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Involvement of a serine esterase in oxidant‐mediated activation of phospholipase A 2 in pulmonary endothelium
Author(s) -
Chakraborti Sajal,
Michael John R.
Publication year - 1991
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(91)80389-k
Subject(s) - esterase , serine , pmsf , elastase , chemistry , biochemistry , trypsin , endothelial stem cell , enzyme , microbiology and biotechnology , biology , in vitro
Exposure of bovine pulmonary arterial endothelial cells to 1 mM H 2 O 2 stimulated associated TAME‐esterase and PLA 2 activities. Pretreatment with the serine esterase inhibitors: PMSF (1 mM), DFP (1 mM), and α 1 ‐PI (1 mg/ml) inhibited H 2 O 2 ‐induced stimulation of TAME‐esterase and PLA 2 activities. The TAME‐esterase and PLA 2 activities under H 2 O 2 exposure were determined to be linearly correlated. Affinity labeling of the endothelial cell membrane with [ 3 H]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 PLA 2 activity.