- Poster presentation
- Open Access
O-glycosylated pro-B-type natriuretic peptide is cleaved intracellularly by furin in ventricular and atrial myocytes: importance of the distance between the O-glycosylation and cleavage sites
© Nishikimi et al; licensee BioMed Central Ltd. 2013
- Published: 29 August 2013
- Heart Failure
- Molecular Mechanism
- Human Plasma
- Natriuretic Peptide
Rat neonatal atrial and ventricular myocytes were cultured separately. We examined: (1) the molecular forms of secreted and intracellular BNP in atrial and ventricular myocytes; (2) levels of corin and furin mRNA in atrial and ventricular myocytes and the effect their knockdown on proBNP processing; (3) molecular forms of BNP in plasma from rats and humans with and without heart failure; (4) the structure of proBNP in humans and rats; (5) the impact of the distance between the glycosylation and cleavage sites in wild-type and mutant human proBNP expressed in rat myocytes transfected with lentiviral vectors.
These results suggest that proBNP is processed into BNP and N-terminal proBNP intracellularly, most likely by furin in rat. The level of proBNP processing is lower in humans than rats, most likely due to the smaller distance between the O-glycosylation and cleavage sites in humans.
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