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The inositol 1,4,5-trisphosphate receptor (IP
Volume 270,
Number 24,
Issue of June 16, pp. 14700-14704, 1995
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
R)
exists as a tetrameric complex to form a functional inositol
1,4,5-trisphosphate-gated Ca channel. Molecular
cloning studies have shown that there are at least three types of
IP
R subunits, designated type 1, type 2, and type 3. The
levels of expression of IPR subunits in various cell lines
were investigated by Western blot analysis using type-specific
antibodies against 15 C-terminal amino acids of each IPR
subunit. We found that all the three types of IPR subunits
were expressed in each cell line examined, but their levels of
expression varied. To determine whether IPRs form
heterotetramers, we employed immunoprecipitation experiments using
Chinese hamster ovary cells (CHO-K1 cells), in which all three types
are abundantly expressed. Each type-specific antibody
immunoprecipitated not only the respective cognate type but also the
other two types. This result suggests that distinct types of
IPR subunits assemble to form heterotetramers in CHO-K1
cells. We also detected heterotetramers in rat liver, in which
IPR type 1 and type 2 are expressed abundantly. Previous
studies have shown some functional differences among IPR
types, suggesting the possibility that various compositions of subunits
show distinct channel properties. The diversity of IPR
channels may be further increased by the co-assembly of different
IPR subunits to form homo- or heterotetramers.
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