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Structure and function of phosphatidylserine-specific phospholipase A1
Junken Aoki1, Yuki Nagai, Hiroyuki Hosono
1Graduate School of Pharmaceutical Sciences, The University of Tokyo, 7-3-1 Hongo, Bunkyo, Tokyo 113-0033, Japan. jaoki@mol.f.u-tokyo.ac.jp
Biochimica Et Biophysica Acta
|June 19, 2002
Summary
Phospholipase A1 (PLA1) enzymes hydrolyze phospholipids, producing lipid mediators. The study identifies a PLA1 subfamily within the lipase family, highlighting structural features and roles in cell signaling.
Area of Science:
- Biochemistry
- Enzymology
- Lipid Metabolism
Background:
- Phospholipase A1 (PLA1) enzymes hydrolyze phospholipids, generating 2-acyl-lysophospholipids.
- Limited PLA1s have been purified and cloned, despite widespread activity detection.
- Known PLA1s include phosphatidylserine (PS)-specific PLA1 (PS-PLA1) and phosphatidic acid (PA)-preferential PLA1 (PA-PLA1).
Purpose of the Study:
- To characterize the structural and functional aspects of PLA1 enzymes.
- To investigate the role of PLA1 in lysophospholipid mediator production.
- To identify the PLA1 subfamily within the broader lipase family.
Main Methods:
- Purification and cloning of PLA1 enzymes.
- Structural analysis through sequence alignment with lipase family members.
- Enzymatic activity assays under physiological conditions.
Main Results:
- PLA1 enzymes possess unique structural features: extremely short lids and deleted beta9 loops.
- PS-PLA1 efficiently hydrolyzes phosphatidylserine (PS) on apoptotic cells and activated platelets.
- Production of 2-acyl-lysophosphatidylserine (lysoPS), a key lipid mediator, was confirmed.
Conclusions:
- PLA1 enzymes represent a distinct subfamily within the lipase family.
- PLA1 plays a significant role in generating bioactive lysophospholipid mediators.
- PS-PLA1's activity on cell surfaces suggests roles in cellular signaling and apoptosis.