Procyanidin structure defines the extent and specificity of angiotensin I converting enzyme inhibition

التفاصيل البيبلوغرافية
العنوان: Procyanidin structure defines the extent and specificity of angiotensin I converting enzyme inhibition
المؤلفون: Cesar G. Fraga, Javier I. Ottaviani, Lucas Actis-Goretta, Juan Javier Villordo
المصدر: Biochimie. 88:359-365
بيانات النشر: Elsevier BV, 2006.
سنة النشر: 2006
مصطلحات موضوعية: Dimer, Serum albumin, Angiotensin-Converting Enzyme Inhibitors, Peptidyl-Dipeptidase A, Sodium Chloride, Random hexamer, Biochemistry, Catechin, Structure-Activity Relationship, chemistry.chemical_compound, Tetramer, Renin–angiotensin system, Animals, Biflavonoids, Humans, Proanthocyanidins, Quenching (fluorescence), Dose-Response Relationship, Drug, biology, Chemistry, Hydrolysis, Albumin, Endothelial Cells, Serum Albumin, Bovine, General Medicine, Angiotensin II, Enzyme Activation, Kinetics, Spectrometry, Fluorescence, biology.protein, Rabbits
الوصف: Recent reports have shown a decrease in blood pressure associated with the consumption of flavanol-containing foods. However, the mechanism behind this effect is not yet known. Previously we demonstrated that the flavanol epicatechin and its related oligomers, the procyanidins, inhibit angiotensin I converting enzyme (ACE) activity in vitro. In this study, we further characterized epicatechin monomer, dimer, tetramer and hexamer ACE inhibitory effect, by performing fluorescence quenching and kinetic assays, using angiotensin I as substrate. Assessment of ACE activity in cultured human umbilical vein endothelial cells (HUVEC) indicated that the tetramer was the most active inhibitor decreasing the formation of angiotensin II by 52% (P
تدمد: 0300-9084
الوصول الحر: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a92bf38ea3ca33a58b3768dd98d6d7ddTest
https://doi.org/10.1016/j.biochi.2005.10.001Test
حقوق: CLOSED
رقم الانضمام: edsair.doi.dedup.....a92bf38ea3ca33a58b3768dd98d6d7dd
قاعدة البيانات: OpenAIRE