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Volumn 44, Issue 1, 1996, Pages 57-66

Expression of sulfated gp300 and changes in glycosylation during pancreatic development

Author keywords

Development; Glycoprotein; Lectin; Mouse; Sulfation; Western blot

Indexed keywords

GALAPTIN; GLYCOPROTEIN; PANCREAS ENZYME; PEANUT AGGLUTININ; SIALIC ACID; ULEX EUROPAEUS AGGLUTININ; ZYMOGEN GRANULE;

EID: 0030048295     PISSN: 00221554     EISSN: None     Source Type: Journal    
DOI: 10.1177/44.1.8543783     Document Type: Article
Times cited : (4)

References (28)
  • 1
    • 0015110201 scopus 로고
    • Sulfate metabolism m pancreatic acinar cells
    • Berg NB, Young RW: Sulfate metabolism m pancreatic acinar cells. J Cell Biol 50:469, 1971
    • (1971) J Cell Biol , vol.50 , pp. 469
    • Berg, N.B.1    Young, R.W.2
  • 2
    • 0026354164 scopus 로고
    • Proteoglycan sulfation and storage parallels storage of basic secretory proteins in exocrine cells
    • Blair EA, Castle AM, Castle JD: Proteoglycan sulfation and storage parallels storage of basic secretory proteins in exocrine cells. Am J Physiol 261:C897, 1991
    • (1991) Am J Physiol , vol.261
    • Blair, E.A.1    Castle, A.M.2    Castle, J.D.3
  • 3
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM: A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72:248, 1976
    • (1976) Anal Biochem , vol.72 , pp. 248
    • Bradford, M.M.1
  • 5
    • 0025100834 scopus 로고
    • Glycosylation of lactase-phlorizin hydrolase in rat small intestine during development
    • Bullet HA, Rings HHM, Pajkrt D, Montgomery RK, Grand RJ: Glycosylation of lactase-phlorizin hydrolase in rat small intestine during development. Gastroenterology 98:667, 1990
    • (1990) Gastroenterology , vol.98 , pp. 667
    • Bullet, H.A.1    Hhm, R.2    Pajkrt, D.3    Montgomery, R.K.4    Grand, R.J.5
  • 6
    • 0015793092 scopus 로고
    • Galactosyltransferase activities in pancreas, liver and gut of the developing rat
    • Carlson DM, David J, Rutter WJ: Galactosyltransferase activities in pancreas, liver and gut of the developing rat. Arch Biochem Biophys 157:605, 1973
    • (1973) Arch Biochem Biophys , vol.157 , pp. 605
    • Carlson, D.M.1    David, J.2    Rutter, W.J.3
  • 7
    • 0028929793 scopus 로고
    • Increased expression of sulfated gp300 and acinar tissue pathology in pancreas of CFTR (-/-) mice
    • De Lisle RC: Increased expression of sulfated gp300 and acinar tissue pathology in pancreas of CFTR (-/-) mice. Am J Physiol 268:G717, 1995
    • (1995) Am J Physiol , vol.268
    • De Lisle, R.C.1
  • 8
    • 0028130410 scopus 로고
    • Characterization of the major sulfated protein of mouse pancreatic acinar cells, a high molecular weight peripheral membrane glycoprotein of zymogen granules
    • De Lisle RC Characterization of the major sulfated protein of mouse pancreatic acinar cells, a high molecular weight peripheral membrane glycoprotein of zymogen granules. J Cell Biochem 56:385, 1994
    • (1994) J Cell Biochem , vol.56 , pp. 385
    • De Lisle, R.C.1
  • 9
    • 0026709706 scopus 로고
    • The major zymogen granule membrane protein GP-2 in the rat pancreas is not involved in granule formation
    • Dittié A, Kern HF: The major zymogen granule membrane protein GP-2 in the rat pancreas is not involved in granule formation. Eur J Cell Biol 58:243, 1992
    • (1992) Eur J Cell Biol , vol.58 , pp. 243
    • Dittié, A.1    Kern, H.F.2
  • 10
    • 0021051920 scopus 로고
    • Increase in zymogen granule volume accounts for increase in volume density during prenatal development of pancreas
