Characterization of p26olf, a Novel Calcium-binding Protein
in the Frog Olfactory Epithelium*
Naofumi
Miwa
,
Tatsuya
Uebi, and
Satoru
Kawamura
From the Department of Biology, Graduate School of Science, Osaka
University, Machikane-yama 1-1, Toyonaka, Osaka 560-0043, Japan
We have previously shown that p26olf is a novel
S100-like Ca2+-binding protein in the frog olfactory
epithelium. In this paper, we characterized the Ca2+
binding property of p26olf, examined the precise localization in the
frog olfactory epithelium, and searched for the possible target
proteins of p26olf. By flow dialysis experiments using 45Ca, p26olf was suggested to bind ~4 Ca2+.
Circular dichroism measurement showed that binding of Ca2+
to p26olf induces an increase in the apparent content of both 
-helix
and 
-sheet with an apparent Kd value of 2.4 µM. Electron microscopic observation disclosed p26olf
immunoreactivity in the cilia, dendritic knob, and dendrite of
olfactory receptor cells. Blot overlay analysis and affinity
purification of p26olf-binding proteins showed that p26olf binds to a
frog -adrenergic receptor kinase-like protein in a
Ca2+-dependent manner. These results suggested
that p26olf has some roles in the olfactory transduction or adaptation.
*
This work was supported by the Research for the Future
program of the Japan Society for the Promotion of Science under the project "Cell Signalling" (JSPS-RFTF97L00301), the Mitsubishi Foundation, and the Uehara Memorial Foundation (to S. K.).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.
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