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J Biol Chem, Vol. 275, Issue 2, 1161-1168, January 14, 2000
From the Department of Health Chemistry, School of Pharmaceutical
Sciences, Showa University, 1-5-8 Hatanodai,
Shinagawa-ku, Tokyo 142-8555, Japan
Cytosolic phospholipase A2
(cPLA2)
Identification of a Cellular Protein That Functionally
Interacts with the C2 Domain of Cytosolic Phospholipase
A2
*
plays critical roles in lipid mediator
synthesis. We performed far-Western analysis and identified a 60-kDa
protein (P60) that interacted with cPLA2 in a
Ca2+-dependent manner. Peptide microsequencing
revealed that purified P60 was identical to vimentin, a major component
of the intermediate filament. The interaction occurred between the C2
domain of cPLA2 and the head domain of vimentin.
Immunofluorescence microscopic analysis demonstrated that
cPLA2 and vimentin colocalized around the perinuclear
area in cPLA2-overexpressing human embryonic kidney 293 cells following A23187 stimulation. Forcible expression of vimentin in
vimentin-deficient SW13 cells augmented A23187-induced arachidonate
release. Moreover, overexpression of the vimentin head domain in rat
fibroblastic 3Y1 cells exerted a dominant inhibitory effect on
arachidonate metabolism, significantly reducing A23187-induced arachidonate release and attendant prostanoid generation. These results
suggest that vimentin is an adaptor for cPLA2 to
function properly during the eicosanoid-biosynthetic process.
*
This work was supported by grants-in-aid for scientific
research from the Ministry of Education, Science, Sports and Culture of
Japan; the Human Science Foundation; and Special Coordination Funds for
Promoting Science and Technology from the Science and Technology
Agency.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.
To whom correspondence should be addressed. Tel.: 81-3-3784-8196;
Fax: 81-3-3784-8245; E-mail: kudo@pharm.showa-u.ac.jp.
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