Novel isoforms of intracellular platelet activating factor acetylhydrolase (PAFAH1b2) in human testis; encoded by alternatively spliced mRNAs.

Platelet activating factor acetylhydrolase (paf-ah), a potent regulator of platelet activating factor activity, plays an important role in various physiological and pathophysiological functions including development, reproduction, inflammation, hemostasis, and apoptosis. Intracellular paf-ah (paf-ah-Ib) is composed of a regulatory subunit, Pafah1b1, and two highly conserved but non-identical catalytic subunits, Pafah1b2 and Pafah1b3. The present study identifies new splice variants of the Pafah1b2 gene transcript. The splice variants retain exons 1-5 and replace exon 6 with alternative exons derived from genomic sequence 3' to exon 6. Splice variants encode two proteins with different novel carboxy termini. One of the isoforms is expressed exclusively in testis. These new isoforms of pafah1b2 retain the ability to form higher order complexes while replacing known key catalytic residues, which raises the possibility that they may alter the subunit composition and catalytic function of paf-ah-Ib.