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Abstract
Livin, also called melanoma inhibitor of apoptosis protein (IAP) or kidney IAP, is a member of the IAP family of caspase inhibitors that selectively binds the endogenous IAP antagonist SMAC and caspase-3, caspase-7, and caspase-9. As such, Livin inhibits apoptosis, and its overexpression renders malignant cells resistant to chemotherapy. Therefore, inhibitors of Livin could be useful adjuncts to chemotherapy in the treatment of malignancies. This review will discuss Livin as a potential therapeutic target and strategies for its inhibition, including antisense oligonucleotides, small-molecule inhibitors, and immune-mediated approaches.
Highlights
Caspases are cysteine proteases and are the executioners of apoptosis
Membership in the Inhibitor of apoptosis proteins (IAP) family is based on the presence of at least one baculovirus IAP repeat (BIR) domain (1, 3 – 5)
The BIR domain is required for the antiapoptotic activity of IAPs, but not all proteins with BIR domains have antiapoptotic functions and are part of the IAP family [6]
Summary
Membership in the IAP family is based on the presence of at least one baculovirus IAP repeat (BIR) domain (1, 3 – 5). Livin is similar to Survivin in that it contains only one BIR domain, sequence alignment studies predicted that this IAP would function more like XIAP or c-IAP 1/2. Using the known nuclear magnetic resonance structures of XIAP and c-IAP-1, Vucic et al [8] developed a virtual three-dimensional model of the BIR domain of Livin (MLIAP). According to their model, the Livin BIR has a secondary structure of four a helices and a three-stranded h sheet. Livin and survivin have only one BIR domain, and studies have compared the structure and function of these IAP family members. Consistent with its role in cell division, survivin localizes to components of the mitotic apparatus [1]
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