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Secreted phospholipase A(2) induces vascular endothelial cell migration
M T Rizzo1, E Nguyen, M Aldo-Benson
1Signal Transduction Laboratory, Methodist Research Institute and Arthritis Care Center, Clarian Health, Indianapolis, IN 46201, USA. mrizzo@clarian.com
Blood
|November 23, 2000
Summary
Secreted phospholipase A(2) (sPLA(2)) promotes endothelial cell migration, a process crucial for various cellular functions. This effect is dependent on sPLA(2) catalytic activity and its hydrolytic products.
Area of Science:
- Cell Biology
- Biochemistry
- Physiology
Background:
- Secreted phospholipase A(2) (sPLA(2)) is known to regulate diverse cellular functions.
- The specific role of sPLA(2) in endothelial cell (EC) migration requires further elucidation.
Purpose of the Study:
- To investigate the potential role of sPLA(2) in regulating endothelial cell migration.
- To determine the mechanisms underlying sPLA(2)-induced EC migration.
Main Methods:
- Utilized a modified Boyden chamber assay to assess bovine aortic endothelial cell (BAEC) migration.
- Investigated the dose- and time-dependent effects of various sPLA(2)s and their hydrolytic products.
- Employed a catalytic site mutant of pancreatic sPLA(2) and an sPLA(2) inhibitor (p-bromophenacyl bromide) to assess the role of enzymatic activity.
Main Results:
- sPLA(2) significantly increased BAEC migration in a time- and dose-dependent manner.
- Various sPLA(2) enzymes, including bee venom and pancreatic PLA(2)s, stimulated EC migration.
- sPLA(2) inhibition and the use of a catalytic mutant reduced EC migration, while hydrolytic products like arachidonic acid stimulated it.
Conclusions:
- sPLA(2) plays a physiological role in inducing endothelial cell migration.
- The observed effects of sPLA(2) on EC migration are mediated, at least in part, by its catalytic activity.
- sPLA(2) hydrolytic products contribute to EC migration.
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