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Survivin may be a member of the inhibitor of apoptosis (IAP) family. The survivin protein functions to inhibit caspase activation, thereby resulting in negative regulation of apoptosis or programmed necrobiosis . This has been shown by disruption of survivin induction pathways resulting in increase in apoptosis and reduce in tumour growth. The survivin protein is expressed highly in most human tumours and fetal tissue, but is totally absent in terminally differentiated cells. These data suggest survivin might provide a replacement target for cancer therapy that might discriminate between transformed and normal cells. Survivin expression is additionally highly regulated by the cell cycle and is merely expressed within the G2-M phase. it's known that Survivin localizes to the mitotic spindle by interaction with tubulin during mitosis and should play a contributing role in regulating mitosis. The molecular mechanisms of survivin regulation are still not well understood, but regulation of survivin seems to be linked to the p53 protein. It is also an immediate target gene of the Wnt pathway and is upregulated by beta-catenin.


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