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Melatonin prevents nitric oxide‐induced apoptosis by increasing the interaction between 14‐3‐3β and p‐Bad in SK‐N‐MC cells
Author(s) -
Choi SeungIl,
Joo SeongSoo,
Yoo YeongMin
Publication year - 2008
Publication title -
journal of pineal research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.881
H-Index - 131
eISSN - 1600-079X
pISSN - 0742-3098
DOI - 10.1111/j.1600-079x.2007.00494.x
Subject(s) - melatonin , apoptosis , nitric oxide , cytosol , mitochondrion , cytochrome c , protein kinase b , biology , programmed cell death , cgmp dependent protein kinase , medicine , endocrinology , microbiology and biotechnology , phosphorylation , protein kinase a , biochemistry , enzyme , cyclin dependent kinase 2
  The anti‐apoptotic effect of melatonin has been described in vivo and in vitro. A previous report has revealed that melatonin suppresses nitric oxide (NO)‐induced apoptosis via the induction of Bcl‐2 expression in PGT‐β pineal cells. To investigate the protective mechanism of melatonin on NO donor S ‐nitroso‐ N ‐acetyl‐penicillamine (SNAP)‐induced apoptosis, we examined the anti‐apoptotic upstream signaling pathway of Bcl‐2 in the human neuroblastoma cell line SK‐N‐MC. The flow cytometry results revealed that apoptosis occurred in NO‐treated cells, while cell death was inhibited by pretreatment with melatonin (100 μ m ). In addition, decreased Bax expression, increased Bcl‐2 expression and a decreased release of cytochrome c into the cytosol were observed in the melatonin‐pretreated SK‐N‐MC cells. We also found that melatonin treatment induced the activation of Akt/PKB and the phosphorylation of GSK3α/β and Bad. Furthermore, melatonin treatment not only increased the protein–protein interactions between 14‐3‐3β and p‐Bad, but also decreased the release of cytochrome c from mitochondria into the cytosol. In summary, the protective effect of melatonin against NO‐induced apoptosis was mediated by the inhibition of Bad translocation from the cytosol to the mitochondria by the induction of protein–protein interactions between 14‐3‐3β and p‐Bad.

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