Localization of protein disulfide isomerase on plasma membranes of rat exocrine pancreatic cellsS Akagi, A Yamamoto, T Yoshimori, R Masaki, R Ogawa and Y Tashiro Department of Physiology, Kansai Medical University, Osaka, Japan. We investigated immunocytochemically the ultrastructural localization of protein disulfide isomerase (PDI) in rat pancreatic exocrine cells by use of the post-embedding protein A-gold technique. We found that not only the endoplasmic reticulum (ER) and nuclear envelope but also the trans-Golgi cisternae, secretory granules, and plasma membranes were heavily labeled with gold particles. Labeling density of the gold particles in the rough ER and plasma membranes of the exocrine pancreatic cells was twofold and twentyfold greater, respectively, than that of hepatocytes. In the acinar lumen, amorphous material presumably corresponding to the secreted zymogens was also labeled with gold particles. These results suggest that in rat exocrine pancreatic cells a significant amount of PDI is transported to the plasma membrane and secreted to the acinar lumen.
Volume 36,
Issue 8,
pp. 1069-1074,
08/01/1988
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K. L. Asquith, R. M. Baleato, E. A. McLaughlin, B. Nixon, and R. J. Aitken Tyrosine phosphorylation activates surface chaperones facilitating sperm-zona recognition J. Cell Sci., July 15, 2004; 117(16): 3645 - 3657. [Abstract] [Full Text] [PDF] |
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K. Hatsuzawa, H. Hirose, K. Tani, A. Yamamoto, R. H. Scheller, and M. Tagaya Syntaxin 18, a SNAP Receptor That Functions in the Endoplasmic Reticulum, Intermediate Compartment, and cis-Golgi Vesicle Trafficking J. Biol. Chem., April 28, 2000; 275(18): 13713 - 13720. [Abstract] [Full Text] [PDF] |
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J. K. Burgess, K. A. Hotchkiss, C. Suter, N. P. B. Dudman, J. Szollosi, C. N. Chesterman, B. H. Chong, and P. J. Hogg Physical Proximity and Functional Association of Glycoprotein 1balpha and Protein-disulfide Isomerase on the Platelet Plasma Membrane J. Biol. Chem., March 24, 2000; 275(13): 9758 - 9766. [Abstract] [Full Text] [PDF] |
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H. A. Lucero and B. Kaminer The Role of Calcium on the Activity of ERcalcistorin/Protein-disulfide Isomerase and the Significance of the C-terminal and Its Calcium Binding. A COMPARISON WITH MAMMALIAN PROTEIN-DISULFIDE ISOMERASE J. Biol. Chem., January 29, 1999; 274(5): 3243 - 3251. [Abstract] [Full Text] [PDF] |
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X.-M. Jiang, M. Fitzgerald, C. M. Grant, and P. J. Hogg Redox Control of Exofacial Protein Thiols/Disulfides by Protein Disulfide Isomerase J. Biol. Chem., January 22, 1999; 274(4): 2416 - 2423. [Abstract] [Full Text] [PDF] |
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C. Velez-Granell, A. Arias, J. Torres-Ruiz, and M Bendayan 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., January 3, 1994; 107(3): 539 - 549. [Abstract] [PDF] |
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K. K. Graven, C. Molvar, J. S. Roncarati, B. D. Klahn, S. Lowrey, and H. W. Farber Identification of protein disulfide isomerase as an endothelial hypoxic stress protein Am J Physiol Lung Cell Mol Physiol, May 1, 2002; 282(5): L996 - L1003. [Abstract] [Full Text] [PDF] |
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