glycosylation

(redirected from O-linked glycosylation)
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Related to O-linked glycosylation: N-linked glycosylation

glycosylation

 [gli-ko″-sĭ-la´shun]
the formation of linkages with glycosyl groups.

gly·co·sy·la·tion

(glī'kō-si-lā'shŭn),
Formation of linkages with glycosyl groups, as between d-glucose and the hemoglobin chain to form the fraction hemoglobin AIc, the level of which rises in association with the elevated concentration of d-glucose in blood concentration in poorly controlled or uncontrolled diabetes mellitus.
See also: glycosylated hemoglobin.

glycosylation

/gly·co·syl·a·tion/ (gli-ko″sĭ-la´shun) the formation of linkages with glycosyl groups.

glycosylation

(glī′kō-sĭ-lā′shən)
n.
The addition of saccharides to proteins or lipids to form a glycoprotein or glycolipid.

gly·co′sy·late′ v.

glycosylation

[glīkə′səlā′shən]
the formation of linkages with glycosyl groups, covalently attaching a carbohydrate to another molecule.

gly·co·sy·la·tion

(glī'kō-si-lā'shŭn)
Formation of linkages with glycosyl groups, as between d-glucose and the hemoglobin chain to form the fraction hemoglobin AIc, the level of which rises in association with the raised blood d-glucose concentration in poorly controlled or uncontrolled diabetes mellitus.
See also: glycosylated hemoglobin

glycosylation

the addition of a CARBOHYDRATE to an organic molecule such as a PROTEIN.

glycosylation (glī·kōˈ·s·lāˑ·shn),

n process in which a carbohydrate is covalently attached to another molecule.

glycosylation

the formation of linkages with glycosyl groups.

N-linked glycosylation
attachment of oligosaccharides, synthesized on a dolichol-lipid platform to proteins through the amino acid asparagine spaced close to threonine or serine in the polypeptide sequence.
O-linked glycosylation
attachment of groups of oligosaccharides directly to proteins through the hydroxyl group of threonine.
References in periodicals archive ?
However, large comparative studies have failed to reveal major differences between BNP and proBNP measurements in terms of overall clinical performance, although plasma measurement based on assays directed against the N-terminal proBNP fragment is greatly influenced by the degree of O-linked glycosylation.
Finally, O-linked glycosylation is essential for the expression and processing of particular proteins.
Localization of three human polypeptide GalNAc-transferases in HeLa cells suggests initiation of O-linked glycosylation throughout the Golgi apparatus.
Expression of human glycophorin A in wild type and glycosylation-deficient Chinese hamster ovary cells: role of N- and O-linked glycosylation in cell surface expression.
Serum "big insulin-like growth factor II" from patients with tumor hypoglycemia lacks normal E-domain O-linked glycosylation, a possible determinant of normal propeptide processing.
Mutations in GALNT3, encoding a protein involved in O-linked glycosylation, cause familial tumoral calcinosis.