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Clearance of group X secretory phospholipase A 2 via mouse phospholipase A 2 receptor
Author(s) -
Yokota Yasunori,
Notoya Mitsuru,
Higashino Ken-ichi,
Ishimoto Yoshikazu,
Nakano Kazumi,
Arita Hitoshi,
Hanasaki Kohji
Publication year - 2001
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(01)03173-8
Subject(s) - chinese hamster ovary cell , phospholipase a2 , arachidonic acid , receptor , phospholipase , phospholipase d , phospholipase a , phosphatidylcholine , hamster , biology , phospholipase c , enzyme , prostaglandin , biochemistry , microbiology and biotechnology , phospholipid , membrane
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.