Molecular characterization of cDNA for phospholipase A2-activating protein
Identifieur interne : 002161 ( Istex/Curation ); précédent : 002160; suivant : 002162Molecular characterization of cDNA for phospholipase A2-activating protein
Auteurs : A. K. Chopra [États-Unis] ; D. A. Ribardo [États-Unis] ; T. G. Wood [États-Unis] ; D. J. Prusak [États-Unis] ; X.-J. Xu [États-Unis] ; J. W. Peterson [États-Unis]Source :
- BBA - Gene Structure and Expression [ 0167-4781 ] ; 1999.
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Abstract
Abstract: A phospholipase A2-activating protein (PLAP) cDNA was cloned and sequenced from a human monocyte cDNA library, and expressed as a histidine-tagged fusion protein. The DNA-deduced aa sequence of human PLAP was 80,826 Da; however, SDS-PAGE analysis revealed a 72-74 kDa protein which matched the size of native PLAP from human monocytes. Anti-sense plap oligonucleotide blocked cholera toxin-induced release of 3H-labeled arachidonic acid from cells, indicating a potential role for PLAP in regulating phospholipase A2 activity.
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DOI: 10.1016/S0167-4781(98)00249-8
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<term>Chopra</term>
<term>Clone</term>
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<term>Eicosanoid synthesis</term>
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<term>Oligonucleotide</term>
<term>Phospholipase</term>
<term>Plap</term>
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<front><div type="abstract" xml:lang="en">Abstract: A phospholipase A2-activating protein (PLAP) cDNA was cloned and sequenced from a human monocyte cDNA library, and expressed as a histidine-tagged fusion protein. The DNA-deduced aa sequence of human PLAP was 80,826 Da; however, SDS-PAGE analysis revealed a 72-74 kDa protein which matched the size of native PLAP from human monocytes. Anti-sense plap oligonucleotide blocked cholera toxin-induced release of 3H-labeled arachidonic acid from cells, indicating a potential role for PLAP in regulating phospholipase A2 activity.</div>
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