A crystal-clear mechanism of chronic kidney disease

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A crystal-clear mechanism of chronic kidney disease Christian Kurts Kidney International Volume 84, Issue 5, Pages 859-861 (November 2013) DOI: 10.1038/ki.2013.251 Copyright © 2013 International Society of Nephrology Terms and Conditions

Figure 1 Inflammasome activation by intrarenal crystal precipitation. Crystal formation activates assembly of Nlrp3 protein oligomers, to which apoptosis-associated speck-like protein containing a carboxy-terminal CARD (ASC) and caspase-1 are recruited, forming an Nlrp3 inflammasome in tubulointerstitial dendritic cells. This proteolytically activates pro-IL-1 to form bioactive interleukin-1 (IL-1), which drives tubulointerstitial inflammation and chronic kidney disease. The Nlrp3 protein is displayed with its C-terminal leucine-rich repeat domain (white), nucleotide-binding and oligomerization domain (green), and pyrin domain (red). The ASC protein contains a pyrin (red) and a caspase activation and recruitment domain (CARD; brown). Kidney International 2013 84, 859-861DOI: (10.1038/ki.2013.251) Copyright © 2013 International Society of Nephrology Terms and Conditions