First Author | Ribeiro AA | Year | 2015 |
Journal | J Renin Angiotensin Aldosterone Syst | Volume | 16 |
Issue | 4 | Pages | 947-55 |
PubMed ID | 26216430 | Mgi Jnum | J:286484 |
Mgi Id | MGI:6403679 | Doi | 10.1177/1470320315595572 |
Citation | Ribeiro AA, et al. (2015) Characterization of the renal renin-angiotensin system in transgenic mice that express rat tonin. J Renin Angiotensin Aldosterone Syst 16(4):947-55 |
abstractText | INTRODUCTION: Tonin is an enzyme that is able to generate angiotensin II (Ang II) from angiotensin I (Ang I) or directly from angiotensinogen. Our goal was to characterize the renal renin-angiotensin system in transgenic mice that express rat tonin (TGM`(rTon)). MATERIALS AND METHODS: Mice were euthanized and the kidneys removed for analysis. Tonin activity was evaluated by radioimmunoassay and angiotensin I-converting enzyme (ACE) activity by HPLC. Tonin, ACE and angiotensin II-converting enzyme (ACE2) expression was analyzed by Western blotting. RESULTS: Tonin activity was significantly increased in TGM`(rTon) compared to their respective wild-type (WT) littermates (1.7 +/- 0.21 vs 0.11 +/- 0.02 nmol of Ang II/min/mg of protein). Tonin activity had a strong positive correlation with tonin expression in both TGM`(rTon) and their respective wild-type littermates. The ACE activity and expression levels of 65-kDa N-domain angiotensin I-converting enzyme isoform were significantly increased in the TGM`(rTon) when compared with WT. ACE2 expression levels were statistically significantly higher in the TGM`(rTon) when compared with WT. Angiotensin 1-7 (Ang(1-7)) and Ang I levels were significantly lower in the TGM`(rTon). CONCLUSIONS: We suggest that the environment of tonin abundance may increase N-domain ACE activity liberated by a secretase able to cleave somatic ACE. |