functional and molecular aspects
    • Hernell, O. and Blackberg, L. (1994). Human milk bile salt-stimulated lipase: Functional and molecular aspects. J. Pediatrics 125, S56-S61
    • (1994) J. Pediatrics , vol.125
    • Hernell, O.1    Blackberg, L.2
  • 17
    • 0030870534 scopus 로고    scopus 로고
    • Survival of human pancreatic enzymes during small bowel transit: Effect of nutrients, bile acids, and enzymes
    • Holtmann, G., Kelly, D. G., Sternby, B. and Dimagno, E. (1997). Survival of human pancreatic enzymes during small bowel transit: effect of nutrients, bile acids, and enzymes. Am. J. Physiol. 273, G553-G558.
    • (1997) Am. J. Physiol. , vol.273
    • Holtmann, G.1    Kelly, D.G.2    Sternby, B.3    Dimagno, E.4
  • 18
    • 0029989318 scopus 로고    scopus 로고
    • Dietary free and esterified cholesterol absorption in cholesterol esterase (bile salt-stimulated lipase) gene targeted mice
    • Howles, P., Carter, C. and Hui, D. Y. (1996). Dietary free and esterified cholesterol absorption in cholesterol esterase (bile salt-stimulated lipase) gene targeted mice. J. Biol. Chem. 271, 7196-7202
    • (1996) J. Biol. Chem. , vol.271 , pp. 7196-7202
    • Howles, P.1    Carter, C.2    Hui, D.Y.3
  • 19
    • 0025642582 scopus 로고
    • Metabolic fate of pancreas derived cholesterol esterase in intestine: An in vitro study using Caco-2 cells
    • Huang, Y. and Hui, D. Y. (1990). Metabolic fate of pancreas derived cholesterol esterase in intestine: an in vitro study using Caco-2 cells. J. Lipid. Res. 31, 2029-2037.
    • (1990) J. Lipid. Res. , vol.31 , pp. 2029-2037
    • Huang, Y.1    Hui, D.Y.2
  • 20
    • 0024306906 scopus 로고
    • Molecular cloning and expression of cDNA for rat pancreatic cholesterol esterase
    • Kissel, J. A., Fontaine, R. N., Turck, C. W., Brockman, H. L. and Hui, D. Y. (1989). Molecular cloning and expression of cDNA for rat pancreatic cholesterol esterase. Biochim. Biophys. Acta 1006, 227-236.
    • (1989) Biochim. Biophys. Acta , vol.1006 , pp. 227-236
    • Kissel, J.A.1    Fontaine, R.N.2    Turck, C.W.3    Brockman, H.L.4    Hui, D.Y.5
  • 22
    • 0027936075 scopus 로고
    • Several endophismic reticululm stress proteins, including Erp72, interact with ihsroglobulin during its maturatoin
    • Kuznetsov, G., Chen, L. B. and Niyam, S. K. (1994). Several endophismic reticululm stress proteins, including Erp72, interact with ihsroglobulin during its maturatoin. J. Biol. Chem. 267, 22990-22995.
    • (1994) J. Biol. Chem. , vol.267 , pp. 22990-22995
    • Kuznetsov, G.1    Chen, L.B.2    Niyam, S.K.3
  • 23
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 26
    • 0029955716 scopus 로고    scopus 로고
    • Possible association of chaperonin 60 with secretory, proteins in pancreatic acinar cells
    • Le-Gall, I. and Bendayan, M. (1996). Possible association of chaperonin 60 with secretory, proteins in pancreatic acinar cells. J. Histochem. Cytochem. 44, 743-749.
    • (1996) J. Histochem. Cytochem. , vol.44 , pp. 743-749
    • Le-Gall, I.1    Bendayan, M.2
  • 28
    • 0029078946 scopus 로고
    • Structural organization of human bile-salt-activated lipase probed by limited proteolysis and expression of a recombinant truncated variant
    • Loomes, K. M. (1995). Structural organization of human bile-salt-activated lipase probed by limited proteolysis and expression of a recombinant truncated variant. Eur. J. Biochem. 230, 607-613.
    • (1995) Eur. J. Biochem. , vol.230 , pp. 607-613
    • Loomes, K.M.1
  • 29
    • 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
    • Lombarde, D., Fauvel, J. and Guy, O. (1980). 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 611, 136-146.
    • (1980) Biochim. Biophys. Acta , vol.611 , pp. 136-146
    • Lombarde, D.1    Fauvel, J.2    Guy, O.3
  • 30
    • 0018842463 scopus 로고
    • Studies on the substrate specificity of a carboxyl ester hydrolase from human pancreatic juice. II. Action on cholesterol esters and lipid-soluble vitamin esters
    • Lombardo, D. and Guy, O. (1980). Studies on the substrate specificity of a carboxyl ester hydrolase from human pancreatic juice. II. Action on cholesterol esters and lipid-soluble vitamin esters. Biochim. Biophys. Acta 611, 147-155.
