Dog mast cell chymase: molecular cloning and characterization

Caughey, George H.; Raymond, Wilfred W.; Vanderslice, Peter

doi:10.1021/bi00473a024

Cited by 52 publications

(24 citation statements)

References 41 publications

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“…Based on the number of basic (Arg+Lys=29) and acidic (Asp+Glu=14) amino acids, the monkey chymase catalytic domain has a predicted net charge of +15 (Fig. 1), and that of human chymase [16, 17], dog chymase [25]and RMCP I [26]are +13, +16 and +18, respectively. Despite the differences in net charges, chymases are reported to bind to heparin glycosaminoglycan [27–29]; therefore, it is reasonable to assume that monkey chymase will bind in the same manner.…”

Section: Resultsmentioning

confidence: 99%

Induction of chymase that forms angiotensin II in the monkey atherosclerotic aorta

et al. 1997

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Chymase shows a catalytic efficiency in the formation of angiotensin (Ang) II. In the present study, the characterization and primary structure of monkey chymase were determined, and the pathophysiological role of chymase was investigated on the atherosclerotic monkey aorta. Monkey chymase was purified from cheek pouch vascular tissue using heparin affinity and gel filtration columns. The enzyme rapidly converted Ang I to Ang II (K m -98 uM, k cstt -6203/min) but did not degrade several peptide hormones such as Ang II, substance P, vasoactive intestinal peptide and bradykinin. The primary structure, which was deduced from monkey chymase cDNA, showed a high homology to that of human chymase (98%). The mRNA levels of the aorta chymase were significantly increased in the atherosclerotic aorta of monkeys fed a high-cholesterol diet. These results indicate that monkey chymase has a highly specific Ang Il-forming activity and may be related to the pathogenesis of atherosclerosis.

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Section: Resultsmentioning

confidence: 99%

Induction of chymase that forms angiotensin II in the monkey atherosclerotic aorta

et al. 1997

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“…The mechanism by which chymase becomes a primary enzymatic pathway for Ang-(1-12) metabolism remains under investigation. Current studies show that mast cells are a predominant source for chymase [73–75]. Mast cell chymase is increased in the dilated left atrium of patients with mitral regurgitation with evidence for an intracellular presence of chymase in the atrial myocytes (Figure 5).…”

Section: Novel Pathways Upstream From Angiotensin I –The New Research–mentioning

confidence: 99%

An evolving story of angiotensin-II-forming pathways in rodents and humans

et al. 2013

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Lessons learned from the characterization of the biological roles of angiotensin-(1-7) in opposing the vasoconstrictor, proliferative, and prothrombotic actions of angiotensin II created an underpinning for a more comprehensive exploration of the multiple pathways by which the blood and tissues renin angiotensin system regulates homeostasis and its altered state in disease processes. This review summarizes the progress that has been made in the novel exploration of intermediate shorter forms of angiotensinogen through the characterization of the expression and functions of the dodecapeptide angiotensin-(1-12) in the cardiac production of angiotensin II. The studies reveal significant differences in humans versus rodents regarding the enzymatic pathway by which angiotensin-(1-12) undergoes metabolism. Highlights of the research include the demonstration of chymase-direct formation of angiotensin II from angiotensin-(1-12) in human left atrial myocytes and left ventricular tissue, the presence of robust expression of angiotensin-(1-12) and chymase in the atrial appendage of subjects with resistant atrial fibrillation, and the preliminary observation of significantly higher angiotensin-(1-12) expression in human left atrial appendages.

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“…The substrate preferences and kinetics of substrate hydrolysis of dog mastocytoma chymase (4) appear to be very similar to those of the chymase purified from dog skin (18). The amino acid sequence ofdog chymase deduced from cDNA obtained from a dog cDNA library suggests substantial structural similarities between dog and rodent chymases (19).…”

Section: Methodsmentioning

confidence: 99%

Mast cell chymase potentiates histamine-induced wheal formation in the skin of ragweed-allergic dogs.

Rubinstein¹,

Nadel²,

Graf³

et al. 1990

J. Clin. Invest.

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Skin mast cells release the neutral protease chymase along with histamine during degranulation. To test the hypothesis that chymase modulates histamine-induced plasma extravasation, we measured wheal formation following intradermal injection of purified mast cell chymase and histamine into the skin of ragweed-allergic dogs. We found that chymase greatly augments histamine-induced wheal formation. The magnitude of the potentiating effect increases with increasing doses of chymase and becomes maximal -30 min after administration. Injection of chymase without histamine does not evoke wheal formation. The chymase potentiation of histamine-induced skin responses is prevented completely by pretreatment with the HI-receptor antagonist pyrilamine, and is prevented by inactivation of chymase with soybean trypsin inhibitor, suggesting that both histamine and preserved catalytic activity are required for the effects of chymase. To examine the effects of histamine and chymase released in situ in further experiments, we measured wheal size following local degranulation of mast cells by intradermal injection of ragweed antigen or compound 48/80. We found that pretreatment with either soybean trypsin inhibitor or pyrilamine markedly reduces ragweed antigen-or 48/80-induced wheal formation, supporting the results obtained by injection of exogenous chymase and histamine. These findings suggest a novel and important proinflammatory role for chymase in modulating the effects of histamine on vascular permeability during mast cell activation. (J. Clin. Invest. 1990. 86:555-559.) Key words: protease * immediate hypersensitivity * vascular permeability

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Dog mast cell chymase: molecular cloning and characterization

Cited by 52 publications

References 41 publications

Induction of chymase that forms angiotensin II in the monkey atherosclerotic aorta

Induction of chymase that forms angiotensin II in the monkey atherosclerotic aorta

An evolving story of angiotensin-II-forming pathways in rodents and humans

Mast cell chymase potentiates histamine-induced wheal formation in the skin of ragweed-allergic dogs.

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