Molecular structure and tissue-specific expression of the mouse pancreatic phospholipase A(2) gene

Pancreatic phospholipase A(2) (PLA(2)) is involved with the hydrolysis of phospholipids into lysophospholipids and unesterified fatty acids. The enzyme has been postulated to play a key role in lipid absorption by intestinal absorptive cells as well as in the regulation of secretin release from intestinal endocrine cells. This manuscript reports the genomic organization and the primary sequence of the mouse PLA(2). The results showed that the mouse PLA(2) gene contains four exons interspersed by three introns, spans over 8kb in length, and is considerably larger than the human PLA(2) gene. The mouse PLA(2) protein contains 146 amino acid residues, including the signal peptide. The mouse protein is highly homologous to the rat, dog, and human enzyme, but is two residues shorter than the human protein. Mouse PLA(2) message is synthesized predominantly in the pancreas, but the lung also contains low levels of PLA(2) mRNA.