Induction of hepatoma cells migration by phosphoglucose isomerase/autocrine motility factor through the upregulation of matrix metalloproteinase-3.

Abstract

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.

• Authors: Feng-Ling Yu, Ming-Huei Liao, Jeng-Woei Lee, Wen-Ling Shih
• Journal: Biochemical and biophysical research communications (Biochem Biophys Res Commun) Vol. 314 Issue 1 Pg. 76-82 (Jan 30 2004) ISSN: 0006-291X [Print] United States
• PMID: 14715248 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)

Chemical References

• Matrix Metalloproteinase 3
• Glucose-6-Phosphate Isomerase

Topics

• Carcinoma, Hepatocellular (enzymology, pathology, physiopathology)
• Cell Movement
• Gene Expression Regulation, Enzymologic
• Gene Expression Regulation, Neoplastic
• Glucose-6-Phosphate Isomerase (metabolism)
• Humans
• Liver Neoplasms (metabolism, pathology, physiopathology)
• Matrix Metalloproteinase 3 (metabolism)
• Tumor Cells, Cultured
• Up-Regulation