A weakness of our technique is that during

A weakness of our technique is that during the early post-operative period without the scaffold of an enteric channel patients can be at risk for traumatic or difficult catheterization, with 3 of 6 requiring a visit. This appeared to be offset by having skilled and educated housestaff capable of recovering the channel. Although channel creation with an enteric conduit is the gold standard for ACE catheterizable channel, this technique and its limited success raise interesting questions as to whether a full enteric conduit is necessary, or whether simply a mucosa lined tract is adequate [17].
Conclusion
Disclosures
Introduction Angiotensin I-converting enzyme (ACE) is a zinc metallopeptidase that plays an important role in blood pressure regulation [1–3]. The ACE has two homologous catalytic domains, the N- and C-domains, which are able to cleave angiotensin I and bradykinin [4,5,2]. The C-domain of ACE is more efficient in cleaving angiotensin I into vasopressor angiotensin II [4]. However, reports regarding the bradykinin binding site to the ACE are still limited. This information is necessary to measure the strength of binding competition between bradykinin and the angiotensin I to the ACE, although the ACE inhibitors generally have a higher affinity for the bradykinin than the angiotensin I Y-27632 mg [5]. This knowledge is essential for developing more specific ACE inhibitors on angiotensin I binding site as a hypertension drug that has no side effects on cough. Our previous study suggested that Alu insertion (I) in the intron 16 of ACE resulted in premature codon termination, so the protein has only one active site in the N-domain while the Alu deletion allele (D) still has two active sites. The meta-analysis indicated that the D allele is related to higher levels of angiotensinogen that is associated with metabolic syndrome [6], while the I allele of ACE correlated with the development of Alzheimer’s disease [7]. Moreover, the I/D polymorphism in the ACE gene has been linked to several kinds of diseases, such as coronary artery disease [8], infections in post-operative cardiac valve surgery patients [9] and arterial hypertension [10].
Subjects and methods
Results
Discussion Angiotensin-converting enzyme (ACE) is an enzyme that plays a crucial role in controlling blood pressure by the cleavage of angiotensin I into angiotensin II, which triggers vasoconstriction. In addition, ACE also inactivates bradykinin, a substance of the function of which is to increase vasodilatation in the body. Thus, ACE works simultaneously to catalyse angiotensin I and bradykinin [2,3]. ACE has two independent catalytic domains [3–5]. The domains are capable of cleaving angiotensin I and bradykinin but differ in binding affinity [14]. The results of the docking analysis show that the binding affinity of angiotensin I to the N-domain is stronger to the C-domain, while the binding affinity of bradykinin is almost equal to both the N- and C-domain. Moreover, the binding affinity of ACE to bradykinin is stronger than that of angiotensin I. It can be concluded that ACE more preferably binds to bradykinin than angiotensin I, therefore, the inhibition of the bradykinin binding site on ACE is a promising target for developing antihypertension drugs. These data correspond with the previous study that demonstrated that ACE inhibitor has a higher binding affinity towards bradykinin than it has towards angiotensin I binding site [5]. Hence, ACE is the primary target for drugs used to control hypertension [19]. ACE gene variance due to insertion or deletion of Alu elements is predicted to have an influence on bradykinin catalysis. Further analysis shows that bradykinin binds equally strongly to the N- and C-domains of ACE. The data indicate that both ACE domains have a similar quality in bradykinin catalysis. This is in line with the previous study that found that deletion on either the N- or C-domain of ACE does not affect the level of bradykinin in the mice [3]. Thus, the ability of ACE to inactivate bradykinin is not affected by insertion or deletion. This is supported by the study that found that the bradykinin level in the serum of genotype II and DD does not show a significant difference. This is consistent with other studies in Japanese hypertensive patients receiving an ACE inhibitor [17,18].