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

(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.

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.
References in periodicals archive ?
Lu et al., "Mammalian Notch1 is modified with two unusual forms of O-linked glycosylation found on epidermal growth factor-like modules," The Journal of Biological Chemistry, vol.
O-linked glycosylation appears to be one source of the heterogeneity (11).
As indicated by the arrow, the trisaccharide form is not detected in homozygous Gc2 individuals, consistent with the Gc2 genotype lacking the preferred site of O-linked glycosylation ([Thr.sup.420] changed to [Lys.sup.420]) (27, 30).
Finally, O-linked glycosylation is essential for the expression and processing of particular proteins.
Concepts and principles of O-linked glycosylation. Crit Rev Biochem Mol Biol 1998;33:151-208.
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.
Elimination of the O-linked glycosylation site at Thr 104 results in the generation of a soluble human-transferrin receptor.