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This editorial refers to ‘Post-translational modifications enhance NT-proBNP and BNP production in acute decompensated heart failure,’ by N. Vodovar et al. , on page doi:10.1093/eurheartj/ehu314. With the discovery that the heart is an endocrine organ, we now know that the heart produces and releases hormones, including the natriuretic peptides (NPs). NPs are thought to be produced and released mainly in response to mechanical stretching, due to increased intravascular volume or under pathophysiological conditions, especially in heart failure (HF).1 B-type NP (BNP) molecular forms, especially BNP and NT-proBNP, are currently in widespread used as biomarkers in HF. Human BNP is produced as a 134-amino acid preproBNP which is subsequently processed to proBNP1-108 by cleavage of its signal peptide. ProBNP 1-108 is then processed into inactive NT-proBNP 1-76 and the GC-A receptor activator BNP 1-32 by proprotein convertases corin or furin.2 The processing of BNP molecular forms is therefore critical for its bioavailability.Critical regulators in proBNP processing have been revealed, including the proteases corin and furin and the role of glycosylation of proBNP. Corin—a cardiac transmembrane serine protease that is abundantly expressed in the heart and kidneys, with a functional soluble form that is shed into the circulation—cleaves both proANP and proBNP into active hormones.2 It has …

Post-transcriptional modification of pro-BNP in heart failure: Is glycosylation and circulating furin key for cardiovascular homeostasis?: Figure 1