The enzyme is called cytosine monophosphate kinase 2 (CMPK2) and it activates NLRP3, an inflammation-triggering molecule, or inflammasome.
Scientists already knew that finding a way to block NLRP3 without affecting other inflammasomes could lead to new treatments for many inflammatory conditions.
"Dysregulated NLRP3 inflammasome activity results in uncontrolled inflammation, which underlies many chronic diseases," note the authors.
But without a clear understanding of the molecular pathways involved in triggering NLRP3, it was not possible to design drugs that specifically block it.
During the state of inflammation, there is a sharp rise in a hormone called interleukin 1 beta (IL-1B). The hormone is important for many cell events that occur during inflammation, including proliferation and death.
Inflammasomes control the production and release of IL-1B. NLRP3 is most active in this process. It senses diverse stimuli from noxious threats to tissue changes. These range from silica dust and asbestos to the microcrystals of uric acid that cause inflammation in gout.
In their study, Prof. Michael Karin — from the University of California, San Diego — and team focused on CMPK2 and the key role that the enzyme plays in triggering NLRP3 in sparking production of IL-1B and the subsequent development of chronic inflammatory conditions.
CMPK2 is a nucleotide kinase. Drug developers have already "successfully targeted" some of the enzymes in this group.
Prof. Karin suggests that CMPK2 blockers could reduce pain, inflammation, and tissue damage in osteoarthritis and gout, as well as slow the development of Parkinson's and Alzheimer's diseases.