Human glycosylation pathways

Human glycosylation pathways represent the collective enzymatic processes responsible for the covalent attachment of carbohydrate chains, known as glycans, to proteins and lipids [1]. This post-translational modification is highly complex and occurs primarily within the endoplasmic reticulum and Golgi apparatus, involving hundreds of distinct enzymes [4]. These pathways, including N-linked and O-linked glycosylation, are essential for proper protein folding, stability, and intracellular trafficking [1]. Beyond these structural roles, glycans on the cell surface are critical for cell-cell recognition, adhesion, and the modulation of immune signaling [2]. Dysregulation of these pathways is a hallmark of various diseases, including cancer, where aberrant glycosylation promotes tumor metastasis and immune evasion, and Congenital Disorders of Glycosylation (CDG) [2, 3]. While the pathways themselves are too broad to be a single drug target, specific enzymes within them are targeted by small molecules to treat metabolic disorders or are being investigated for their potential in oncology [2, 5].

Other names

Protein glycosylationGlycan biosynthesisGlycosylation machineryN-glycosylation pathwayO-glycosylation pathway

Inhibition of specific glycosyltransferases or glycosidases within the pathway to alter the glycan profile of cell surface or secreted proteins [1, 2].