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Biochem Biophys Res Commun. 2008 Aug 15;373(1):130-5. doi: 10.1016/j.bbrc.2008.05.181. Epub 2008 Jun 10.

N-glycosylation modulates the cell-surface expression and catalytic activity of corin.

Author information

1
Cardiovascular Research Center, Department of Medicine, Medical College of Georgia, 1120 15th Street, CB-2207, Augusta, GA 30912, USA. igladysheva@mcg.edu

Abstract

N-glycosylation may influence the subcellular localization and biological activity of the pro-ANP convertase, corin. In HEK293-corin cells, the inhibition of N-glycosylation, with tunicamycin, reduced the cell-surface expression of murine corin, but did not alter the total expression. Therefore, tunicamycin treatment likely caused the intracellular accumulation of non-glycosylated corin. Tunicamycin treatment also significantly reduced corin activity (pro-ANP cleavage) in these cells. We developed an assay to measure the effect of N-glycosylation on corin activity, independent of its effect on corin localization. We determined that the reduction in corin activity was due to a direct effect of N-glycosylation, and was not secondary to the effect of N-glycosylation on corin cell-surface expression. Our data provide evidence that N-glycosylation is essential for the cell-surface expression of murine corin and modulates its functional activity. N-Glycosylation represents a possible mechanism for the regulation of native corin on the surface of cardiomyocytes.

PMID:
18549807
DOI:
10.1016/j.bbrc.2008.05.181
[Indexed for MEDLINE]

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