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During the congress, E-Posters will be accessible to all participants on the congress website 24/7, as well as in the E-poster stations in the congress center.
Preparing your E-Poster
Please review the E-Poster format requirements carefully when preparing your E-Poster. Should your E-Poster not meet the mentioned requirements, it may not be displayed as described above.
E-Poster Submission Deadline
Please prepare and upload your E-Poster no later than March 14, 2026 11.59PM CET. After this date, you will no longer be able to prepare and upload your E-poster and it will not be displayed and accessible on the congress website.
Please follow the instructions below to input your abstract title.
Abstract titles should be brief and reflect the content of the abstract.
Nephrin is an essential protein expressed at the slit diaphragm of podocytes and plays a crucial role in maintaining the integrity of the glomerular filtration barrier. We previously developed a novel experimental autoimmune nephrotic syndrome mouse model resembling idiopathic nephrotic syndrome in humans, induced by immunization with Crb2, a slit diaphragm protein that interacts with Nephrin. While proper trafficking of Nephrin to the podocyte surface is critical for its function, and impaired Nephrin turnover contributes to podocyte injury, the mechanisms underlying Nephrin trafficking in this model remain unknown.
Cell surface Nephrin expression following anti-Crb2 antibody stimulation was analyzed in immortalized human podocytes using biotinylation and western blotting. Nephrin expression in mouse kidney was evaluated by western blotting, and Nephrin localization in podocytes as well as in mouse and human kidney biopsy samples from anti-CRB2 antibody positive patients was examined by immunofluorescence staining. Markers of endocytosis and autophagy were used to identify the trafficking pathways involved.
Cell surface Nephrin expression was significantly reduced following anti-Crb2 antibody stimulation. In Crb2-immunized mouse kidney, Nephrin staining intensity decreased, and its reduced expression was confirmed by western blotting. Nephrin showed increased colocalization with the endocytosis markers Rab5 and Rab7, indicating enhanced endocytosis. Furthermore, Nephrin colocalized with the autophagy marker LC3. Triple staining for Nephrin, LC3, and Rab7 was elevated, suggesting processing via the amphisomal pathway. Colocalization with the lysosomal marker LAMP1 was increased, indicating lysosomal degradation. Enhanced colocalization between Nephrin and each of Rab5, Rab7, and LC3 was similarly observed in cultured podocytes. Consistently, kidney samples from patients with minimal change disease and focal segmental glomerulosclerosis exhibited reduced Nephrin staining intensity and altered Nephrin localization.
Nephrin undergoes endocytosis and is degraded via the amphisome-lysosome pathway in the Crb2-induced nephrotic syndrome mouse model, leading to a reduction in membrane localization. These results provide new insights into the autoantibody-mediated pathogenesis of podocyte injury in nephrotic syndrome.
