Back
For best output, select "Paper Size" as "A4" and "Margin" as "0" or "None".
To save or print to PDF, please select Print Destination > Save as PDF, enable Background Graphics under "More Settings", then click "Save".
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.
Diabetic kidney disease (DKD) is characterized by podocyte injury and proteinuria, yet the upstream RNA regulatory mechanisms remain poorly defined. We investigated the role of the RNA-binding protein Scaffold Attachment Factor A (SAF-A/hnRNP U) in podocyte pathogenesis in DKD.
We employed a systematic integrative approach, including single-cell RNA sequencing and MARVEL-based splicing analysis of human DKD kidneys. Functional validation was performed through podocyte-specific SAF-A knockdown in db/db mice and overexpression studies in cultured podocytes under diabetic conditions, complemented by RNA-seq, RIP-seq, and ribosome profiling.
DKD kidneys exhibited widespread alternative splicing across cell types, with marked upregulation and perinuclear-to-nuclear relocalization of SAF-A in podocytes. SAF-A levels were elevated in serum and urine and correlated with serum creatinine and eGFR. Podocyte-specific SAF-A knockdown in db/db mice attenuated proteinuria and preserved foot process ultrastructure. Conversely, SAF-A overexpression in cultured podocytes induced injury phenotypes—F-actin disassembly, slit diaphragm disruption, desmin induction, and abnormal nuclear division—alongside altered cytoskeletal and cell cycle protein expression. Mechanistically, SAF-A orchestrates a dual-layer regulatory program: at the pre-mRNA level, it directs alternative splicing of cytoskeletal and cell cycle genes, including the actomyosin regulator Myl12a and microtubule-stabilizing factor Tacc3; at the translational level, it enhances synthesis of Nek2, Ccnd1, Ccnb1, and Tacc3 while repressing Myl12a, collectively disrupting actomyosin and microtubule networks and promoting foot process effacement.
SAF-A is a central mechanistic regulator of podocyte injury in DKD, acting through coordinated splicing and translational control. These findings identify circulating and urinary SAF-A as promising biomarkers and candidate therapeutic targets in DKD.
