Glycosylation

Glycosylation is the enzymatic attachment of sugar groups to proteins, lipids, or other molecules. It creates diverse glycoconjugates that influence molecular structure, recognition, and function.

N-linked glycosylation: A pathway that attaches an oligosaccharide to the nitrogen atom of asparagine in a protein. It is a major protein glycosylation route, beginning in the endoplasmic reticulum.
Glycan: A chain or branched structure of sugar residues linked by glycosidic bonds. Glycosylation produces glycans whose composition and branching vary between molecules.
Monoclonal antibody: An antibody preparation consisting of molecules with the same antigen-binding specificity. Antibody glycans can alter immune-effector activity and influence therapeutic performance.
Cell-cell recognition: The process by which cells identify and interact with other cells through surface molecules. Cell-surface glycans provide patterns that binding proteins use to distinguish cells.
Glycation: A usually nonenzymatic reaction in which sugars attach to proteins or other molecules. Unlike glycosylation, glycation does not require enzymes and often arises from sugar exposure.
O-linked glycosylation: A group of pathways that attach sugars to oxygen atoms in amino-acid side chains, commonly serine or threonine. It contrasts with N-linked attachment and often proceeds stepwise in the Golgi apparatus.
Glycoprotein: A protein covalently linked to one or more carbohydrate groups. It is one of the principal products of protein glycosylation.
Erythropoietin: A glycoprotein hormone that stimulates red blood cell production. Its glycans affect stability and circulation time, making glycosylation central to drug design.
ABO blood group system: A blood-group classification based on A and B carbohydrate antigens on red blood cells and other tissues. Its defining antigens are sugars whose addition depends on glycosyltransferase activity.
Phosphorylation: The enzymatic transfer of a phosphate group to a molecule, often a protein. It is another enzyme-directed protein modification, but adds phosphate rather than sugar.

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