Cathepsin S-Dependent Processing of APOL1-G1 Generates Toxic Fragments Resistant to Membrane-Targeted APOL1 Inhibition (KIDNEY WEEK 2026) - Oct 2, 2026 - Abstract #TH-PO0283; Pres time: Oct 22, 2026; 10:00 AM - 12:00 PM; Location: Exhibit Hall A, Convention Center; "Cytotoxicity assays were used to compare the effects of full-length APOL1-G1 and APOL1-G1 fragments, including their responses to the APOL1 channel inhibitor Inaxaplin...These studies identify Cathepsin S as a potential upstream therapeutic target linking inflammatory signaling to APOL1 fragmentation, altered intracellular trafficking, and nuclear toxicity. More broadly, our data suggest that proteolytic processing of APOL1-G1 may represent a central pathogenic mechanism contributing to HIVAN and other APOL1-associated kidney diseases."
Human Immunodeficiency Virus • Infectious Disease • Nephrology • Renal Disease • CTSS • IFNG • TNFA
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Jinliang Li; Jing Yu; Lian Xu; Jharna R. Das; Zhe Han; Patricio E. Ray
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