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Published online before print June 6, 2008
Protein Science, DOI: 10.1110/ps.036145.108
 Copyright © 2008 The Protein Society
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For the Record

Chemically synthesized human survivin does not inhibit caspase-3

Changqing Li, Zhibin Wu, Min Liu, Marzena Pazgier, and Wuyuan Lu1

Institute of Human Virology University of Maryland School of Medicine

(RECEIVED April 30, 2008; ACCEPTED June 5, 2008)

Survivin is a member of the inhibitor of apoptosis protein (IAP) family that blocks cell death by inhibiting the caspase activation pathways. Over-expressed in all common human neoplasms but undetectable in most normal adult tissues, survivin confers tumor resistance to apoptosis and represents an ideal molecular target for therapeutic intervention. How survivin blocks apoptosis, however, has been a subject of intense debate, as evidenced by conflicting reports regarding whether or not survivin can directly bind and inactivate effector caspases. We chemically synthesized large amounts of highly pure human survivin of 142 amino acid residues using native chemical ligation, and functionally compared synthetic survivin and a recombinant XIAP - the most intensively studied member of the IAP family. Inhibition assays showed that while caspase-3 could be effectively inhibited by XIAP, survivin had no detectable inhibitory activity against the enzyme even at concentrations several thousand fold higher than XIAP. Our finding supports the premise that survivin does not directly inhibit effector caspases.

Keywords: Enzymes; Enzyme Inhibitors; Methods of protein and peptide synthesis; Synthesis of Peptides and Proteins

1 E-mail: wlu{at}ihv.umaryland.edu


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