Abstract
Human mast cell chymase, which is predominantly distributed in the perivascular tissues and heart, selectively, and neutrophil cathepsin G transiently, cleaved the Tyr31-Gly32 bond of three forms of big endothelin (ET)-1, -2 and -3, and generated new bioactive 31-arnino acid ETs, Ets( 1-31). Unlike the distribution of 21-arnino acid ET-1 in cardiovascular endothelial cells and bronchiolar epithelial cells, ET-1(1-31) was distributed predominantly in neutrophils, eosinophils and mast cells in addition to these tissues. Besides the biological activities of ET-l(1-31) on smooth muscle constriction and stimulation of mitosis, it induced local eotaxin and interleukin-5, resulting in eosinophil recruitment in mice, and also exhibited chemotactism for human neutrophils and monocytes. Concentrations of ET1(1-31) were markedly increased at sites of inflammation in lungs, while the increase in ET-1 (1-21) concentrations was not significant, suggesting that ET-1 (1-31) is a sensitive inflammatory mediator. In addition, human chymase itself was a potent chemoattractant for neutrophils and monocytes. Overall, these findings indicate that chymase, cathepsin G and ET derivatives in the perivascular tissues and heart represent a network of inflammatory mediators, and play pathophysiologic roles in cardiovascular diseases.
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Kido, H. et al. (2003). Human Mast Cell Chymase and 31 Amino Acid Endothelin-1. In: Matsumori, A. (eds) Cardiomyopathies and Heart Failure. Developments in Cardiovascular Medicine, vol 248. Springer, Boston, MA. https://doi.org/10.1007/978-1-4419-9264-2_13
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DOI: https://doi.org/10.1007/978-1-4419-9264-2_13
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