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(Received for publication, February 14, 1997, and in revised form, April 23, 1997)
From the Critical Care Medicine Department, National Institutes of
Health, Bethesda, Maryland 20892
Using a two hybrid system screen of a human
cDNA library, we have found that p11, a unique member of the S100
family of calcium-binding proteins, interacts with the carboxyl region
of the 85-kDa cytosolic phospholipase A2
(cPLA2). p11 synthesized in a cell-free system interacts
with cPLA2 in vitro. The p11-cPLA2
complex is detectable from a human bronchial epithelial cell line (BEAS
2B). Furthermore, p11 inhibits cPLA2 activity in
vitro. Selective inhibition of p11 expression in the BEAS 2B
cells by antisense RNA results in an increased PLA2
activity as well as an increased release of prelabeled arachidonic
acid. This study demonstrates a novel mechanism for the regulation of
cPLA2 by an S100 protein.
Volume 272, Number 27,
Issue of July 4, 1997
pp. 17145-17153
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
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