    • (1980) Biochim. Biophys. Acta , vol.611 , pp. 147-155
    • Lombardo, D.1    Guy, O.2
  • 31
    • 0027434874 scopus 로고
    • Cholesterol transport function of pancreatic cholesterol esterase: Directed sterol uptake and esterification in enterocytes
    • Lopez-Candales, A., Bosner, M. S., Spilburg, C. A. and Lange, L. G. (1993). Cholesterol transport function of pancreatic cholesterol esterase: directed sterol uptake and esterification in enterocytes. Biochemistry 32, 12085-12089
    • (1993) Biochemistry , vol.32 , pp. 12085-12089
    • Lopez-Candales, A.1    Bosner, M.S.2    Spilburg, C.A.3    Lange, L.G.4
  • 32
    • 0030949925 scopus 로고    scopus 로고
    • Phosphatidylcholine hydrolysis is required for pancreatic cholesterol esterase and phospholipase A: Facilitated cholesterol uptake into intestinal Caco-2 cells
    • Mackay, K., Starr, J. R., Lawn, R. M. and Ellsworth, J. L. (1997). Phosphatidylcholine hydrolysis is required for pancreatic cholesterol esterase and phospholipase A: facilitated cholesterol uptake into intestinal Caco-2 cells. J. Biol. Own. 272, 13380-13389.
    • (1997) J. Biol. Own. , vol.272 , pp. 13380-13389
    • Mackay, K.1    Starr, J.R.2    Lawn, R.M.3    Ellsworth, J.L.4
  • 33
    • 0030714076 scopus 로고    scopus 로고
    • Biotinyl-tyramide: A novel approach for electron microscopic immunocytochemisiry
    • Mayer, G. and Bendayan, M. (1997). Biotinyl-tyramide: a novel approach for electron microscopic immunocytochemisiry. J. Histochem. Cytochem. 45, 1449-1454.
    • (1997) J. Histochem. Cytochem. , vol.45 , pp. 1449-1454
    • Mayer, G.1    Bendayan, M.2
  • 34
    • 0023664518 scopus 로고
    • ERP99. an abundant, conserved glycoprotein of the endoplasmic reticulum, is homologous to the 90 kDa heat shock protein (hsp90) and the 94 kDa glucose regulated protein (Grp94)
    • Mazzerella, R. A. and Green, M. (1987). ERP99. an abundant, conserved glycoprotein of the endoplasmic reticulum, is homologous to the 90 kDa heat shock protein (hsp90) and the 94 kDa glucose regulated protein (Grp94). J. Biol. Chem. 262, 8875-8883.
    • (1987) J. Biol. Chem. , vol.262 , pp. 8875-8883
    • Mazzerella, R.A.1    Green, M.2
  • 35
    • 0028170231 scopus 로고
    • Sequential interation of the chaperones BiP and Grp94 with immunoglobulin chains in the endoplasmic reticulum
    • Melnick, J., Dui, J. L. and Argon, Y. (1994). Sequential interation of the chaperones BiP and Grp94 with immunoglobulin chains in the endoplasmic reticulum. Nature 370, 373-375.
    • (1994) Nature , vol.370 , pp. 373-375
    • Melnick, J.1    Dui, J.L.2    Argon, Y.3
  • 36
    • 0026808864 scopus 로고
    • The endoplasmic reticulum stress protein Grp94 in addition to BiP, associates with unassembled immunoglobulin chains
    • Melnick, J., Ariel, S. and Argon, Y. (1992). The endoplasmic reticulum stress protein Grp94 in addition to BiP, associates with unassembled immunoglobulin chains. J. Biol. Chem. 267, 21303-21306.
    • (1992) J. Biol. Chem. , vol.267 , pp. 21303-21306
    • Melnick, J.1    Ariel, S.2    Argon, Y.3
  • 38
    • 0028964421 scopus 로고
    • Calreticulin function as a molecular chaperone in the biosynthesis of myeloperoxidase
    • Nauseef, W. N., McCormick, S. J. and Clark, R. A. (1995). Calreticulin function as a molecular chaperone in the biosynthesis of myeloperoxidase. J. Biol. Chem. 270, 4741-4747.
    • (1995) J. Biol. Chem. , vol.270 , pp. 4741-4747
    • Nauseef, W.N.1    McCormick, S.J.2    Clark, R.A.3
  • 39
    • 0032007324 scopus 로고    scopus 로고
    • Biochemical, cell biological and immunological issues surrounding the endoplasmic reticulum chaperone Grp94 / gp96
    • Nicchitta, C. V. (1998). Biochemical, cell biological and immunological issues surrounding the endoplasmic reticulum chaperone Grp94 / gp96. Curr. Opin. Immnnol. 10, 103-109
    • (1998) Curr. Opin. Immnnol. , vol.10 , pp. 103-109
    • Nicchitta, C.V.1
  • 40
    • 0016785996 scopus 로고
    • Intracellular aspects of the process of protein secretion
    • Palade G. E. (1975). Intracellular aspects of the process of protein secretion. Science. 189, 347-358.
