Both Dimerization and Interdomain Processing Are Essential for Caspase-4 Activation.
From: Research Center for Proteineous Materials (RCPM) and Department of Bio-Materials Engineering, School of Medicine, Chosun University, Gwangju 501-759, Republic of Korea.
Biochemical and biophysical research communications
- Publish Date: May 2007
- ISSN: 0006-291X
- Volume: 356
- Issue: 4
- Pages: 1056-61
- Medium: Print
- Language: English
- Citation (JAMA): Karki Pratap, Dahal Giri Raj, Park Il-Seon, et al. Both Dimerization and Interdomain Processing Are Essential for Caspase-4 Activation.. Biochem. Biophys. Res. Commun. May 2007;356:1056-61
Abstract
A subgroup of caspase family of inflammatory caspases (-1, -4, -5, -11, and -12) play important role during cytokine maturation and inflammation but their regulation is not well understood as much as the initiator and effector caspases. Here, the biochemical mechanism of caspase-4 activation is elucidated. With citrate, a well-known kosmotrope to enhance the monomer-dimer transition, caspase-4 was activated approximately 40 times that was comparable with that of caspase-9 ( approximately 75-fold increments). The activation reaction was mainly bimolecular (n=1.67+/-0.04) for monomeric caspase-4. In addition, the interdomain cleavage was also responsible to activate caspase-4 more than 100-fold, again comparable with that of effector caspases where the proteolytic processing is considered as the sole activation mechanism. Thus, caspase-4 shows a novel activation mechanism of the synergism between dimerization and proteolysis that sharply differs from the established activation mechanism of dimerization for initiators and interdomain cleavage for effector caspases.
Mesh Headings (Keywords): Binding Sites, Caspases, Initiator, Citric Acid, Computer Simulation, Dimerization, Enzyme Activation, Models, Chemical, Protein Binding, Protein Structure, Tertiary
Check for Full Text / PubMed Unique Identifier (PMID): 17400183
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