Anti-metastatic effect of cantharidin in A549 human lung cancer cells

• Published in: Archives of pharmacal research Vol. 36; no. 4; pp. 479 - 484
• Main Authors: Kim, Young Min, Ku, Min Jeong, Son, Young-Jin, Yun, Jung-Mi, Kim, Seong Hwan, Lee, Sang Yeol
• Format: Journal Article
• Language: English
• Published: Heidelberg Pharmaceutical Society of Korea 01.04.2013; 대한약학회
• Subjects: anticarcinogenic activity; Antineoplastic Agents - pharmacology; blood; cantharidin; Cantharidin - pharmacology; Cell Line, Tumor; Cell Movement - drug effects; Dose-Response Relationship, Drug; extracellular matrix; gelatinase A; Humans; lung neoplasms; Lung Neoplasms - metabolism; Lung Neoplasms - pathology; Matrix Metalloproteinase 2 - metabolism; Matrix Metalloproteinase Inhibitors - pharmacology; Medicine; Meloidae; metastasis; neoplasm cells; Neoplasm Invasiveness; Pharmacology/Toxicology; Pharmacy; Phosphatidylinositol 3-Kinase - metabolism; Proto-Oncogene Proteins c-akt - metabolism; Research Article; signal transduction; Signal Transduction - drug effects; 약학; Cantharidin; Matrix metalloproteinases; Metastasis; Human lung cancer
• ISSN: 0253-6269; 1976-3786; 1976-3786
• DOI: 10.1007/s12272-013-0044-3

Cancer metastasis is represented by migration and invasion of cancer cells. Cancer cells invade into the blood or lymphatic vessels and this leads to the spread of cancer into the organs in distant sites. For cancer cells to migrate, extracellular matrix (ECM) must be degraded. Cantharidin, a compound derived from blister beetles, is known for its anti-cancer effect in several cancer cells. Here we report that cantharidin inhibits migration and invasion of A549 human lung cancer cell. We found that cantharidin inhibits activation of phosphatidylinositol 3-kinase/Akt signaling pathway. This leads to the selective attenuation of one of the gelatinases, matrix metalloproteinase 2, which can degrade components of ECM, and inhibits migration and invasion of A549 human lung cancer cell.