engleski

What've glycans got to do with it?

Molecular and structural recognition is a central event in all sorts of biological phenomena. Any change at the site of interaction will disturb or disrupt the original molecular communication. Glycosylation is a post-translational, not genetically coded modification involving the covalent attachment of oligosaccharide chains to proteins or lipids. It is regulated by the cell's glycosylation machinery and the temporal conditions experienced during modification. Glycan chains are ordered structures composed of various monosaccharides and charged molecules (sialic acids) in a specific sequence. Glycans can therefore influence both the intramolecular (physiochemical) properties, such as conformation, stability, time of life and intermolecular properties, for example molecular recognition, of the proteins to which they are attached. The oligosaccharides of the same glycoprotein can exhibit subtle structural variation resulting in the formation of glycoforms which have identical amino acid sequences but different glycosylation patterns. Protein glycosylation changes even in the course of the regular metabolism and the integrity of carbohydrate attachments are often markers for a molecule to be degraded or targeted to function. Many cell receptors including  1-adrenergic receptor and angiotensin II receptors (AT1 and AT2) are heavily glycosylated. However, in many cases precise function of attached glycans as well as the consequences of altered glycosylation is still elusive. In this lecture the effects of glycosylation on the structure and function of glycoproteins will be discussed.

glycosylation; receptores; hypertension

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