Possible association of chaperonin 60 with secretory proteins in pancreatic acinar cells

Journal of Histochemistry and Cytochemistry

Volumn 44, Issue 7, 1996, Pages 743-749

  Le Gall, Isabelle M ^a   Bendayan, Moïse ^a  

^a UNIVERSITÉ DE MONTRÉAL   (Canada)

Author keywords

Hsp60; Immunocytochemistry; Pancreas; Secretion

Indexed keywords

AMYLASE; CARBOXYPEPTIDASE B; CHAPERONIN; CHYMOTRYPSINOGEN; ENZYME PRECURSOR; SECRETORY PROTEIN; TRIACYLGLYCEROL LIPASE; TRYPSINOGEN;

ANIMAL CELL; ANIMAL TISSUE; ANTIBODY LABELING; ARTICLE; CYTOSOL; ENZYME ACTIVITY; HYPOTHESIS; IMMUNOCYTOCHEMISTRY; IMMUNOPRECIPITATION; NONHUMAN; PANCREAS CELL; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN PROCESSING; RAT;

EID: 0029955716     PISSN: 00221554     EISSN: None     Source Type: Journal    
DOI: 10.1177/44.7.8675995     Document Type: Article

References (40)

1. Ellis J. Proteins as molecular chaperones. Nature 1987;328:378-379
2. Gething MJ, Sambrook J. Protein folding in the cell. Nature 1992; 355:33-45
3. Becker J, Craig EA. Heat-shock proteins as molecular chaperones. Eur J Biochem 1994; 219:11-23
4. Hartl FU, Hlodan R, Langer T. Molecular chaperones in protein folding: the art of avoiding sticky situations. Trends Biochem Sci 1994; 19:20-25
5. Ellis RJ. Roles of molecular chaperones in protein folding. Curr Opin Struct Biol 1994;4:117-122
6. Hemmingsen SM, Woolford C, van der Vies SM, Tilly K, Dennis DT, Georgopoulos CP, Hendrix RW, Ellis RJ. Homologous plant and bacterial proteins chaperone oligomeric protein assembly. Nature 1988; 333:330-334
7. Hendrix RW. Purification and properties of groE, a host protein involved in bacteriophage asesmbly. J Mol Biol 1979;129:375-392
8. Ostermann J, Horwich AL, Neupert W, Hartl FU. Protein folding in mitochondria requires complex formation with hsp60 and ATP hydrolysis. Nature 1989;341:125-130
9. Lubben TH, Gatenby AA, Donaldson GK, Lorimer GH, Viitanen PV. Identification of a groES-like chaperonin in mitochondria that facilitates protein folding. Proc Natl Acad Sci USA 1990;87:7683-7687
10. Martin J, Mayhew M, Langer T, Hartl FU. The reaction cycle of GroEL and GroES in chaperonin-assisted protein folding. Nature 1993; 366:228-233
11. Gupta RS. Sequence and structural homology between a mouse T-complex protein TCP-1 and the "chaperonin" family of bacterial (groEL, 60-65 kDa heat shock antigen) and eukaryotic proteins. Biochem Int 1990;20:833-841
12. McMullin TW, Hallberg RL. A highly evolutionary conserved mitochondrial protein is structurally related to the protein encoded by the Escherichia coli groEL gene. Mol Cell Biol 1988;8:371-380
13. Vélez-Granell CS, Arias AE, Torres-Ruíz JA, Bendayan M. Immunocytochemical localization of chaperonins 10 and 60 in rat liver tissue. Biol Cell, in press
14. Barraclough R, Ellis RJ. Protein synthesis in chloroplasts. IX. Assembly of newly-synthesized large subunits into ribulose bisphosphate carboxylase in isolated intact pea chloroplasts. Biochim Biophys Acta 1980; 608:19-31
15. Vélez-Granell CS, Arias AE, Torres-Rúz JA, Bendayan M. Molecular chaperones in pancreatic tissue: the presence of cpn10, cpn60, and hsp70 in distinct compartments along the secretory pathway of the acinar cells. J Cell Sci 1994;107:539-549
16. Bendayan M, Roth J, Perrelet A, Orci L. Quantitative immunocytochemical localization of pancreatic secretory proteins in subcellular compartments of the rat acinar cell. J Histochem Cytochem 1980;28:149-160
17. Palade GE. Intracellular aspects of the process of protein synthesis. Science 1980;189:347-358
18. Arias AE, Vélez-Granell CS, Torres-Ruíz JA, Bendayan M. Involvement of molecular chaperones in the aberrant aggregation of secretory proteins in pancreatic acinar cells. Exp Cell Res 1994;215:1-8
