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Comparative Study
. 1999 Jan 18;1444(1):125-30.
doi: 10.1016/s0167-4781(98)00249-8.

Molecular characterization of cDNA for phospholipase A2-activating protein

A K Chopra  1 , D A Ribardo, T G Wood, D J Prusak, X J Xu, J W Peterson
Affiliations
Comparative Study

Molecular characterization of cDNA for phospholipase A2-activating protein

A K Chopra et al. Biochim Biophys Acta. .

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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