Human Caspases: Activation, Specificity, and Regulation*

By C. Pop, G. Salvesen. 2009

751 citations recorded by the source corpus.

Caspases are intracellular proteases that propagate programmed cell death, proliferation, and inflammation. Activation of caspases occurs by a conserved mechanism subject to strict cellular regulation. Once activated by a specific stimulus, caspases execute limited proteolysis of downstream substrates to trigger a cascade of events that culminates in the desired biological response. Much has been learned of the mechanisms that govern the activation and regulation of caspases, and this minireview provides an update of these areas. We also delineate substantial gaps in knowledge of caspase function, which can be approached by techniques and experimental paradigms that are currently undergoing development.

Subfields: Epidemiology, Immunology, Molecular Biology

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Citations in the corpus

Apoptosis as anticancer mechanism: function and dysfunction of its modulators and targeted therapeutic strategies (2016, background): “Considering that proteolysis is an irreversible process, strict control of caspases-mediated proteolytic cleavage is imperative to prevent inappropriate cell destruction [41].”
Chondrocyte Apoptosis in the Pathogenesis of Osteoarthritis (2015, background): “At present, 14 mammalian caspases have been identified, and they are classified into initiator caspases (caspases-2, -8, -9 and -10), effector caspases (caspases-3, -6 and -7) and the inflammatory caspases (caspases-1, -4, -5, -11, -12 and -13) (Table 1) [15,16].”
Focus on Extracellular Vesicles: Introducing the Next Small Big Thing (2016, background): “This is predominantly performed by caspases; cysteine proteases designed for protein cleavage rather than degradation, which are normally present within the cell as catalytically inactive zymogens [105].”
Pattern Recognition Receptors and the Host Cell Death Molecular Machinery (2018, background): “Caspases are produced as an inactive pro-form (zymogen) that can be activated either through proteolytic processing by upstream caspases (in the case of caspases-3, -6, and-7) or via dimerization in the context of multimolecular platforms, such as the apoptosome (caspase9), the DISC (death-inducing ”
PROSPER: An Integrated Feature-Based Tool for Predicting Protease Substrate Cleavage Sites (2012, background): “As expected, one of the hallmarks of the substrate specificities of caspases is that they preferentially cleave after Asp residues at both P1 and P4 positions (Figure 2), forming the well-known canonical DXXD motif [65,66].”
IAPs: from caspase inhibitors to modulators of NF-κB, inflammation and cancer (2010, background): “Generally, caspases are ubiquitously expressed as inactive zymogens, however, in response to specific death stimuli, caspases are activated in cascades of auto-stimulation and trans-stimulatio”