| First Author | Yokota Y | Year | 2001 |
| Journal | FEBS Lett | Volume | 509 |
| Issue | 2 | Pages | 250-4 |
| PubMed ID | 11741598 | Mgi Jnum | J:73331 |
| Mgi Id | MGI:2154891 | Doi | 10.1016/s0014-5793(01)03173-8 |
| Citation | Yokota Y, et al. (2001) Clearance of group X secretory phospholipase A(2) via mouse phospholipase A(2) receptor. FEBS Lett 509(2):250-4 |
| abstractText | Given the potent hydrolyzing activity toward phosphatidylcholine, group X secretory phospholipase A(2) (sPLA(2)-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 sPLA(2)-X can also act as a ligand for mouse phospholipase A(2) receptor (PLA(2)R). Here, we found that sPLA(2)-X was internalized and degraded via binding to PLA(2)R associated with the diminished prostaglandin E(2) (PGE(2)) formation in PLA(2)R-expressing Chinese hamster ovary (CHO) cells compared to CHO cells. Indirect immunocytochemical analysis revealed that internalized sPLA(2)-X was co-localized with PLA(2)R in the punctate structures in PLA(2)R-expressing CHO cells. Moreover, in mouse osteoblastic MC3T3-E(1) cells that endogenously express the PLA(2)R, the internalized sPLA(2)-X was localized in lysosomes. These findings demonstrate that PLA(2)R acts as a clearance receptor for sPLA(2)-X to suppress its strong enzymatic activity. |
