Brefeldin A inhibits the constitutive-like secretion of a sulfated protein in pancreatic acinar cells

European Journal of Cell Biology

Volumn 71, Issue 1, 1996, Pages 62-71

  De Lisle, Robert C ^a   Bansal, Rina ^a  

^a UNIVERSITY OF KANSAS SCHOOL OF MEDICINE   (United States)

Author keywords

Brefeldin A; Constitutive like secretion; gp300; Pancreatic acinar cell; Pancreatic lipase; Secretory granule biogenesis; Sulfated protein

Indexed keywords

BREFELDIN A; SECRETORY PROTEIN; SULFUR 35; TRIACYLGLYCEROL LIPASE; ZYMOGEN GRANULE;

ACINAR CELL; ANIMAL CELL; ARTICLE; CELL KINETICS; CELLULAR DISTRIBUTION; CONTROLLED STUDY; IMMUNOFLUORESCENCE; MOUSE; NONHUMAN; PRIORITY JOURNAL; PROTEIN PROCESSING; PROTEIN SECRETION; SULFATION;

ANIMALIA;

EID: 0029822947     PISSN: 01719335     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

References (28)

1. Arvan, P., J. D. Castle: Phasic release of newly synthesized secretory proteins in the unstimulated rat exocrine pancreas. J. Cell Biol. 104, 243-252 (1987).
2. Arvan, P., J. D. Castle: Protein sorting and secretion granule formation in regulated secretory cells. Trends Cell Biol. 2, 327-331 (1992).
3. Arvan, P., A. Chang: Constitutive protein secretion from the exocrine pancreas of fetal rats. J. Biol. Chem. 262, 3886-3890 (1987).
4. Beaudoin, A. R., G. Grondin: Secretory pathways in animal cells: With emphasis on pancreatic acinar cells. J. Electron Microsc. Tech. 17, 51-69 (1991).
5. Burnham, D. B., D. J. McChesney, K. C. Thurston, J. A. Williams: Interaction of cholecystokinin and vasoactive intestinal peptide on function of mouse pancreatic acini in vitro. J. Physiol. 349, 475-482 (1984).
6. Carnell, L., H.-P. H. Moore: Transport via the regulated secretory pathway in semi-intact PC12 cells: role of intra-cisternal calcium and pH in the transport and sorting of secretogranin II. J. Cell Biol. 127, 693-705 (1994).
7. Colomer, V., M. J. Rindler, A. W. Lowe: Apical plasma membrane proteins are not obligatorily stored in secretory granules in exocrine cells. J. Cell Sci. 107, 2271-2277 (1994).
8. De Lisle, R. C.: 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, 385-396 (1994).
9. Göke, B., J. A. Williams, M. J. Wishart, R. C. De Lisle: Low molecular mass GTP-binding proteins in subcellular fractions of the pancreas: regulated phosphoryl G-proteins. Am. J. Physiol. Cell Physiol. 262, C493-C500 (1992).
10. Harlow, E., D. Lane: Antibodies: A laboratory manual. Cold Spring Harbor, NY. (1988).
11. Hendricks, L. C., S. L. McClanahan, G. E. Palade, M. G. Farquhar: Brefeldin A affects early but docs not affect late events along the exocytic pathway in pancreatic acinar cells. Proc. Natl. Acad. Sci. 89, 7242-7246 (1992).
12. Huang, X. F., P. Arvan: Formation of the insulin-containing secretory granule core occurs within immature β-granules. J. Biol. Chem. 269, 20838-20844 (1994).
13. Jamieson, J. D., G. E. Palade: Condensing vacuole conversion and zymogen granule discharge in pancreatic exocrine cells: metabolic studies. J. Cell Biol. 48, 503-522 (1971).
14. Kömhoff, M., M. Hollinshead, J. Tooze, H. F. Kern: Brefeldin A induced dose-dependent changes to Golgi structure and function in the rat exocrine pancreas. Eur. J. Cell Biol. 63, 192-207 (1994).
15. Kuliawat, R., P. Arvan: Protein targeting via the "constitutive-like" secretory pathway in isolated pancreatic islets: Passive sorting in the immature granule compartment. J. Cell Biol. 118, 521-529 (1992).
16. Ladinsky, M. S., K. E. Howell: The trans-Golgi network can be dissected structurally and functionally from the cisternae of the Golgi complex by brefeldin A. Eur. J. Cell Biol. 59, 92-105 (1992).
17. Lippincott-Schwartz, J., L. Yuan, C. Tipper, M. Amherdt, L. Orci, R. D. Klausner: Brefeldin A's effects on endosomes, lysosomes, and the TGN suggest a general mechanism for regulating organelle structure and membrane traffic. Cell 67, 601-616 (1991).
18. Miller, S. G., H.-P. H. Moore: Movement from trans-Golgi network to cell surface in semiintact cells. Methods Enzymol. 219, 234-248 (1992).
19. Moss, J., M. Vaughan: Structure and function of ARF proteins: activators of cholera toxin and critical components of intracellular vesicular transport processes. J. Biol. Chem. 270, 12327-12330 (1995).
20. Robinson, M. S., T. E. Kreis: Recruitment of coat proteins onto Golgi membranes in intact and permeabilized cells. Effects of brefeldin A and G protein activators. Cell 69, 129-138 (1992).
21. Rosa, P., F. A. Barr, J. C. Stinchcombe, C. Binacchi, W. B. Huttner: Brefeldin A inhibits the formation of constitutive secretory vesicles and immature secretory granules from the trans-Golgi network. Eur. J. Cell Biol. 59, 265-274 (1992).
22. Rosa, P., S. Mantovani, R. Rosboch, W. B. Huttner: Monensin and brefeldin A differentially affect the phosphorylation and sulfation of secretory proteins. J. Biol. Chem. 267, 12227-12232 (1992).
23. Tooze, S. A., W. B. Huttner: Cell-free protein sorting to the regulated and constitutive secretory pathways. Cell 60, 837-847 (1990).
24. Von Zastrow, M., A. M. Castle, J. D. Castle: Ammonium chloride alters secretory protein sorting within the maturing exocrine storage compartment. J. Biol. Chem. 264, 6566 (1989).
25. Von Zastrow, M., J. D. Castle: Protein sorting among two distinct export pathways occurs from the content of maturing exocrine storage granules. J Cell Biol. 105, 2675-2684 (1987).
26. Wagner, M., A. K. Rajasekaran, D. K. Hanzel, S. Mayor, E. Rodriguez-Boulan: Brefeldin A causes structural and functional alterations of the trans-Golgi network of MDCK cells. J. Cell Sci. 107, 933-943 (1994).
27. Wicker-Planquart, C., A. Puigserver: Primary structure of rat pancreatic lipase mRNA. FEBS Lett. 296, 61-66 (1992).
28. Yamashina, S., O. Katsumata, H. Tamaki, A. Takatsuki: Morphological effects of brefeldin A on the intracellular transport of secretory materials in parotid acinar cells. Cell Struct. Funct. 15, 31-37 (1990).