Involvement of a serine esterase in oxidant‐mediated activation of phospholipase A2 in pulmonary endothelium

FEBS Letters

Michael, John R.²  Chakraborti, Sajal¹ 

[1] Department of Biochemistry and Biophysics, University of Kalyani, Kalyani 741235, India;Department of Medicine, University of Utah Health Sciences Centre, Salt Lake City, UT 84132, USA

关键词: Serine esterase;    Phospholipase A2;    Hydrogen peroxide;    Oxidant;    Antiproteases;    Trypsin;    Endothelial cells;    PMSF;    phenylmethylsulfonyl fluoride;    DEP;    diisopropyl fluorophosphate;    TAME;    p-tosyl-L-arginine methylester;    H2O2;    hydrogen peroxide;    α1-PI;    alpha;    proteinase inhibitor;    AA;    arachidonic acid;    PBS;    phosphate buffered saline;    PLA2;    Phospholipase A2;   

DOI  :  10.1016/0014-5793(91)80389-K

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Exposure of bovine pulmonary arterial endothelial cells to 1 mM H₂O₂ stimulated associated TAME-esterase and PLA₂ activities. Pretreatment with the serine esterase inhibitors: PMSF (1 mM), DFP (1 mM), and α₁-PI (1 mg/ml) inhibited H₂O₂-induced stimulation of TAME-esterase and PLA₂ activities. The TAME-esterase and PLA₂ activities under H₂O₂ exposure were determined to be linearly correlated. Affinity labeling of the endothelial cell membrane with [³H]DFP demonstrated that the serine esterase resides in a protein having molecular weight of 29000 daltons (29 kDa) which is similar to that of elastase. Treatment of the endothelial cell homegenate with trypsin (1 μ/ml) also stimulated PLA₂ activity.

【 授权许可】

Unknown