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J Biol Chem, Vol. 274, Issue 48, 34203-34211, November 26, 1999

Purified Group X Secretory Phospholipase A2 Induced Prominent Release of Arachidonic Acid from Human Myeloid Leukemia Cells

Kohji Hanasaki, Takashi Ono, Akihiko Saiga, Yasuhide Morioka, Minoru Ikeda, Keiko Kawamoto, Ken-ichi Higashino, Kazumi Nakano, Katsutoshi Yamada, Jun Ishizaki, and Hitoshi Arita

From the Shionogi Research Laboratories, Shionogi and Co., Ltd., Sagisu 5-12-4, Fukushima-ku, Osaka 553-0002, Japan

Group X secretory phospholipase A2 (sPLA2-X) possesses several structural features characteristic of both group IB and IIA sPLA2s (sPLA2-IB and -IIA) and is postulated to be involved in inflammatory responses owing to its restricted expression in the spleen and thymus. Here, we report the purification of human recombinant COOH-terminal His-tagged sPLA2-X, the preparation of its antibody, and the purification of native sPLA2-X. The affinity-purified sPLA2-X protein migrated as various molecular species of 13-18 kDa on SDS-polyacrylamide gels, and N-glycosidase F treatment caused shifts to the 13- and 14-kDa bands. NH2-terminal amino acid sequencing analysis revealed that the 13-kDa form is a putative mature sPLA2-X and the 14-kDa protein possesses a propeptide of 11 amino acid residues attached at the NH2 termini of the mature protein. Separation with reverse-phase high performance liquid chromatography revealed that N-linked carbohydrates are not required for the enzymatic activity and pro-sPLA2-X has a relatively weak potency compared with the mature protein. The mature sPLA2-X induced the release of arachidonic acid from phosphatidylcholine more efficiently than other human sPLA2 groups (IB, IIA, IID, and V) and elicited a prompt and marked release of arachidonic acid from human monocytic THP-1 cells compared with sPLA2-IB and -IIA with concomitant production of prostaglandin E2. A prominent release of arachidonic acid was also observed in sPLA2-X-treated human U937 and HL60 cells. Immunohistochemical analysis of human lung preparations revealed its expression in alveolar epithelial cells. These results indicate that human sPLA2-X is a unique N-glycosylated sPLA2 that releases arachidonic acid from human myeloid leukemia cells more efficiently than sPLA2-IB and -IIA.

Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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