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Angiotensin-I converting enzyme (ACE) regulates the levels of disparate bioactive peptides, notably converting angiotensin-I to angiotensin-II and degrading amyloid beta. ACE is a heavily glycosylated dimer, containing 4 analogous catalytic sites, and exists in membrane bound and soluble (sACE) forms. ACE inhibition is a frontline, FDA-approved, therapy for cardiovascular diseases yet is associated with significant side effects, including higher rates of lung cancer.
View Article and Find Full Text PDFTransport and action of sesame protein-derived ACE inhibitory peptides ITAPHW and IRPNGL.
Food Chem
January 2025
State Key Laboratory of Food Science and Resources, Nanchang University, No. 235 Nanjing East Road, Nanchang, Jiangxi, 330047, PR China; School of Food Science and Technology, Nanchang University, No. 235 Nanjing East Road, Nanchang, Jiangxi, 330047, PR China.
Vascular endothelial dysfunction is an important pathogenic factor in hypertension, in which angiotensin-converting enzyme (ACE) plays an important role. Peptides that bind to ACE may attenuate vascular endothelial dysfunction by altering the structure of ACE. This study demonstrated that ITAPHW and IRPNGL were resistant to simulated gastrointestinal fluid and were transported across the Caco-2 monolayer via the intercellular space, with ITAPHW showing a high apparent permeability coefficient of (1.
View Article and Find Full Text PDFBackground: Arterial hypertension and left ventricular hypertrophy and remodeling are independent cardiovascular risk factors in patients with Cushing's syndrome. Changes in the renin-angiotensin system and in the mineralocorticoid axis activity could be involved as potential mechanisms in their pathogenesis, in addition to cortisol excess.
Methods: In this ancillary study of our previous study prospectively investigating patients with ACTH-dependent Cushing's syndrome by cardiac magnetic resonance imaging (NCT02202902), 11 patients without any interfering medication were cross-sectionally compared to 20 control subjects matched for age, sex and body mass index.
Research Progress of Food-Derived Antihypertensive Peptides in Regulating the Key Factors of the Renin-Angiotensin System.
Nutrients
December 2024
Key Laboratory of Environmental Medicine and Engineering of Ministry of Education, Department of Nutrition and Food Hygiene, School of Public Health, Southeast University, Nanjing 210009, China.
Food protein-derived antihypertensive peptides have attracted substantial attention as a safer alternative for drugs. The regulation of the renin-angiotensin system (RAS) is an essential aspect underlying the mechanisms of antihypertensive peptides. Most of the identified antihypertensive peptides exhibit the angiotensin-converting enzyme (ACE) inhibitory effect.
View Article and Find Full Text PDFEffect of cooking treatment on protein digestibility, peptide profile and potential bioactive peptides of beef tripe during in vitro gastrointestinal digestion.
Food Chem
April 2025
College of Food Science, Southwest University, No.2 Tiansheng Road, Beibei District, Chongqing 400715, China; Chongqing Key Laboratory of Speciality Food Co-Built by Sichuan and Chongqing, No.2 Tiansheng Road, Beibei District, Chongqing 400715, China; Chongqing Engineering Research Center of Regional Food, No.2 Tiansheng Road, Beibei District, Chongqing 400715, China. Electronic address:
The purpose of this study was to understand the effects of cooking treatment on the protein hydrolysis of beef tripe and the release of potentially bioactive peptides using an in vitro gastrointestinal model. The results showed that digestion promoted the hydrolysis of proteins and release of free amino acids in beef tripe, but cooking treatment significantly reduced them. The sample of the cooked beef tripe after gastrointestinal digestion had the highest antioxidant activity.
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