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Originally published In Press as doi:10.1074/jbc.M107532200 on October 2, 2001

J. Biol. Chem., Vol. 276, Issue 49, 45806-45812, December 7, 2001
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Localization of Three Types of the Inositol 1,4,5-Trisphosphate Receptor/Ca2+ Channel in the Secretory Granules and Coupling with the Ca2+ Storage Proteins Chromogranins A and B*

Seung Hyun YooDagger , Young Soo Oh, Moon Kyung Kang, Yang Hoon Huh, Seung Ho So, Hyung Seon Park, and Hee Yun Park

From the National Creative Research Initiative Center for Secretory Granule Research, Korea Advanced Institute of Science and Technology, Yu Sung Gu, Dae Jeon, Korea 305-701

Although the role of secretory granules as the inositol 1,4,5-trisphosphate (IP3)-sensitive intracellular Ca2+ store and the presence of the IP3 receptor (IP3R)/Ca2+ channel on the secretory granule membrane have been established, the identity of the IP3R types present in the secretory granules is not known. We have therefore investigated the presence of different types of IP3R in the secretory granules of bovine adrenal medullary chromaffin cells using immunogold electron microscopy and found the existence of all three types of IP3R in the secretory granules. To determine whether these IP3Rs interact with CGA and CGB, each IP3R isoform was co-transfected with CGA or CGB into NIH3T3 or COS-7 cells, and the expressed IP3R isoform and CGA or CGB were co-immunoprecipitated. From these studies it was shown that all three types of IP3R form complexes with CGA and CGB in the cells. To further confirm whether the IP3R isoforms and CGA and CGB form a complex in the secretory granules the potential interaction between all three isoforms of IP3R and CGA and CGB was tested by co-immunoprecipitation experiements of the mixture of secretory granule lysates and the granule membrane proteins. The three isoforms of IP3R were shown to form complexes with CGA and CGB, indicating the complex formation between the three isoforms of IP3R and CGA and CGB in the secretory granules. Moreover, the pH-dependent Ca2+ binding property of CGB was also studied using purified recombinant CGB, and it was shown that CGB bound 93 mol of Ca2+/mol with a dissociation constant (Kd) of 1.5 mM at pH 5.5 but virtually no Ca2+ at pH 7.5. The high capacity, low affinity Ca2+-binding property of CGB at pH 5.5 is comparable with that of CGA and is in line with its role as a Ca2+ storage protein in the secretory granules.

* The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EMBL Data Bank with accession number(s) AF402600 and AF402601.

Dagger To whom correspondence should be addressed. Tel.: 82-42-869-8279; Fax: 82-42-869-8280; E-mail: shyoo@kaist.ac.kr.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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