Title
Inhibition of PAD4 activity is sufficient to disrupt mouse and human NET formation.
UMMS Affiliation
Department of Biochemistry and Molecular Pharmacology
Publication Date
2015-03-01
Document Type
Article
Subjects
Animals; Binding, Competitive; Calcium; Citrulline; Enzyme Inhibitors; HEK293 Cells; Histones; Humans; Hydrolases; In Vitro Techniques; Mice; Models, Molecular; Neutrophils; Small Molecule Libraries; Substrate Specificity
Disciplines
Biochemistry | Enzymes and Coenzymes | Medicinal-Pharmaceutical Chemistry | Therapeutics
Abstract
PAD4 has been strongly implicated in the pathogenesis of autoimmune, cardiovascular and oncological diseases through clinical genetics and gene disruption in mice. New selective PAD4 inhibitors binding a calcium-deficient form of the PAD4 enzyme have validated the critical enzymatic role of human and mouse PAD4 in both histone citrullination and neutrophil extracellular trap formation for, to our knowledge, the first time. The therapeutic potential of PAD4 inhibitors can now be explored.
DOI of Published Version
10.1038/nchembio.1735
Source
Nat Chem Biol. 2015 Mar;11(3):189-91. doi: 10.1038/nchembio.1735. Link to article on publisher's site
Journal/Book/Conference Title
Nature chemical biology
Related Resources
Repository Citation
Lewis, Huw D. and Thompson, Paul R., "Inhibition of PAD4 activity is sufficient to disrupt mouse and human NET formation." (2015). Thompson Lab Publications. 4.
https://escholarship.umassmed.edu/thompson/4
Comments
Full author list omitted for brevity. For the full list of authors, see article.