Action of human group IIa secreted phospholipase A2 on cell membranes. Vesicle but not heparinoid binding determines rate of fatty acid release by exogenously added enzyme.

@article{Koduri1998ActionOH,
  title={Action of human group IIa secreted phospholipase A2 on cell membranes. Vesicle but not heparinoid binding determines rate of fatty acid release by exogenously added enzyme.},
  author={Rao S Koduri and Sharon F Baker and Y Snitko and S K Han and Wonhwa Cho and David Wilton and Michael H Gelb},
  journal={The Journal of biological chemistry},
  year={1998},
  volume={273 48},
  pages={32142-53}
}
Human group IIa phospholipase A2 (hIIa-PLA2) is a highly basic protein that is secreted from a number of cells during inflammation and may play a role in arachidonate liberation and in destruction of invading bacteria. It has been proposed that rodent group IIa PLA2 is anchored to cell surfaces via attachment to heparan sulfate proteoglycan and that this interaction facilitates lipolysis. hIIa-PLA2 contains 13 lysines, 2 histidines, and 10 arginines that fall into 10 clusters. A panel of 26… CONTINUE READING

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