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

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 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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Atrial Natriuretic Factor / metabolism*
  • Catalysis
  • Cell Line
  • Cell Membrane / enzymology*
  • Glycosylation / drug effects
  • Humans
  • Mice
  • Myocytes, Cardiac / enzymology
  • Recombinant Proteins / metabolism
  • Serine Endopeptidases / metabolism*
  • Tunicamycin / pharmacology


  • Recombinant Proteins
  • Tunicamycin
  • Atrial Natriuretic Factor
  • Corin protein, mouse
  • Serine Endopeptidases