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Molecular characterization of cDNA for phospholipase A2-activating protein

Identifieur interne : 002607 ( Main/Exploration ); précédent : 002606; suivant : 002608

Molecular 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 :

RBID : ISTEX:3A687B02B3C3A2EFF436CCCF3EA7AC6C3ED1D33F

English descriptors

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.

Url:
DOI: 10.1016/S0167-4781(98)00249-8


Affiliations:


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