分泌型IIA磷脂酶A2（sPLA2-IIA）作为甘草甜素（GL）结合蛋白的特性以及GL在体外对CK-II介导的sPLA2-IIA活性刺激的抑制作用。

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.

作者信息

Shimoyama Y, Sakamoto R, Akaboshi T, Tanaka M, Ohtsuki K

机构信息

Laboratory of Genetical Biochemistry, School of Allied Health Sciences, Kitasato University, Sagamihara, Japan.

出版信息

Biol Pharm Bull. 2001 Sep;24(9):1004-8. doi: 10.1248/bpb.24.1004.

DOI:10.1248/bpb.24.1004

PMID:11558558

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.

摘要

通过肝素亲和色谱法和甘草酸（GL）亲和柱色谱法（高效液相色谱法），从类风湿性关节炎患者的滑液中选择性纯化出一种GL结合型磷脂酶A2（gbPLA2）。这种纯化的gbPLA2被鉴定为分泌型IIA磷脂酶A2（sPLA2-IIA），因为它与抗sPLA2-IIA血清发生交叉反应。纯化的sPLA2-IIA的活性被甘草次酸（GA）和一种GA衍生物（oGA）以剂量依赖的方式抑制，但它对GA比对GL更敏感。此外，还发现：（i）纯化的sPLA2-IIA在体外被酪蛋白激酶II（CK-II）磷酸化；（ii）这种磷酸化导致PLA2活性显著增强；（iii）浓度为GL十分之一的oGA抑制CK-II介导的sPLA2-IIA活性增强。这些结果表明：（i）sPLA2-IIA是一种GL结合蛋白；（ii）CK-II在体外介导其PLA2活性的增强。