Endogenous inhibitors of caspases

• Published in: Journal of clinical immunology Vol. 19; no. 6; pp. 388 - 398
• Main Authors: DEVERAUX, Q. L, STENNICKE, H. R, SALVESEN, G. S, REED, J. C
• Format: Journal Article
• Language: English
• Published: New York, NY Kluwer/Plenum 01-11-1999; Springer Nature B.V
• Subjects: Ageing, cell death; Animals; Apoptosis; Biological and medical sciences; Caspase; Caspase Inhibitors; Caspases - physiology; Cell death; Cell physiology; Cowpox; Cysteine Proteinase Inhibitors - physiology; Fundamental and applied biological sciences. Psychology; Humans; IAP protein; Inhibitor of Apoptosis Proteins; Molecular and cellular biology; Proteins - physiology; Signal Transduction; Viral Proteins - physiology; X-Linked Inhibitor of Apoptosis Protein; Human; Peptidases; Enzyme; Animal; Cysteine endopeptidases; Cell biology; Caspase; Hydrolases; Inhibitor; Apoptosis
• ISSN: 0271-9142; 1573-2592
• DOI: 10.1023/A:1020502800208

Caspases are cysteine proteases that are specific for aspastic acid residues. These enzymes have been extensively characterized as integral and highly conserved components of a variety of cell death programs. Cowpox and several insect viruses have evolved mechanisms that counter host cell suicide by encoding proteins that directly inhibit caspases-thereby allowing propagation of viral progeny within the host cell. It has only recently been elucidated, however, that endogenous cellular inhibitors of the caspases exist. To date five members of the inhibitor of apoptosis (IAP) family of proteins has been identified in humans and at least three of these have been shown directly to inhibit specific caspases. Thus, members of the IAP family of proteins are the only endogenous inhibitors of caspases known in mammals. Here we discuss the caspase and IAP families of proteins and review the data concerning their relationship.