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Editorial
B Type natriuretic peptide: a good omen in myocardial ischaemia?
  1. S P D’Souza1,
  2. G F Baxter2
  1. 1The Heart Hospital, London, UK
  2. 2The Royal Veterinary College, University of London, London, UK
  1. Correspondence to:
    Dr G F Baxter, Department of Basic Sciences, The Royal Veterinary College, University of London, Royal College Street, London NW1 0TU, UK;
    gfbaxter{at}rvc.ac.uk

https://doi.org/10.1136/heart.89.7.707

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    Although BNP is now firmly established as a diagnostic and prognostic marker of ventricular dysfunction, its autocrine and paracrine actions within the heart have received less attention

    The natriuretic peptide family consists of a number of structurally homologous but genetically distinct polypeptide mediators. The peptides are highly conserved across mammalian and invertebrate species and, in humans, are released from various tissues in response to physiological and pathological stimuli. All the peptides have at their core a 17-amino acid disulfide ring essential for receptor recognition and biological function.

    The first description of secretory granules in the cardiac atria was given in 1956, to be followed by the physiological characterisation of an atrial natriuretic factor in the work of de Bold and colleagues in 1981.1 Several further natriuretic peptides have subsequently been identified. These include B type natriuretic peptide (BNP) predominantly from ventricular myocardium (although originally isolated from pig brain)2 and C type natriuretic peptide (CNP) expressed in the nervous system and endothelial cells.3 A homologue of the natriuretic factor, DNP, in the venom of the green mamba Dendroaspis angusticeps, is found in plasma and atrial myocardium of normal humans.4 Urodilatin is a renal derived natriuretic peptide.5 ANP and BNP, the predominant natriuretic peptides in mammalian cardiomyocytes, are stored within secretory granules as pro-peptides, pro-ANP and pro-BNP, that are post-translationally modified by peptide bond cleavage to form the mature circulating peptides and amino (N)-terminal residues.6

    Biological activity of the peptides generally resides in the mature carboxy-terminal residues, although pro-ANP and pro-BNP may exhibit some activity. The (N)-terminal residues are generally inactive. Relatively little is known about the processing of BNP in the circulation. The peptides …

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