Novel survivin-related members of the inhibitor of apoptosis (IAP) family

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The inhibitor of apoptosis proteins (IAPs) have first been described as baculovirus-encoded proteins that upon infection of insect cells inhibit the host's apoptotic defense mechanisms and enhance viral replication. Recently, several cellular members have been identified in baker's and fission yeast, in the nematode Caenorhabditis elegans, the fruitfly Drosophila melanogaster and several mammals.^1,2 The common feature of IAPs is that they bear one to three domains of about 70 amino acids in length known as BIRs (baculovirus inhibitory repeats) that inhibit certain caspases and therefore confer anti-apoptotic ability to the cell. Attention was focused on IAP research with the recent discovery of the survivin gene,³ a human IAP with a single BIR motif. Survivin is expressed in fetal tissues and is not detectable in most adult tissues, but re-expressed in most common human tumors.⁴ For several neoplastic diseases such as neuroblastoma, gastric and colorectal carcinoma, the re-expression of survivin has been suggested to be a prognostic factor.⁵ Survivin inhibits apoptosis induced by anti-cancer drugs and is able to inhibit CD95- and caspase-induced apoptosis, probably by binding to caspase-3 and -7.⁶ In addition to its anti-apoptotic ability, survivin seems to be involved in cell cycle regulation at the G2/M checkpoint.^7,8

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