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Serine/threonine protein kinase B (PKB/Akt) is involved in cell survivaland growth. Carboxyl-terminal modulator protein (CTMP), a novel Akt binding partner,prevents Akt activation at the plasma membrane in response to various stimuli,and thus possesses a tumor suppressor-like function. In a previous study, we havedemonstrated that CTMP inhibits tumor progression by facilitating apoptosis ina mouse lung cancer model. However, the precise mechanism of CTMP-induced apoptosisremains to be elucidated. The present study was performed to examine the roleof CTMP in mitochondrial-mediated apoptosis and regulation of mitochondrial functionin human lung carcinoma cells. Our results showed that CTMP altered mitochondrialmorphology and caused the release of cytochrome c by inhibiting OPA1 expression.Additionally, CTMP facilitated mitochondrial-mediated apoptosis by inhibitingheat-shock protein 27 and preventing cytochrome c interaction with Apaf-1. Ourdata suggest that CTMP may therefore play a critical role in mitochondrial-mediatedapoptosis in lung cancer cells.

Carboxyl-terminal modulator protein induces apoptosis by regulating mitochondrial function in lung cancer cells