Chymase, recombinant human

Recent discoveries have implicated chymase to be a key mediator in cardiovascular and inflammatory cell signaling pathways. Sigma now offers recombinant human Chymase expressed in Pichia pastoris

Applications in: Angiotensin II Generation Big Endothelin Conversion ECM Degradation NO Production Inflammatory Cytokines Hypertension Apoptosis

Product Number C8118
EC 3.4.21.39
Synonyms: mast cell protease I; skeletal muscle protease; skin chymotryptic proteinase; mast cell serine proteinase, chymase; skeletal muscle (SK) protease¹

Physical properties and Specificity
Chymase is a cathepsin G-like, S1 serine proteinase found primarily in mast cells. It has a molecular mass of ~ 30 kDa, however its apparent molecular mass on SDS-PAGE is around 37 kDa.

Preferential cleavage: Phe-|-Xaa > Tyr-|-Xaa > Trp-|-Xaa > Leu-|-Xaa. ¹

Applications and Clinical Implications
Chymase plays an important role in generating angiotensin II in response to injury of vascular tissues. Inhibition of chymase may be useful for preventing vascular proliferation in grafted vessels.³ Cardiac chymase has been shown to participate directly in the pathophysiologic state after myocardial infarction in hamsters.⁴

Human chymase selectively converts big endothelin 1 to the 31 amino acid length peptide endothelin 1 [ET-1(1-31)]. ET-1(1-31) increases Ca²⁺ concentration and produces NO in endothelial cells through ETB.⁵ Chymase may contribute to development of induced dermatitis by promoting eosinophile infiltration.⁶ In addition chymase is reported to degrade the ECM, and processes procollagenase, inflammatory cytokines and other bioactive peptides. ⁷ Chymase inhibitors may find applications for the treatment of cardiovascular as well as inflammatory diseases.⁸

Chymase cleavage of stem cell factor yields a bioactive, soluble product. ⁹ Mast cell chymase induces apoptosis of vascular smooth muscle cells, suggesting that mast cells may participate in the apoptotic regulation of SMCs in atherosclerotic lesions. ¹⁰

Over expression of vascular chymase was found to result in the occurrence of hypertension in transgenic mice.¹¹ Chymase is a 137 amino acid, cathepsin G-like, serine proteinase found primarily mast cells.² Mast cell chymase is particularly abundant in the dermis of human skin. Human mast cell chymase was found to be essentially identical to cardiac chymase.2 It has a molecular mass of approximately 30 kDa.

Supplied as a solution in 20 mM Tris pH 7.6, 0.8M NaCl and 25% glycerol w/v.

Specific Activity: ≥ 40 units per mg protein (Bradford)

Unit Definition: One unit hydrolyzes one micromole of N-benzoyl-L-tyrosine ethyl ester (BTEE) per minute at pH 7.8 and 25°C. The assay buffer used to determine the enzyme activity contains 27 mM Tris-HCl, pH 7.8, with 150 mM NaCl and 0.43 mM BTEE.

Storage Temperature –20°C
Purity: ≥ 90% (SDS-PAGE)

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References

1. IUBMB Enzyme Nomenclature
2. Schechter, N.M., J. Immunol., 152, 4062-9 (1994).
3. Miyazaki, M., and Takai. S.J., Renin Angiotensin Aldosterone Syst., 1, 23-6 (2000).
4. Jin, D., et al., Life Sci., 71, 437-46 (2002).
5. Niwa, Y., et al., Life Sci., 67, 1103-9 (2000).
6. Tomimori, Y., et al., Lab. Invest., 82, 789-94 (2002)
7. Fukami H., et al., Curr Pharm Des., 4, 439-53 (1998)
8. Muto T and Fukami H., Idrugs., 12, 1141-50 (2002)
9. Longley, J., et al., Proc. Natl. Acad. Sci. USA., 94, 9017–9021 (1997)
10. Leskinen, M., et al., Arterioscler Thromb Vasc Biol, 21, 516-22 (2001)
11. Ju, H., et al., Proc. Natl. Acad. Sci. USA., 98, 7469–7474 (2001)