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Expression of Angiotensin Converting Enzyme 2 (ACE2) in Mice Mesangial Cells
Author(s) -
Aragão Danielle Sanches,
Andrade Maria Claudina Camargo,
Casarini Dulce Elena
Publication year - 2009
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.23.1_supplement.1019.20
Subject(s) - renin–angiotensin system , angiotensin converting enzyme 2 , angiotensin ii , enzyme , chemistry , angiotensin converting enzyme , cytosol , biochemistry , endocrinology , medicine , microbiology and biotechnology , blood pressure , biology , receptor , covid-19 , infectious disease (medical specialty) , disease
ACE2 is a new component of renin angiotensin system (RAS), an important physiological regulator of blood pressure, fluid and salt balance. ACE2 discovery added a new level of complexity to this system once it is able to metabolize angiotensin II, a potent vasoconstrictor, to angiotensin (1‐7), a potent vasodilator with high catalytic efficiency. Thus, this enzyme can be considered an endogenous ACE inhibitor. The relation between ACE2 and blood pressure is still controversial but this enzyme acting as a RAS negative regulator could have a vasodilator and antihypertensive potential effects. Once mesangial cells present all the components of RAS, the aim of this study was verify the expression and characterize ACE2 in immortalized mesangial cells (IMC). We purified the enzyme 5.4 fold through ion exchange chromatography with a specific activity of 40.3 nM/mg and the homogeneity was visualized by SDS‐Page. The molecular mass determined was 60 kDa. Using Western Blotting the enzyme was recognized by a specific antibody. N‐terminal sequence was determined and showed similarity with ACE2 from different species. Purified ACE2 was able to hydrolyze angiotensin II into angiotensin (1‐7), and the optimum pH and chloride concentration were 7.5 and 200 mM respectively. Enzyme activity was stable at 4º and 37ºC and it was inhibited at 1, 10 and 100μM of DX600. In conclusion, the presence ACE2 in mesangial cells may contribute to the local generation of angiotensin1‐7 and modulation of renal hemodynamic, contributing to the comprehension of the RAS. Supported by FAPESP.