Title : Functional implications of corticosteroid-binding globulin N-glycosylation.

Pub. Date : 2018 Feb

PMID : 29273683






7 Functional Relationships(s)
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1 Glycosylation of human CBG influences its steroid-binding activity, and there are N-glycosylation sites in the reactive center loops (RCLs) of human and rat CBGs. Steroids serpin family A member 6 Homo sapiens
2 Proteolysis of the RCL of human CBG causes a structural change that disrupts steroid binding. Steroids serpin family A member 6 Homo sapiens
3 We now show that mutations of conserved N-glycosylation sites at N238 in human CBG and N230 in rat CBG disrupt steroid binding. Steroids serpin family A member 6 Homo sapiens
4 Deglycosylation of fully glycosylated human CBG or human CBG with only one N-glycan at N238 with Endo H-reduced steroid-binding affinity, while PNGase F-mediated deglycosylation does not, indicating that steroid binding is preserved by deamidation of N238 when its N-glycan is removed. Steroids serpin family A member 6 Homo sapiens
5 Deglycosylation of fully glycosylated human CBG or human CBG with only one N-glycan at N238 with Endo H-reduced steroid-binding affinity, while PNGase F-mediated deglycosylation does not, indicating that steroid binding is preserved by deamidation of N238 when its N-glycan is removed. Steroids serpin family A member 6 Homo sapiens
6 When expressed in N-acetylglucosaminyltransferase-I-deficient Lec1 cells, human and rat CBGs, and a human CBG mutant with only one glycosylation site at N238, have higher (2-4 fold) steroid-binding affinities than when produced by sialylation-deficient Lec2 cells or glycosylation-competent CHO-S cells. Steroids serpin family A member 6 Homo sapiens
7 Thus, the presence and composition of an N-glycan in this conserved position both appear to influence the steroid binding of CBG. Steroids serpin family A member 6 Homo sapiens