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- W1819561430 abstract "Group IID secretory phospholipase A2 (sPLA2-IID), a heparin-binding sPLA2 that is closely related to sPLA2-IIA, augments stimulus-induced cellular arachidonate release in a manner similar to sPLA2-IIA. Here we identified the residues of sPLA2-IID that are responsible for heparanoid binding, are and therefore essential for cellular function. Mutating four cationic residues in the C-terminal portion of sPLA2-IID resulted in abolition of its ability to associate with cell surface heparan sulfate and to enhance stimulus-induced delayed arachidonate release, cyclooxygenase-2 induction, and prostaglandin generation in 293 cell transfectants. As compared with several other group II subfamily sPLA2s, which were equally active on A23187- and IL-1-primed cellular membranes, sPLA2-IID showed apparent preference for A23187-primed membranes. Several human colon carcinoma cell lines expressed sPLA2-IID and sPLA2-X constitutively, the former of which was negatively regulated by IL-1. sPLA2-IID, but not other sPLA2 isozymes, was expressed in human cord blood-derived mast cells. The expression of sPLA2-IID was significantly altered in several tissues of mice with experimental inflammation. These results indicate that sPLA2-IID may be involved in inflammation in cell- and tissue-specific manners under particular conditions." @default.
- W1819561430 created "2016-06-24" @default.
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- W1819561430 date "2002-05-26" @default.
- W1819561430 modified "2023-10-01" @default.
- W1819561430 title "Group IID heparin-binding secretory phospholipase A<sub>2</sub>is expressed in human colon carcinoma cells and human mast cells and up-regulated in mouse inflammatory tissues" @default.
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- W1819561430 doi "https://doi.org/10.1046/j.1432-1033.2002.02938.x" @default.
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