【 摘 要 】
Given the potent hydrolyzing activity toward phosphatidylcholine, group X secretory phospholipase A2 (sPLA2-X) elicits a marked release of arachidonic acid linked to the potent production of lipid mediators in various cell types. We have recently shown that sPLA2-X can also act as a ligand for mouse phospholipase A2 receptor (PLA2R). Here, we found that sPLA2-X was internalized and degraded via binding to PLA2R associated with the diminished prostaglandin E2 (PGE2) formation in PLA2R-expressing Chinese hamster ovary (CHO) cells compared to CHO cells. Indirect immunocytochemical analysis revealed that internalized sPLA2-X was co-localized with PLA2R in the punctate structures in PLA2R-expressing CHO cells. Moreover, in mouse osteoblastic MC3T3-E1 cells that endogenously express the PLA2R, the internalized sPLA2-X was localized in lysosomes. These findings demonstrate that PLA2R acts as a clearance receptor for sPLA2-X to suppress its strong enzymatic activity.
【 授权许可】
Unknown
【 预 览 】
Files | Size | Format | View |
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RO201912020311271ZK.pdf | 320KB | download |