    • Ennak TH, Rothman SS: Increase in zymogen granule volume accounts for increase in volume density during prenatal development of pancreas. Anat Rec 207:487, 1983
    • (1983) Anat Rec , vol.207 , pp. 487
    • Ennak, T.H.1    Rothman, S.S.2
  • 11
    • 0028305619 scopus 로고
    • Lectins are sensitive tools for defining the differentiation programs of mouse gut epithelial cell lineages
    • Falk P, Roth KA, Gordon JI: Lectins are sensitive tools for defining the differentiation programs of mouse gut epithelial cell lineages. Am J Physiol 266:G987, 1994
    • (1994) Am J Physiol , vol.266
    • Falk, P.1    Roth, K.A.2    Gordon, J.I.3
  • 12
    • 0027376899 scopus 로고
    • Reversible pH-induced homophilic binding of GP2, a glycosyl-phosphatidylinositol-anchored protein in pancreatic zymogen granule membranes
    • Freedman SD, Scheele GA: Reversible pH-induced homophilic binding of GP2, a glycosyl-phosphatidylinositol-anchored protein in pancreatic zymogen granule membranes. Eur J Cell Biol 61:229, 1993
    • (1993) Eur J Cell Biol , vol.61 , pp. 229
    • Freedman, S.D.1    Scheele, G.A.2
  • 13
    • 0017832443 scopus 로고
    • The lectins: Carbohydrate-binding proteins of plants and animals
    • Tipson RS, Horton D, eds. New York, Academic Press
    • Goldstein IJ, Hayes CE: The lectins: carbohydrate-binding proteins of plants and animals. In Tipson RS, Horton D, eds. Advances in carbohydrate chemistry and biochemistry New York, Academic Press, 1978, 127
    • (1978) Advances in Carbohydrate Chemistry and Biochemistry , pp. 127
    • Goldstein, I.J.1    Hayes, C.E.2
  • 14
    • 0025900044 scopus 로고
    • Biosynthetic maturation of an ascites tumor cell surface sialomucin
    • Hull SR, Sugarman ED, Spielman J, Cartaway KL: Biosynthetic maturation of an ascites tumor cell surface sialomucin. J Biol Chem 266:13580, 1991
    • (1991) J Biol Chem , vol.266 , pp. 13580
    • Hull, S.R.1    Sugarman, E.D.2    Spielman, J.3    Cartaway, K.L.4
  • 15
    • 0018864097 scopus 로고
    • Preparation and application of procion yellow starch for amylase assay
    • Jung DH: Preparation and application of procion yellow starch for amylase assay. Clin Chim Acta 100:7, 1980
    • (1980) Clin Chim Acta , vol.100 , pp. 7
    • Jung, D.H.1
  • 16
    • 0024473572 scopus 로고
    • Topographical and planar distribution of Helix pomatia lectin-binding glycoconjugates in secretory granules and plasma membrane of pancreatic exocrine acinar cells of the rat: Demonstration of membrane heterogeneity
    • Kan FWK, Bendayan M: Topographical and planar distribution of Helix pomatia lectin-binding glycoconjugates in secretory granules and plasma membrane of pancreatic exocrine acinar cells of the rat: demonstration of membrane heterogeneity. Am J Anat 185:165, 1989
    • (1989) Am J Anat , vol.185 , pp. 165
    • Kan, F.W.K.1    Bendayan, M.2
  • 17
    • 0025875756 scopus 로고
    • Proteoglycans: Structures and interactions
    • Kjellén L, Lindahl U: Proteoglycans: structures and interactions. Annu Rev Biochem 60:443, 1991
    • (1991) Annu Rev Biochem , vol.60 , pp. 443
    • Kjellén, L.1    Lindahl, U.2
  • 18
    • 0023770955 scopus 로고
    • Remodeling of a rat hepatocyte plasma membrane glycoprotein. De- and reglycosylation of dipeptidyl peptidase IV
    • Kreisel W, Hanski C, Tran-Thi T-A, Katz N, Decker K, Reutter W, Gerok W: Remodeling of a rat hepatocyte plasma membrane glycoprotein. De- and reglycosylation of dipeptidyl peptidase IV. J Biol Chem 263:11736, 1988
    • (1988) J Biol Chem , vol.263 , pp. 11736
    • Kreisel, W.1    Hanski, C.2    Tran-Thi, T.-A.3    Katz, N.4    Decker, K.5    Reutter, W.6    Gerok, W.7
  • 19
    • 0023811466 scopus 로고
