Application of immobilized ATP to the study of NLRP inflammasomes
Section snippets
The NLRP inflammasome
The inflammasome is a protein complex and caspase-activating platform that drives inflammation and plays a crucial role in the innate immune response [[1], [2], [3], [4]]. Following stimulation by pathogen or danger/damage associated molecular patterns (PAMPs or DAMPs), inflammasome assembly induces the recruitment and autocatalytic cleavage of pro-caspases-1, 8 and 11, which are cysteine proteases and the key effectors of the inflammasome [[5], [6], [7]]. Activated caspases in turn regulate
NLRPs possess ATP-binding properties
Comparative sequence analyses reveal conservation within NACHT that designate NLRPs as members of the Signal Transduction ATPases with Numerous Domains (STAND) clade within the larger ATPases-Associated with various cellular Activities (AAA + ATPase) superfamily of proteins [[38], [39], [40]]. The vast majority of STAND ATPases are modular proteins, containing multiple domains involved in DNA or protein binding, signal transduction and scaffolding. STAND proteins have a conserved core,
Application of immobilized ATP supports to the study of NLRPs
Many different protein families possess biochemical properties in terms of amino acid sequence and three-dimensional structural folds that enable ATP-binding. Two major groups of enzymes are associated with binding of ATP: the AAA + ATPases and the universal stress protein (USPs) which bind and hydrolyze ATP, and the kinases which bind and mediate the transfer of the γ-terminal phosphoryl of ATP to another molecule (i.e., to a small molecule by metabolic kinases such as 6-phosphofructokinase or
Materials and methods
Reagents- ATP, phorbol 12-myristate 13-acetate (PMA), glyburide, puromycin and N6-linked ATP-Sepharose were purchased from Sigma Chemical Co (St. Louis, MO). All other chemicals were of reagent grade and were obtained from VWR (Edmonton, AB) or Sigma Chemical Co. P-linked γ-aminodecyl ATP Sepharose was synthesized at Duke University using published protocols [50,69]. Other immobilized ATP resins (R-linked and N8-linked ATP Sepharose resins) were obtained from Jena Bioscience GmbH (Germany). Bay
Acknowledgements
This work was supported by grants-in-aid from the University of Calgary University Research Grants Committee, the Canadian National Transplant Research Program (CNTRP), the Canadian Institutes of Health Research Health Challenges in Chronic Disease Signature Initiative (#THC-13523), and the Canada Foundation for Innovation. K.-C.L. was supported by a University of Calgary Eyes-High Fellowship. C.F.S. was supported by a Natural Sciences and Engineering Research Council (NSERC) Postgraduate
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- 1
Contributed equally to the manuscript.
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Current location: Programme in Emerging Infectious Diseases, Duke-NUS Medical School, Singapore.