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Molecular characterization of cDNA for phospholipase A2-activating protein
A K Chopra1, D A Ribardo, T G Wood
1Department of Microbiology and Immunology, The University of Texas Medical Branch, Galveston, TX 77555-1070, USA. achopra@utmb.edu
Biochimica Et Biophysica Acta
|February 5, 1999
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.