biostudies-literatureGarapati KDBT/Wellcome Trust India Alliance entitled "Center for Rare Disease Diagnosis, Research, and Training"DBT/Wellcome Trust India Alliance entitled “Center for Rare Disease Diagnosis, Research, and Training”DBT/Wellcome Trust India AllianceWellcome Trustcwae076https://www.ebi.ac.uk/biostudies/studies/S-EPMC7617596biostudies-literatureUnknown34(11)SRD5A3-CDG is a congenital disorder of glycosylation (CDG) resulting from pathogenic variants in SRD5A3 and follows an autosomal recessive inheritance pattern. The enzyme encoded by SRD5A3, polyprenal reductase, plays a crucial role in synthesizing lipid precursors essential for N-linked glycosylation. Despite insights from functional studies into its enzymatic function, there remains a gap in understanding global changes in patient cells. We sought to identify N-glycoproteomic and proteomic signatures specific to SRD5A3-CDG, potentially aiding in biomarker discovery and advancing our understanding of disease mechanisms. Using tandem mass tag (TMT)-based relative quantitation, we analyzed fibroblasts derived from five patients along with control fibroblasts. N-glycoproteomics analysis by lGlycobiologyN-glycoproteomic and proteomic alterations in SRD5A3-deficient fibroblasts.PMC7617596IA/CRC/20/1/600002Garapati KJoshi NSabu SMorava EPreston GRanatunga WBudhraja RPandey AKantautas KAPerlstein EOKozicz TfalseN-glycoproteomic and proteomic alterations in SRD5A3-deficient fibroblasts.SRD5A3-CDG is a congenital disorder of glycosylation (CDG) resulting from pathogenic variants in SRD5A3 and follows an autosomal recessive inheritance pattern. The enzyme encoded by SRD5A3, polyprenal reductase, plays a crucial role in synthesizing lipid precursors essential for N-linked glycosylation. Despite insights from functional studies into its enzymatic function, there remains a gap in understanding global changes in patient cells. We sought to identify N-glycoproteomic and proteomic signatures specific to SRD5A3-CDG, potentially aiding in biomarker discovery and advancing our understanding of disease mechanisms. Using tandem mass tag (TMT)-based relative quantitation, we analyzed fibroblasts derived from five patients along with control fibroblasts. N-glycoproteomics analysis by l2024-01-01T00:00:00Z2024 Sep2026-05-22T03:15:35.907Z2025-07-12T03:04:38.139ZS-EPMC76175963936084810.1093/glycob/cwae076