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A more recent version of this article appeared on October 1, 2002
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Submitted on March 18, 2002
Revised on July 11, 2002
Accepted on July 22, 2002
1 Department of Molecular Medicine, Institute for Molecular and Cellular Regulation, Gunma University, Maebashi, 371-8512, Japan
2 Department of Anatomy II, Asahikawa Medical College, Asahikawa, Hokkaido 078-8510, Japan
3 Department of Cell Biology and Neuroscience, Osaka University Graduate School of Medicine, Suita, Osaka 565-0871, Japan
* Corresponding author. E-mail address: tstake{at}showa.gunma-u.ac.jp.
Chromogranin A (CgA) is transported restrictedly to secretory granules in neuroendocrine cells. In addition to pH- and Ca2+-dependent aggregation, CgA is known to bind to a number of vesicle matrix proteins. Because the binding-prone property of CgA with secretory proteins may be essential for its targeting to secretory granules, we screened its binding partner proteins using a yeast two-hybrid system. We found that CgA bound to secretogranin III (SgIII) by specific interaction both in vitro and in endocrine cells. Localization analysis showed that CgA and SgIII were co-expressed in pituitary and pancreatic endocrine cell lines, while SgIII was not expressed in the adrenal glands and PC12 cells. Immunoelectron microscopy demonstrated that CgA and SgIII were specifically co-localized in large secretory granules in male rat gonadotropes, which possess large-type and small-type granules. An immunocytochemical analysis revealed that deletion of the binding domain (CgA 48-111) for SgIII mis-sorted CgA to the constitutive pathway, whereas deletion of the binding domain (SgIII 214-373) for CgA did not affect the sorting of SgIII to the secretory granules in AtT-20 cells. These findings suggest that CgA localize with SgIII by specific binding in secretory granules in SgIII-expressing pituitary and pancreatic endocrine cells, while other mechanisms are likely to be responsible for CgA localization in secretory granules of SgIII-lacking adrenal chromaffin cells and PC12 cells.
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