Sci. STKE, 23 April 2002
Phospholipase A2 Endogenous Antivenom
Higashino et al. found that in mammals (specifically mice), as in venomous snakes, there is a circulating inhibitor of secreted phospholipase A2 (PLA2). Secreted PLA2 can activate cellular signaling pathways through interaction with the PLA2 receptor (PLA2R) or by hydrolyzing membrane lipids to release various eicosanoid species. The inhibitor was a secreted form of the extracellular portion of PLA2 receptor (sPLA2R). Purified sPLA2R from mouse serum inhibited the enzymatic activity of mouse PLA2 and inhibited specific binding of PLA2 to the PLA2R expressed in transfected Chinese hamster ovary (CHO) cells. The mechanism of release of the sPLA2R appeared to involve metalloproteases, because the addition of a metalloprotease inhibitor to the PLA2R-expressing CHO cells inhibited release of sPLA2R into the culture medium. Thus, the biological activity of secreted PLA2 may be regulated by the presence of this sPLA2R in vivo.
K.-i. Higashino, Y. Yokota, T. Ono, S. Kamitani, H. Arita, K. Hanasaki, Identification of a soluble form of phospholipase A2 receptor as a circulating endogenous inhibitor for secretory phospholipase A2. J. Biol. Chem. 277, 13583-13588 (2002). [Abstract] [Full Text]
Citation: Endogenous Antivenom. Sci. STKE 2002, tw153 (2002).
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