    • The major protein of pancreatic zymogen granule membranes (GP-2) is anchored via covalent bonds to phosphatidylinositol
    • LeBel D, Beattie M: The major protein of pancreatic zymogen granule membranes (GP-2) is anchored via covalent bonds to phosphatidylinositol. Biochem Biophys Res Commun 154:818, 1988
    • (1988) Biochem Biophys Res Commun , vol.154 , pp. 818
    • Lebel, D.1    Beattie, M.2
  • 20
    • 0027383762 scopus 로고
    • The epithelial sialomucin, episialin, is sialylated during recycling
    • Litvinov SV, Hilkens J: The epithelial sialomucin, episialin, is sialylated during recycling. J Biol Chem 268:21364, 1993
    • (1993) J Biol Chem , vol.268 , pp. 21364
    • Litvinov, S.V.1    Hilkens, J.2
  • 21
    • 0002923914 scopus 로고
    • Development of the embryonic endocrine pancreas
    • Greed OR, Astwood EB, eds. Washington DC, American Physiological Society
    • Pictet R, Rutter WJ: Development of the embryonic endocrine pancreas. In Greed OR, Astwood EB, eds. Handbook of physiology. Sect 7. Endocrinology. Washington DC, American Physiological Society, 1972, 25
    • (1972) Handbook of Physiology. Sect 7. Endocrinology , pp. 25
    • Pictet, R.1    Rutter, W.J.2
  • 22
    • 13344289863 scopus 로고
    • Packaging of pancreas secretory proteins in the condensing vacuoles of the Golgi complex
    • Ribet A, Pradayrol L, Susini C, eds. New York. Elsevier/North Holland Biomedical Press
    • Reggio H, Dagorn JC: Packaging of pancreas secretory proteins in the condensing vacuoles of the Golgi complex. In Ribet A, Pradayrol L, Susini C, eds. Biology of normal and cancerous exocrine pancreatic cells. New York. Elsevier/North Holland Biomedical Press, 1980, 229
    • (1980) Biology of Normal and Cancerous Exocrine Pancreatic Cells , pp. 229
    • Reggio, H.1    Dagorn, J.C.2
  • 23
    • 0018146277 scopus 로고
    • Ionic interactions between bovine chymotrypsinogen A and chondroitin sulfate A.B.C
    • Reggio H, Dagorn JC: Ionic interactions between bovine chymotrypsinogen A and chondroitin sulfate A.B.C. J Cell Biol 78:951, 1978
    • (1978) J Cell Biol , vol.78 , pp. 951
    • Reggio, H.1    Dagorn, J.C.2
  • 24
    • 0017808680 scopus 로고
    • Sulfated compounds in the zymogen granules of the guinea pig pancreas
    • Reggio HA, Palade GE: Sulfated compounds in the zymogen granules of the guinea pig pancreas. J Cell Biol 77:288, 1978
    • (1978) J Cell Biol , vol.77 , pp. 288
    • Reggio, H.A.1    Palade, G.E.2
  • 25
    • 0021048692 scopus 로고
    • Light microscopic detection of sugar residues in glycoconjugates of salivary glands and the pancreas with lectin-horseradish peroxidase conjugates. I. Mouse
    • Schulte BA, Spicer SS: Light microscopic detection of sugar residues in glycoconjugates of salivary glands and the pancreas with lectin-horseradish peroxidase conjugates. I. Mouse. Histochem J 15:1217, 1983
    • (1983) Histochem J , vol.15 , pp. 1217
    • Schulte, B.A.1    Spicer, S.S.2
  • 27
    • 0018254603 scopus 로고
    • Development of exocrine cells of the pancreas and parotid gland in rats
    • Takeuchi T, Kameya T, Tsumuraya M, Sugimura T: Development of exocrine cells of the pancreas and parotid gland in rats. Digestion 18:266, 1978
    • (1978) Digestion , vol.18 , pp. 266
    • Takeuchi, T.1    Kameya, T.2    Tsumuraya, M.3    Sugimura, T.4
  • 28
    • 0018418602 scopus 로고
    • Development of secretory mechanisms in rat pancreas
    • Werlin SL, Grand RJ: Development of secretory mechanisms in rat pancreas. Am J Physiol 236:E446, 1979
    • (1979) Am J Physiol , vol.236
    • Werlin, S.L.1    Grand, R.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.