By Aldo Clerico MD, Michele Emdin MD, PhD (auth.), Prof. Aldo Clerico, Dr. Michele Emdin (eds.)

The fast wisdom within the box of neuro-humoral law of cardiovascular pathophysiology is altering the image of present analysis and therapy of cardiac patients.

The rising conceptual innovative inspiration is that center acts now not as a pump, in simple terms, yet as a "gland", that's as a regulator of circulatory homeostasis and salt-water balance.

Cardiovascular pathophysiology should be written, certainly, in this foundation: this body structure textbook offers an updated description of the complexity and novelty of exact wisdom, with all its capability scientific implications.

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Studies in fish, based on nucleotide and amino acid sequence similarity, suggest that the natriuretic peptide family of iso-hormones may have evolved from a neuromodulatory CNP-like brain peptide (Fig. 6) [4]. However, caution should be exercised in identification and comparison of vertebrate hormones from phylogenetically distant organisms [1]. 3. Amino acid sequences of C-type natriuretic peptide precursors in selected species of mammals and in nonmammalian vertebrates. The identical amino acid residues within CNP precursors are shadowed.

As far as hormones more specifically acting on intermediate metabolism are concerned, insulin (but not hyperglycemia) increased protein synthesis and ANP secretion and gene expression in cultured rat cardiac myocytes [75]. Moreover, in a model of genetic murine dilated cardiomyopathy, short-term RhGH treatment improved left ventricular function and significantly reduced elevated mRNA expression of ANP and BNP gene expression in left ventricular tissue [76]. In conclusion, a huge number of experimental and clinical studies demonstrated that production and secretion of CNH (especially BNP) are not only related to hemodynamic variations, but also subtly regulated by neuro-hormonal and immunological factors.

11) and receptor-mediated cellular uptake via NPR-C [14] (Fig. 22). 3. 3. 1 ANP Metabolism Atrial natriuretic peptides are a family of peptides derived from a common precursor, called preproANP, which in humans contains 151 amino acids and has a signal peptide sequence at its amino-terminal end (Fig. 11). The pro-hormone is stored in secretion granules of cardiomyocytes as a 126-amino-acid peptide, proANP1-126, which is produced by cleavage of the signal peptide. When appropriate signals for hormone release are given, proANP1-126 is further split by some proteases (especially the serine protease corin) [192] into N-terminal fragment NT-proANP and the COOH-terminal peptide ANP, which is generally considered to be the biologically active hormone, because it contains the cysteine ring (Figs.

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