RPLP0 (ribosomal protein lateral stalk subunit P0) is a structural component of the cytosolic large ribosomal subunit that functions as the eukaryotic functional equivalent of bacterial L10 protein 1. As a core ribosomal protein, RPLP0 participates in translation and ribonucleoprotein complex assembly 1. Beyond its canonical ribosomal function, RPLP0 has emerged as a critical player in multiple pathological conditions. In high-altitude pulmonary edema (HAPE), RPLP0 downregulation drives endothelial cell apoptosis and increased vascular permeability 2. Conversely, RPLP0 is markedly upregulated in Alzheimer's disease brain capillaries alongside increased ribosomal protein expression and endoplasmic reticulum protein processing activity 3. In cancer contexts, RPLP0 demonstrates oncogenic properties. Elevated RPLP0 expression in lung adenocarcinoma correlates with poor prognosis, worse overall survival, and enhanced immune infiltration 4. In hepatocellular carcinoma, RPLP0 upregulation—regulated by c-Myc and the ROS-mediated JAK2/STAT3 pathway—promotes proliferation, invasion, and epithelial-mesenchymal transition while suppressing apoptosis 5. In cervical and non-small-cell lung cancers, RPLP0 suppression mediates tumor-suppressive effects including cell cycle arrest and apoptosis 6, 7. These findings establish RPLP0 as a multifunctional protein with disease-specific roles spanning vascular biology, neurodegeneration, and malignancy.