    • (1975) Science , vol.189 , pp. 347-358
    • Palade, G.E.1
  • 42
    • 0022971952 scopus 로고
    • Amino acid sequences common to rapidly degraded proteins: The PEST hypothesis
    • Rogers, S., Wells, R. and Rechsteiner, M. (1986). Amino acid sequences common to rapidly degraded proteins: the PEST hypothesis. Science 234, 364-369.
    • (1986) Science , vol.234 , pp. 364-369
    • Rogers, S.1    Wells, R.2    Rechsteiner, M.3
  • 43
    • 0032584533 scopus 로고    scopus 로고
    • Molecular cloning of the bile salt-dependent lipase of ferret lactaiing mammary gland: An overview of functional residues
    • in press
    • Sbarra, V., Bruneau, N., Mas, E., Hamosh, M., Lombardo, D. and Hamosh, P. (1998). Molecular cloning of the bile salt-dependent lipase of ferret lactaiing mammary gland: an overview of functional residues. Biochim. Biophys. Acta (in press).
    • (1998) Biochim. Biophys. Acta
    • Sbarra, V.1    Bruneau, N.2    Mas, E.3    Hamosh, M.4    Lombardo, D.5    Hamosh, P.6
  • 44
    • 0029066878 scopus 로고
    • The role of bile salt-dependent cholesteryl ester hydrolase in the uptake micellar cholesterol by intestinal cells
    • Shamir, R., Johnson, W. J., Zolfaghari, R., Lee, H. S. and Fisher, F. A. (1995). The role of bile salt-dependent cholesteryl ester hydrolase in the uptake micellar cholesterol by intestinal cells. Biochemistry 34, 6351-6358.
    • (1995) Biochemistry , vol.34 , pp. 6351-6358
    • Shamir, R.1    Johnson, W.J.2    Zolfaghari, R.3    Lee, H.S.4    Fisher, F.A.5
  • 45
    • 0023660117 scopus 로고
    • The glucose regulated protein Grp94 is related to heal shock protein Hsp90
    • Sorger, P. K. and Pelham, H. R. B. (1987). The glucose regulated protein Grp94 is related to heal shock protein Hsp90. J. Mol. Biol. 194, 341-344.
    • (1987) J. Mol. Biol. , vol.194 , pp. 341-344
    • Sorger, P.K.1    Pelham, H.R.B.2
  • 46
    • 0026689538 scopus 로고
    • Heavy chain binding protein and endoplasmin are exported from the endoplasmic reticulum in rat exocrine pancreatic cells similar to protein disulfide-isomerase
    • Takemoto, H., Voshimoro, T., Yamamoto, A., Mlyutu, Y., Yahara, I., Inouo, K. and Tashiro, Y. (1992). Heavy chain binding protein and endoplasmin are exported from the endoplasmic reticulum in rat exocrine pancreatic cells similar to protein disulfide-isomerase. Arch. Biochem. Biophys. 296, 129-136.
    • (1992) Arch. Biochem. Biophys. , vol.296 , pp. 129-136
    • Takemoto, H.1    Voshimoro, T.2    Yamamoto, A.3    Mlyutu, Y.4    Yahara, I.5    Inouo, K.6    Tashiro, Y.7
  • 47
    • 0028345717 scopus 로고
    • Molecular chaperones in pancreatic tissue: The presence of epn10, cpn60 und tap70 in distinct compartments along the secretory pathway of the acinar cells
    • Vélez-Granell, C. S., Arias, A. E., Torres-Ruiz, J. A. and Bendayun, M. (1994). Molecular chaperones in pancreatic tissue: the presence of epn10, cpn60 und tap70 in distinct compartments along the secretory pathway of the acinar cells. J. Cell Sci. 107, 539-549.
    • (1994) J. Cell Sci. , vol.107 , pp. 539-549
    • Vélez-Granell, C.S.1    Arias, A.E.2    Torres-Ruiz, J.A.3    Bendayun, M.4
  • 48
    • 0027467140 scopus 로고
    • Bile suit-activated lipuse. A multiple function lipolytie enzyme
    • Wang, C. S. and Hartsuck, J. A. (1993). Bile suit-activated lipuse. A multiple function lipolytie enzyme. Biochim. Biophys. Acta. 1166, 1-19.
    • (1993) Biochim. Biophys. Acta. , vol.1166 , pp. 1-19
    • Wang, C.S.1    Hartsuck, J.A.2
  • 49
    • 0030087534 scopus 로고    scopus 로고
    • Puritication and partial molecular characterization of Grp94, an ER resident chaperone
    • Wearsch, P. A. and Nicchitta, C. V. (1996). Puritication and partial molecular characterization of Grp94, an ER resident chaperone. Protein Expression Purification 7, 114-121.
    • (1996) Protein Expression Purification , vol.7 , pp. 114-121
    • Wearsch, P.A.1    Nicchitta, C.V.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.