Mammalian genomes encode genes for more than 30 phospholipase A
2s (PLA
2s) or related enzymes, which are subdivided into several subgroups based on their structures, catalytic mechanisms, localizations and evolutionary relationships. More than one third of the PLA
2 enzymes
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Mammalian genomes encode genes for more than 30 phospholipase A
2s (PLA
2s) or related enzymes, which are subdivided into several subgroups based on their structures, catalytic mechanisms, localizations and evolutionary relationships. More than one third of the PLA
2 enzymes belong to the secreted PLA
2 (sPLA
2) family, which consists of low-molecular-weight, Ca
2+-requiring extracellular enzymes, with a His-Asp catalytic dyad. Individual sPLA
2 isoforms exhibit unique tissue and cellular localizations and enzymatic properties, suggesting their distinct pathophysiological roles. Recent studies using transgenic and knockout mice for several sPLA
2 isoforms, in combination with lipidomics approaches, have revealed their distinct contributions to various biological events. Herein, we will describe several examples of sPLA
2-mediated phospholipid metabolism
in vivo, as revealed by integrated analysis of sPLA
2 transgenic/knockout mice and lipid mass spectrometry. Knowledge obtained from this approach greatly contributes to expanding our understanding of the sPLA
2 biology and pathophysiology.
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