Abstract
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.
MeSH terms
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Annexin A2 / metabolism
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Arachidonic Acid / metabolism
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Bronchi / cytology
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Bronchi / enzymology
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Calcium-Binding Proteins / metabolism*
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Cell Line
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Cell-Free System
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Cytosol / enzymology
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DNA / metabolism
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DNA-Binding Proteins / metabolism
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Epithelium / enzymology
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Humans
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Oligonucleotides, Antisense / metabolism
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Phospholipases A / antagonists & inhibitors*
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Phospholipases A / genetics
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Phospholipases A2
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Protein Binding
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Saccharomyces cerevisiae Proteins*
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Transcription Factors / metabolism
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Transfection
Substances
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Annexin A2
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Calcium-Binding Proteins
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DNA-Binding Proteins
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GAL4 protein, S cerevisiae
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Oligonucleotides, Antisense
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Saccharomyces cerevisiae Proteins
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Transcription Factors
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Arachidonic Acid
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DNA
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Phospholipases A
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Phospholipases A2