Biological and Pharmaceutical Bulletin
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ISSN-L : 0918-6158
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Characterization of Secretory Type IIA Phospholipase A2 (sPLA2-IIA) as a Glycyrrhizin (GL)-Binding Protein and the GL-Induced Inhibition of the CK-II-Mediated Stimulation of sPLA2-IIA Activity in Vitro
Yoshihito SHIMOYAMARyoko SAKAMOTOTohru AKABOSHIMichi TANAKAKenzo OHTSUKI
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2001 Volume 24 Issue 9 Pages 1004-1008

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Abstract

By means of heparin-affinity and glycyrrhizin (GL)-affinity column chromatographies (HPLC), a GL-binding phospholipase A2 (gbPLA2) was selectively purified from the synovial fluids of patients with rheumatoid arthritis. This purified gbPLA2 was identified as a secretory type IIA PLA2 (sPLA2-IIA) since it was crossreacted with anti-sPLA2-IIA serum. The activity of purified sPLA2-IIA was inhibited by glycyrrhetinic acid (GA) and a GA derivative (oGA) in a dose-dependent manner, but it was more sensitive to GA than GL. Furthermore, it was found that (i) purified sPLA2-IIA is phosphorylated by casein kinase II (CK-II) in vitro; (ii) this phosphorylation induces in a significant stimulation of PLA2 activity; and (iii) oGA at one-tenth the concentration of GL inhibits the CK-II-mediated stimulation of sPLA2-IIA activity. These results show that (i) sPLA2-IIA is a GL-binding protein; and (ii) CK-II mediates stimulation of its PLA2 activity in vitro.

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© 2001 The Pharmaceutical Society of Japan
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