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.
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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.
Protein Posttranslational Modifications: Roles in Aging and Age-Related Disease
O-linked glycosylation appears to be one source of the heterogeneity (11).
Characterization of molecular forms of N-terminal B-type natriuretic peptide in vitro
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).
Full-length characterization of proteins in human populations
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.
Mechanisms in protein O-glycan biosynthesis and clinical and molecular aspects of protein O-glycan biosynthesis defects: a review
Elimination of the O-linked glycosylation site at Thr 104 results in the generation of a soluble human-transferrin receptor.
Ratio of transferrin (Tf) to Tf-receptor complex in circulation differs depending on Tf iron saturation

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