Copper-responsive proteome changes in human kidney proximal tubule epithelial cells
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ABSTRACT: Copper is essential for cellular function but potentially toxic in excess. While copper's influence on cytoskeletal dynamics remains unclear, loss of mechanical integrity is a hallmark of kidney disease. Here we investigated how copper availability modulates mechanical properties and cytoskeletal architecture of human proximal tubule epithelial cells (HK-2). Cells were treated for 24h with 50 µM CuCl₂ (copper supplementation) or 10 µM tetrathiomolybdate (TTM, copper chelation). Quantitative proteomics revealed coordinated changes in actin-regulatory proteins including Rab35, Septin2, MsrB2, and CK2 subunits, establishing redox-dependent pathways linking copper homeostasis to cytoskeletal dynamics. A total of 4,933 proteins were quantified with 89-90% data completeness, including detection of 13,919 PTMs per run (carbamidomethylation, oxidation, phosphorylation sites)
INSTRUMENT(S):
ORGANISM(S): Homo Sapiens (human)
TISSUE(S): Epithelial Cell Of Proximal Tubule, Kidney
SUBMITTER:
Rafael Valverde
LAB HEAD: Marcelo Einicker Lamas
PROVIDER: PXD072220 | Pride | 2026-07-21
REPOSITORIES: Pride
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