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, 28 (11), 755-764

Chymase Inhibitors for the Treatment of Cardiac Diseases: A Patent Review (2010-2018)


Chymase Inhibitors for the Treatment of Cardiac Diseases: A Patent Review (2010-2018)

Sarfaraz Ahmad et al. Expert Opin Ther Pat.


Introduction: Chymase is primarily found in mast cells (MCs), fibroblasts, and vascular endothelial cells. MC chymase is released into the extracellular interstitium in response to inflammatory signals, tissue injury, and cellular stress. Among many functions, chymase is a major extravascular source for angiotensin II (Ang II) generation. Several recent pre-clinical and a few clinical studies point to the relatively unrecognized fact that chymase inhibition may have significant therapeutic advantages over other treatments in halting progression of cardiac and vascular disease.

Areas covered: The present review covers patent literature on chymase inhibitors for the treatment of cardiac diseases registered between 2010 and 2018.

Expert opinion: Increase in cardiac MC number in various cardiac diseases has been found in pathological tissues of human and experimental animals. Meta-analysis data from large clinical trials employing angiotensin-converting enzyme (ACE) inhibitors show a relatively small risk reduction of clinical cardiovascular endpoints. The disconnect between the expected benefit associated with Ang II blockade of synthesis or activity underscores a greater participation of chymase compared to ACE in forming Ang II in humans. Emerging literature and a reconsideration of previous studies provide lucid arguments to reconsider chymase as a primary Ang II forming enzyme in human heart and vasculature.

Keywords: Mast cells; angiotensin I; angiotensin II; angiotensin-(1-12); angiotensin-converting enzyme; angiotensinogen; chymase; chymase inhibitors; metabolism; renin; renin-angiotensin system; serine protease.


Figure 1.
Figure 1.
Schematic description of the main biochemical pathways involved in the formation of biologically active angiotensins. Neprilysin, NEP; Prolyl oligopeptidase, POP; Thimet oligopeptidase, TOP; Other abbreviations as in text.

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