Caspases

Abstract

Caspases are a family of cysteine proteases with a strict specificity for aspartate residues involved in inflammatory process and programmed cell death. This overview unit provides basic information on their structure, enzymatic activity, substrate specificity, activation,inhibition and their implication in pathologies. It is intended to be an overview for investigators that are unfamiliar with this family of enzymes but it is also applicable to scientists pursuing research in this field.

Who Benefits from Building Insurance Groups? A Welfare Analysis of Optimal Group Capital Management

“…In previous articles, certain capital allocation methods are investigated to what extent they meet certain axiomatic requirements. 55 In our approach, we endogenise capital allocation by determining the optimal equity capital at the subsidiary level by shareholder-value-maximisation and thus find an economic foundation for group-wide capital allocation.…”

Quantitative studies of caspase-3 catalyzed αII-spectrin breakdown

“…Caspase-3 is the most abundant caspase in cells (around 200 nM), with its activity often dominant over the activities of other members in the caspase family (Denault and Salvesen, 2001). While many proteins are cleaved during apoptosis, a prominent target of caspase-3 action is αII- and βII-spectrin, also known as fodrin (Moon and McMahon, 1990).…”

Characterization of the interactions between Caspase-9 and phosphatases PP1A and PP2A in apoptosis: applications as therapeutic target in cancer

“…There are 14 different types of caspases in mammals, but only 11 of them are present in humans. Caspases are produced in cells as inactive zymogens and they are constituted by a large subunit and a small subunit, showing all crystallographic structures solved from caspases the same basic fold (Denault and Salvesen, 2002a). .…”

“…Both domains are distantly related and are implicated in homophilic interactions with other proteins, allowing caspase zymogens to be recruited to protein complexes to promote their activation. Caspases containing CARD or DED domains are usually activated by proteolytic cleavage with the exception of Caspase-9, as described before (Denault and Salvesen, 2002a). Initiator caspases are activated through limited proteolysis when adaptor proteins interact with the N-terminal prodomains and promote caspase dimerization.…”

“…Hay 14 tipos diferentes de caspasas en mamíferos, pero sólo 11 de ellos están presentes en humanos. Las caspasas se producen en las células como zimógenos inactivos y están constituidas por una subunidad grande y una subunidad pequeña, de modo que todas las estructuras cristalográficas resueltas de caspasas muestran el mismo plegamiento básico (Denault and Salvesen, 2002a). Las caspasas activas generalmente se encuentran como dímeros de dominios catalíticos, principalmente unidos a través de interacciones hidrofóbicas.…”