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

Inna P. Gladysheva, Sarah M. King, Aiilyan K. Houng

Research output: Contribution to journalArticlepeer-review

31 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)130-135
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume373
Issue number1
DOIs
StatePublished - Aug 15 2008
Externally publishedYes

Keywords

  • Atrial natriuretic peptide
  • Cell-surface expression
  • Corin
  • Glycosylation

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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