Salvianolic acid A positively regulates PTEN protein level and inhibits growth of A549 lung cancer cells

• Published in: Biomedical reports Vol. 1; no. 2; pp. 213 - 217
• Main Authors: BI, LEI, CHEN, JIANPING, YUAN, XIAOJING, JIANG, ZEQUN, CHEN, WEIPING
• Format: Journal Article
• Language: English
• Published: England D.A. Spandidos 01.03.2013; Spandidos Publications; Spandidos Publications UK Ltd
• Subjects: Akt phosphorylation; AKT protein; Apoptosis; Autophagy; Cancer; Care and treatment; Cell cycle; Cell growth; Cell regulation; Fluorides; Health aspects; Homology; Kinases; Lung cancer; Membrane permeability; Mitochondria; Phosphatase; phosphatase and tensin homolog; Phosphatases; Phosphorylation; Plant extracts; Proteins; PTEN protein; Sage; Salvia miltiorrhiza; salvianolic acid A; Tensin; China; salvianolic acid A; apoptosis; Akt phosphorylation; phosphatase and tensin homolog
• ISSN: 2049-9434; 2049-9442
• DOI: 10.3892/br.2012.33

Salvianolic acid A (Sal A) is an effective compound extracted from Salvia miltiorrhiza which has been used in the treatment of various diseases. Preliminary data indicate that Sal A treatment has a specific anti-lung cancer effect. However, the manner in which Sal A regulates cancer growth remains unknown. In this study, the A549 lung cancer cell line and its response to Sal A treatment was examined. Results showed that Sal A treatment significantly decreased A549 cell growth, promoted partial apoptosis and increased mitochondrial membrane permeability. Western blot analysis showed that Sal A upregulated the phosphatase and tensin homolog (PTEN) protein level, while consistently downregulating Akt phosphorylation. These results indicate that Sal A negatively mediates A549 lung cancer cell line growth or apoptosis, most likely by positively regulating PTEN protein level.