XDH-1 inactivation causes xanthine stone formation in C. elegans which is inhibited by SULP-4-mediated anion exchange in the excretory cell.

ABSTRACT: Xanthine dehydrogenase (XDH-1) is a molybdenum cofactor (Moco) requiring enzyme that catabolizes hypoxanthine into xanthine and xanthine into uric acid, the final steps in purine catabolism. Human patients with mutations in xdh-1 develop xanthinuria which can lead to xanthine stones in the kidney, recurrent urinary tract infections, and renal failure. Currently there are no therapies for treating human XDH-1 deficiency. Thus, understanding mechanisms that maintain purine homeostasis is an important goal of human health. Here, we used the nematode C. elegans to model human XDH-1 deficiency using 2 clinically relevant paradigms, Moco deficiency or loss-of-function mutations in xdh-1. Both Moco deficiency and xdh-1 mutations caused the formation of autofluorescent

SUBMITTER: Snoozy J 

PROVIDER: S-EPMC11838210 | biostudies-literature | 2025 Jan

REPOSITORIES: biostudies-literature