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Vol. 13, Issue 10, 3388-3399, October 2002
-Cells
*Department of Molecular Medicine, Institute for Molecular and
Cellular Regulation, Gunma University, Maebashi, 371-8512, Japan;
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 coexpressed in
pituitary and pancreatic endocrine cell lines, whereas SgIII was not
expressed in the adrenal glands and PC12 cells. Immunoelectron microscopy demonstrated that CgA and SgIII were specifically
colocalized 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 missorted 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 localizes with SgIII by specific binding in secretory
granules in SgIII-expressing pituitary and pancreatic endocrine cells,
whereas other mechanisms are likely to be responsible for CgA
localization in secretory granules of SgIII-lacking adrenal chromaffin
cells and PC12 cells.
Department of Anatomy II, Asahikawa Medical College,
Asahikawa, Hokkaido 078-8510, Japan; and §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.
These two authors contributed equally to this work.
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