19. Scala C, Cenacchi G, Ferrari C, Pasquinelli G, Preda P, Manara GC. A new acrylic resin formulation: a useful tool for histological, ultrastructural and immunocytochemical investigations. J Histochem Cytochem 1992;40:1799-1804
20. Bendayan M. Colloidal gold post-embedding immunocytochemistry. Prog Histochem Cytochem 1995;29:1-163
21. Doerr-Schott J. Colloidal gold for multiple staining. In Hayat M, ed. Colloidal Gold: Principles, Methods, and Applications. Vol, 1. San Diego: Academic Press, 1989: 145-190
22. Tapia FJ, Varndell IM, Probert L, De Mey J, Polak JM. Double immunogold staining method for the simultaneous ultrastructural localization of regulatory peptides. J Histochem Cytochem 1983;31:977-981
23. Bendayan M, Ito S. Immunohistochemical localization of exocrine enzymes in normal rat pancreas. J Histochem Cytochem 1979:27:1029-1034
24. Pâquet MR, St-Jean P, Roberge M, Beaudoin AR. Isolation of zymogen granules from rat pancreas and characterization of their membrane proteins. Eur J Cell Biol 1982;28:20-26
25. Smith PK, Krohn RI, Hermanson GT, Mallia AK, Gartner FH, Provenzano MD, Fujimoto EK, Goeke NM, Olson BJ, Klenk DC. Measurement of protein using bicinchroninic acid. Ann Biochem 1985; 150:76-85
26. Kessler SW. Use of protein A-bearing staphylococci for the immunoprecipitation and isolation of antigens from cells. Methods Enzymol 1981;73:442-459
27. Towbin H, Staehelin T, Gordon J. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc Natl Acad Sci USA 1979;76:4350-4354
28. Hobson AH, Buckley CM, Aamand JL, Jørgensen ST, Diderichsen B, McConnell DJ. Activation of a bacterial lipase by its chaperone. Proc Natl Acad Sci USA 1993;90:5682-5686
29. Bruneau N, Lombarde D. Chaperone function of a Grp 94-related protein for folding and transport of the pancreatic bile salt-dependent lipase. J Biol Chem 1995;270:13524-13533
30. Marchis-Mouren G. Étude comparée de l'équipement enzymatique du suc pancréatique de diverses espèces. Bull Soc Chim Biol 1965; 47:2207-2217
31. Beckmann RP, Mizzen LA, Welch WJ. Interaction of Hsp70 with newly synthesized proteins: implications for protein folding and assembly. Science 1990;248:850-854
32. Langer T, Lu C, Echols H, Flanagan J, Hayer MK, Hartl FU. Successive action of DnaK, DnaJ, and GroEL along the pathway of chaperone-mediated protein folding. Nature 1992;356:683-689
33. Martin J, Langer T, Boteva R, Schramel A, Horwich AI, Hartl FU. Chaperonin-mediated protein folding at the surface of groEL through a "molten globule"-like intermediate. Nature 1991;352:36-42
34. Fisher MK, Yuan X. The rates of commitment to renaturation of rhodanese and glutamine synthetase in the presence of the GroE chaperonins. J Biol Chem 1994;269:29598-29601
35. Kern G, Schmidt M, Buchner J, Jaenicke R. Glycosylation inhibits the interaction of invertase with the chaperone GroEL. FEBS Lett 1992; 305:203-205
36. Itoh H, Kobayashi R, Wakui H, Komatsuda A, Ohtani H, Miura AB, Otaka M, Masamune O, Andoh H, Koyama K, Sato Y, Tashima Y. Mammalian 60-kDa stress protein (chaperonin homolog). J Biol Chem 1995;270:13429-13435
37. Bochkareva ES, Lissin NM, Girshovich AS. Transient association of newly synthesized unfolded proteins with the heat-shock GroEL protein. Nature 1988;336:254-257
38. Simons JF, Ferro-Novick S, Rose MD, Helenius A. Bip/Kar2p serves as a molecular chaperone during carboxypeptidase Y folding in yeast. J Cell Biol 1995;130;41-49
39. Buchner J, Schmidt M, Fuchs M, Jaenicke R, Rudolph R, Schmid FX, Kiefhabet T. GroE facilitates refolding of citrate synthase by suppressing aggregation. Biochemistry 1991;30:1586-1591
40. Braun JEA, Scheller RH. Cysteine string protein, a DnaJ family member, is present on diverse secretory vesicles. Neuropharmacology 1995; 34:1361-1369