| First Author | Gladysheva IP | Year | 2008 |
| Journal | Biochem Biophys Res Commun | Volume | 373 |
| Issue | 1 | Pages | 130-5 |
| PubMed ID | 18549807 | Mgi Jnum | J:137759 |
| Mgi Id | MGI:3802853 | Doi | 10.1016/j.bbrc.2008.05.181 |
| Citation | Gladysheva IP, et al. (2008) N-glycosylation modulates the cell-surface expression and catalytic activity of corin. Biochem Biophys Res Commun 373(1):130-5 |
| abstractText | 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. |
