Distinct arachidonate-releasing functions of mammalian secreted phospholipase A2s in human embryonic kidney 293 and rat mastocytoma RBL-2H3 cells through heparan sulfate shuttling and external plasma membrane mechanisms.

@article{Murakami2001DistinctAF,
  title={Distinct arachidonate-releasing functions of mammalian secreted phospholipase A2s in human embryonic kidney 293 and rat mastocytoma RBL-2H3 cells through heparan sulfate shuttling and external plasma membrane mechanisms.},
  author={Makoto Murakami and Rao S Koduri and Atsushi Enomoto and Satoko Shimbara and Mineaki Seki and Kumiko Yoshihara and Alan G. Singer and Emmanuel Valentin and Farideh Ghomashchi and G{\'e}rald Lambeau and Michael H Gelb and Ichiro Kudo},
  journal={The Journal of biological chemistry},
  year={2001},
  volume={276 13},
  pages={10083-96}
}
We analyzed the ability of a diverse set of mammalian secreted phospholipase A(2) (sPLA(2)) to release arachidonate for lipid mediator generation in two transfected cell lines. In human embryonic kidney 293 cells, the heparin-binding enzymes sPLA(2)-IIA, -IID, and -V promote stimulus-dependent arachidonic acid release and prostaglandin E(2) production in a manner dependent on the heparan sulfate proteoglycan glypican. In contrast, sPLA(2)-IB, -IIC, and -IIE, which bind weakly or not at all to… CONTINUE READING
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