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Identification of group X secretory phospholipase A 2 as a natural ligand for mouse phospholipase A 2 receptor
Author(s) -
Yokota Yasunori,
Higashino Ken-ichi,
Nakano Kazumi,
Arita Hitoshi,
Hanasaki Kohji
Publication year - 2000
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(00)01848-2
Subject(s) - phospholipase , phospholipase c , recombinant dna , receptor , phospholipase a , biology , ligand (biochemistry) , phospholipase a2 , microbiology and biotechnology , biochemistry , gene , chemistry , enzyme
Phospholipase A 2 receptor (PLA 2 R) mediates various biological responses elicited by group IB secretory phospholipase A 2 (sPLA 2 ‐IB). The recently cloned group X sPLA 2 (sPLA 2 ‐X) possesses several structural features characteristic of sPLA 2 ‐IB. Here, we detected a specific binding site of sPLA 2 ‐X in mouse osteoblastic MC3T3‐E 1 cells. Cross‐linking experiments demonstrated its molecular weight (180 kDa) to be similar to that of PLA 2 R. In fact, sPLA 2 ‐X was found to bind the recombinant PLA 2 R expressed in COS‐7 cells, and its specific binding detected in mouse lung membranes was abolished by the deficiency of PLA 2 R. These findings demonstrate sPLA 2 ‐X to be one of the high‐affinity ligands for mouse PLA 2 R.