Yu Feng-Ling, Liao Ming-Huei, Lee Jeng-Woei, Shih Wen-Ling
Department of Veterinary Medicine, National Pingtung University of Science and Technology, Pingtung, Taiwan, ROC.
Biochem Biophys Res Commun. 2004 Jan 30;314(1):76-82. doi: 10.1016/j.bbrc.2003.12.056.
Phosphoglucose isomerase/autocrine motility factor (PGI/AMF) catalyzes the isomerization between glucose-6-phosphate and fructose-6-phosphate, and is involved in cytokine activity, mitogenesis, differentiation, oncogenesis, and tumor metastasis. Presently, we demonstrate that exogenous PGI/AMF stimulates the migration of Huh7 and HepG2 hepatoma cells, but not Hep3B cells. Inhibition of PGI/AMF by PGI/AMF specific inhibitor 5-phospho-D-arabinonate markedly repressed the cellular migration. RT-PCR was used to examine the expression profile of matrix metalloproteinases (MMPs). MMP-3 transcripts, protein level, and secreted form were significantly upregulated in PGI/AMF-treated Huh7 and HepG2 cells, but not in Hep3B cells. MMP-3 inhibition abolished the PGI/AMF-induced cell motility. The observations are consistent with a downstream mediation role of MMP-3 in PGI/AMF-stimulated tumor cell metastasis.
磷酸葡萄糖异构酶/自分泌运动因子（PGI/AMF）催化6-磷酸葡萄糖与6-磷酸果糖之间的异构化反应，并参与细胞因子活性、有丝分裂、分化、肿瘤发生及肿瘤转移过程。目前，我们证明外源性PGI/AMF可刺激Huh7和HepG2肝癌细胞迁移，但对Hep3B细胞无此作用。PGI/AMF特异性抑制剂5-磷酸-D-阿拉伯糖抑制PGI/AMF后，显著抑制了细胞迁移。采用逆转录聚合酶链反应（RT-PCR）检测基质金属蛋白酶（MMPs）的表达谱。在PGI/AMF处理的Huh7和HepG2细胞中，MMP-3转录本、蛋白水平及分泌形式均显著上调，但在Hep3B细胞中未出现此现象。抑制MMP-3可消除PGI/AMF诱导的细胞运动。这些观察结果与MMP-3在PGI/AMF刺激的肿瘤细胞转移中起下游介导作用一致。
