## 3 Results
### Tissue RAS-Regulating Enzyme Activities
#### 3.7.7 Adrenal Cortex  
Figure 17 presents the soluble and membrane-bound forms of RAS-regulating specific enzyme activities in the adrenal cortex in WKY and SHRs receiving TW, NAB, TW/NAB, AB and TW/AB. The ACE activity remains largely unchanged across treatments and between both rat strains (Figure 17A).  
In the same way, the soluble specific APA activity showed no significant changes across beverage treatments in WKY or SHRs (Figure 17B). Regarding the membrane-bound APA activity, significant changes were only observed in WKY animals receiving NAB (\(p<0.05\)) or TW/AB (\(p<0.05\); Figure 17C).  
The soluble ASAP activity (Figure 17D) showed significant changes in neither WKY or SHRs across treatments, and the membrane-bound form, as for APA, showed significant changes only in WKY animals receiving NAB (\(p<0.05\)) or TW/AB (\(p<0.05\); Figure 17E).  
More pronounced changes appear for APN-specific activities. The soluble form was significantly decreased in WKY animals receiving NAB (\(p<0.05\)), AB (\(p<0.05\)) and TW/AB (\(p<0.01\); Figure 17F). The membrane-bound APN specific activity also decreased significantly in WKY animals with all beverage treatments (\(p<0.01\) in all cases); however, in SHRs, significant increases were found (\(p<0.05\) and \(p<0.01\)) with AB and TW/AB beverage intake (Figure 17G).  
Figure 16: (**A**) Angiotensin-converting enzyme (ACE) activity, and specific activities of soluble (**B**) and membrane-bound (**C**) aminopeptidase A (APA), soluble (**D**) and membrane-bound (**E**) aspartyl aminopeptidase (ASAP), soluble (**F**) and membrane-bound (**G**) aminopeptidase N (APN), and soluble (**H**) and membrane-bound (**I**) aminopeptidase B (APB) in the posterior pituitary of Wistar-Kyoto rats (WKY) and spontaneously hypertensive rats (SHRs). Experimental groups included animals provided with tap water (TW), alcohol-free beer (NAB), tap water or alcohol-free beer at their discretion (TW/NAB), alcoholic beer (AB), or tap water and alcoholic beer at their discretion (TW/AB). Results are presented as ACE activity in IU/L, and for APA, ASAP, APN and APB, in picomoles of the corresponding aminoacyl-\(\beta\)-naphthyllamide hydrolyzed per minute per milligram of protein (mean \(\pm\) SEM; \(n\) = 8; \({}^{*}\)\(p\)\(<\) 0.05; \({}^{**}\)\(\ast\)\(p\)\(<\) 0.01).  
Figure 17: (**A**) Angiotensin-converting enzyme (ACE) activity, and specific activities of soluble (**B**) and membrane-bound (**C**) aminopeptidase A (APA), soluble (**D**) and membrane-bound (**E**) aspartyl aminopeptidase (ASAP), soluble (**F**) and membrane-bound (**G**) aminopeptidase N (APN), and soluble (**H**) and membrane-bound (**I**) aminopeptidase B (APB) in the adrenal cortex of Wistar-Kyoto rats (WKY) and spontaneously hypertensive rats (SHRs). Experimental groups included animals provided with tap water (TW), alcohol-free beer (NAB), tap water or alcohol-free beer at their discretion (TW/NAB), alcoholic beer (AB), or tap water and alcoholic beer at their discretion (TW/AB). Results are presented as ACE activity in IU/L, and for APA, ASAP, APN and APB, in picomoles of the corresponding aminoacyl-\(\beta\)-naphthyllamide hydrolyzed per minute per milligram of protein (mean \(\pm\) SEM; \(n\) = 8; \({}^{\ast}\)\(p\)\(<\) 0.05; \({}^{\ast\ast}\)\(p\)\(<\) 0.01).  
The soluble APB specific activity decreased significantly only in WKY animals treated with TW/AB (\(p<0.05\) compared to TW and \(p<0.01\) compared to TW/NAB) (Figure 17H), whereas no significant changes were found in SHRs. In the same way, the membrane-bound APB (Figure 17I) significantly decreased in WKY animals in all beverage groups (\(p<0.05\) and \(p<0.01\)) but no significant changes were observed in SHRs (Figure 17I).