Kidney diseases present substantial clinical challenges, with aberrant glycoprotein emerging as a key pathogenic driver. Minor glomerular abnormalities (MGAs), a category of unclassified glomerular lesions defined by subtle structural changes, are commonly detected in patients with persistent, asymptomatic, isolated proteinuria or microhematuria., yet their site-specific N-glycosylation patterns remain unelucidated. To address this gap, we applied a laboratory-developed pressure cycling technology (PCT)-based quantitative glycoproteomics workflow (GlycoPCT) to compare intact N-glycopeptides (IGPs) between distant non-neoplastic tissues (DNT; n=24) and trace renal biopsy samples from MGA patients (n=27). Integrated with high-sensitivity, high-resolution mass spectrometry (EThcD-sceHCD-MS/MS), GlycoPCT identified 672 upregulated IGPs (FC>1.5, p<0.05) and 573 downregulated IGPs (FC<0.67, p<0.05) in MGA tissues. Total fucosylation type N-glycans were significantly downregulated (p<0.05), while sialylation type N-glycans were markedly downregulated (p<0.001). Additionally, 24 glycoproteins associated with the PI3K-Akt signaling pathway (a well-documented mediator of renal injury) showed broadly N-glycosylation upregulation. Site-specific N-glycosylation analysis further revealed differential patterns in IgG subclasses and complement-related markers that distinguish MGA from DNT, offering new mechanistic insights into MGA pathogenesis. These novel glyco-signatures clarify the role of N-glycosylation in renal disease, highlight TINAGL1, IgG, IgM, and complement-related glycoproteins as potential MGA biomarkers, and validate GlycoPCT as a powerful tool for trace tissue analysis. This study lays the groundwork for translating N-glycosylation findings into clinical applications to improve MGA diagnosis and management.