Protective ability and binding affinity of captopril towards serum albumin in an in vitro glycation model of diabetes mellitus

Mariee, Amr D.; Al‐Shabanah, Othman A.

doi:10.1016/j.jpba.2005.12.025

Cited by 11 publications

(6 citation statements)

References 39 publications

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“…The two major drug-binding sites are Sudlow site I and site II [170][171][172], but other sites for drug binding exist as well [173,174]. Drug binding to GA has been investigated for several drugs, including warfarin [175][176][177], acetohexamide [178], tolbutamide [179], phenylbutazone [180], diclofenac [181], captopril [182], diazepam [183], ketoprofen [130,184], and others. The observed effects of glycation on drug binding are drug and glycation dependent, are not generally predictable and sometime contradictory.…”

Section: Effect Of Glycation Of Albumin On Drug Bindingmentioning

confidence: 99%

Glycated Serum Albumin and AGE Receptors

Vetter

2015

Advances in Clinical Chemistry

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Section: Effect Of Glycation Of Albumin On Drug Bindingmentioning

confidence: 99%

Glycated Serum Albumin and AGE Receptors

Vetter

2015

Advances in Clinical Chemistry

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“…Angiotensin (Ang) II, generated from AngI by angiotensin‐converting enzyme (ACE), has been implicated in the development of progressive glomerulosclerosis via the regulation of intraglomerular haemodynamic changes and the modulation of glomerular mesangial cell proliferation and ECM formation. It has been reported that treatment with either an ACE inhibitor (ACEI) or an angiotensin AT 1 receptor antagonist can inhibit the accumulation of AGE and diminish the progression of vascular, renal and retinal complications in diabetic rats 9–11 . However, little is known about the impact of ACEI treatment on AGE–RAGE‐related signalling in animal models of hypertension.…”

Section: Introductionmentioning

confidence: 99%

“…It has been reported that treatment with either an ACE inhibitor (ACEI) or an angiotensin AT 1 receptor antagonist can inhibit the accumulation of AGE and diminish the progression of vascular, renal and retinal complications in diabetic rats. [9][10][11] However, little is known about the impact of ACEI treatment on AGE-RAGE-related signalling in animal models of hypertension. Benazepril, an ACEI, has been used to retard the progression of hypertension-or diabetes-related nephropathy.…”

Section: Introductionmentioning

confidence: 99%

Benazepril, an Angiotensin‐converting Enzyme Inhibitor, Alleviates Renal Injury in Spontaneously Hypertensive Rats by Inhibiting Advanced Glycation End‐product‐mediated Pathways

Liu

Pang

Zhu

et al. 2009

Clin Exp Pharma Physio

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1. Advanced glycation end-products (AGE) and their receptors (RAGE) have been implicated in renal damage in diabetes. The aim of the present study was to investigate the effects of benazepril, an angiotensin-converting enzyme inhibitor (ACEI), on the formation of AGE, the expression RAGE and other associated components in the oxidative stress pathway in spontaneously hypertensive rats (SHR). 2. Groups of SHR were treated with or without 10 mg/kg per day benazepril for 12 weeks. Systolic blood pressure (SBP) and angiotensin (Ang) II levels were evaluated in SHR and control Wistar-Kyoto (WKY) rats. Renal function was investigated by determining levels of proteinuria and glomerulosclerosis. Furthermore, reactive oxygen species (ROS) in the rat renal cortex were analysed using an H(2)O(2)-based hydroxyl radical-detection assay and the renal content of AGE, RAGE, NADPH oxidase p47phox, nuclear factor (NF)-kappaB p65, phosphorylated (p-) NF-kappaB p65, vascular cell adhesion molecule (VCAM)-1 and transforming growth factor (TGF)-beta1 was determined by immunohistochemistry, quantitative real-time polymerase chain reaction and western blot analysis. 3. Treatment with benazepril inhibited the formation of AngII, reduced SBP and alleviated renal lesions in SHR compared with both untreated SHR and control WKY rats. Benazepril treatment significantly suppressed the accumulation of AGE and expression of RAGE in the kidney of SHR. In addition, benazepril treatment reduced the upregulation of NADPH oxidase p47phox, ROS generation and NF-kappaB p65, p-NF-kappaB p65, VCAM-1 and TGF-beta1 expression in the kidney of SHR compared with both untreated SHR and control WKY rats. 4. The results of the present study provide new insights into the regulation by the renin-angiotensin system of AGE-RAGE, oxidative stress and nephropathy, increasing our understanding of the role of the RAS in nephropathy.

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“…Amino acid-and peptide-based drugs have also been used as AGE inhibitors due to their low toxicity and good metabolic functions (Shantharam et al 2013). Carnosine, a dipeptide of β-Ala-His found in chicken extract, was reported to form complexes with AGEs and prevent them from proceeding to full Maillard brown pigment formation (Seidler and Yeargans 2002;Mariee and Al-Shabanah 2006).…”

Section: Introductionmentioning

confidence: 99%

Brown pigment formation in heated sugar–protein mixed suspensions containing unmodified and peptically modified whey protein concentrates

Rongsirikul

Hongsprabhas

2015

J Food Sci Technol

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Commercial whey protein concentrate (WPC) was modified by heating the acidified protein suspensions (pH 2.0) at 80 °C for 30 min and treating with pepsin at 37 °C for 60 min. Prior to spray-drying, such modification did not change the molecular weights (MWs) of whey proteins determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). After spray-drying the modified whey protein concentrate with trehalose excipient (MWPC-TH), it was found that the α-lactalbumin (α-La) was the major protein that was further hydrolyzed the most. The reconstituted MWPC-TH contained β-lactoglobulin (β-Lg) as the major protein and small molecular weight (MW) peptides of less than 6.5 kDa. The reconstituted MWPC-TH had higher NH2 group, Trolox equivalent antioxidant capacity (TEAC), lower exposed aromatic ring and thiol (SH) contents than did the commercial WPC. Kinetic studies revealed that the addition of MWPC-TH in fructose-glycine solution was able to reduce brown pigment formation in the mixtures heated at 80 to 95 °C by increasing the activation energy (Ea) of brown pigment formation due to the retardation of fluoresced advanced glycation end product (AGEs) formation. The addition of MWPC to reducing sugar-glycine/commercial WPC was also able to lower brown pigment formation in the sterilized (121 °C, 15 min) mixed suspensions containing 0.1 M reducing sugar and 0.5-1.0 % glycine and/or commercial (P < 0.05). It was demonstrated that the modification investigated in this study selectively hydrolyzed α-La and retained β-Lg for the production of antibrowning whey protein concentrate.

show abstract

Protective ability and binding affinity of captopril towards serum albumin in an in vitro glycation model of diabetes mellitus

Cited by 11 publications

References 39 publications

Glycated Serum Albumin and AGE Receptors

Glycated Serum Albumin and AGE Receptors

Benazepril, an Angiotensin‐converting Enzyme Inhibitor, Alleviates Renal Injury in Spontaneously Hypertensive Rats by Inhibiting Advanced Glycation End‐product‐mediated Pathways

Brown pigment formation in heated sugar–protein mixed suspensions containing unmodified and peptically modified whey protein concentrates

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