Glycation of human serum albumin impairs binding to the glucagon-like peptide-1 analogue liraglutide

Soudahome, Angélique Gajahi; Catan, Aurélie; Giraud, Pierre; Kouao, Sandrine Assouan; Guérin-Dubourg, Alexis; Debussche, Xavier; Moullec, N. Le; Bourdon, Emmanuel; Bravo, Susana B.; Paradela-Dobarro, Beatriz; Meilhac, Olivier; Rondeau, Philippe; Couprie, Joël

doi:10.1074/jbc.m117.815274

Cited by 30 publications

(21 citation statements)

References 66 publications

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“…This effect might be explained by a lower affinity of transport proteins for vitamin D metabolites in diabetes mellitus due to the glycosylation process. Our idea is consistent with the literature data on the altered affinity of glycosylated albumin for some ligands (e.g., several drugs [ 46 , 47 ] and zinc [ 48 ]). This hypothesis is also supported by the lack of correlation between the measured and calculated free 25(OH)D in the diabetes group in contrast with the control group.…”

Section: Discussionsupporting

confidence: 92%

Evaluation of Vitamin D Metabolism in Patients with Type 1 Diabetes Mellitus in the Setting of Cholecalciferol Treatment

et al. 2020

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In this prospective controlled study, we examined 25 adults with adequately controlled (HbA1c level < 8.0%) type 1 diabetes mellitus (T1DM) and 49 conditionally healthy adults, intending to reveal the diversity of vitamin D metabolism in the setting of cholecalciferol intake at a therapeutic dose. All patients received a single dose (150,000 IU) of cholecalciferol aqueous solution orally. Laboratory assessments including serum vitamin D metabolites (25(OH)D3, 25(OH)D2, 1,25(OH)2D3, 3-epi-25(OH)D3 and 24,25(OH)2D3), free 25(OH)D, vitamin D-binding protein (DBP) and parathyroid hormone (PTH) as well as serum and urine biochemical parameters were performed before the intake and on Days 1, 3 and 7 after the administration. The studied groups had no significant differences in baseline parameters except that the patients with diabetes showed higher baseline levels of free 25(OH)D (p < 0.05). They also lacked a correlation between the measured and calculated free 25(OH)D in contrast to the patients from the control group (r = 0.41, p > 0.05 vs. r = 0.88, p < 0.05), possibly due to the glycosylation of binding proteins, which affects the affinity constant for 25(OH)D. The elevation of vitamin D levels after the administration of cholecalciferol was comparable in both groups, with slightly higher 25(OH)D3 levels observed in the diabetes group throughout the study since Day 1 (p < 0.05). Overall, our data indicate that in patients with adequately controlled T1DM 25(OH)D3 levels and the therapeutic response to cholecalciferol is similar to that in healthy individuals.

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Section: Discussionsupporting

confidence: 92%

Evaluation of Vitamin D Metabolism in Patients with Type 1 Diabetes Mellitus in the Setting of Cholecalciferol Treatment

et al. 2020

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“…Actually, if albumin and erythrocyte glycation was performed by using supraphysiological concentration of the glycating agent, such concentration was chosen to operate a rapid glycation model for long half-life proteins, 21 days and 120 days for albumin and hemoglobin, respectively. These vitro glycation models appeared relevant to what could be encountered in vivo as most of oxidative damages, identified in our in vitro glycated albumin and erythrocytes preparations, were retrieved in albumin and erythrocytes isolated from diabetics [10,15,69].…”

Section: Discussionmentioning

confidence: 90%

“…The glycoxidation process of this globular protein exerts adverse effects on its structural and functional integrity, particularly in terms of conformational changes and redox status, which may favor the formation of cross β-structure rich amyloid fibril [7,8]. Our group recently evidenced impaired drug binding capacity of albumin when glycoxidized [9,10]. Glycoxidized albumin was associated with metabolic disorders observed in diabetes mellitus, such as retinopathy, nephropathy and coronary artery disease [11].…”

Section: Introductionmentioning

confidence: 99%

Antirhea borbonica Aqueous Extract Protects Albumin and Erythrocytes from Glycoxidative Damages

et al. 2020

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Diabetes constitutes a major health problem associated with severe complications. In hyperglycemic conditions, chronically increased oxidation and glycation of circulating components lead to advanced glycation end-products (AGEs) formation, a key contributor in diabetes complication progression. In line with literature documenting the beneficial properties of herbal teas, this study evaluates the antioxidant/glycant properties of Antirhea borbonica (Ab). Ab aqueous extract effects were tested on human albumin or erythrocytes submitted to methyl glyoxal-mediated glycoxidative damages. By using mass spectrometry, Ab aqueous extracts revealed to be rich in polyphenols. All tested biomarkers of oxidation and glycation, such as AGE, ketoamine, oxidized thiol groups, were decreased in albumin when glycated in the presence of Ab aqueous extract. Ab extract preserve erythrocyte from methylglyoxal (MGO)-induced damages in terms of restored membrane deformability, reduced oxidative stress and eryptosis phenomenon. Antioxidant capacities of Ab extract on erythrocytes were retrieved in vivo in zebrafish previously infused with MGO. These results bring new evidences on the deleterious impacts of glycation on albumin and erythrocyte in diabetes. Furthermore, it reveals antioxidant and antiglycant properties of Ab that could be used for the dietary modulation of oxidative stress and glycation in hyperglycemic situations.

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“…[ 40 ] Glycation of albumin has been reported to impair its binding to liraglutide resulting in the variable therapeutic efficiency of liraglutide in patients, depending on the diabetes stage. [ 41 ] Future studies are envisioned to compare the binding of GLP1‐HL‐ABD to glycated and nonglycated albumin and at different stages of diabetes.…”

Section: Discussionmentioning

confidence: 99%

Recombinant Fusion of Glucagon‐Like Peptide‐1 and an Albumin Binding Domain Provides Glycemic Control for a Week in Diabetic Mice

Yousefpour

Varanko

Subrahmanyan

et al. 2020

Advanced Therapeutics

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Glucagon-like peptide-1 (GLP1) is an intestinally derived incretin currently under investigation for treatment of type 2 diabetes. The clinical application of GLP1 is limited by its short half-life, which necessitates frequent administration. To address this challenge, GLP1 is recombinantly synthesized as a fusion to an albumin binding domain (ABD). The native GLP1 sequence is engineered to inhibit an inactivating cleavage site and a rigid helical linker (HL) is utilized between the GLP1 and ABD to reduce interference of albumin binding by the ABD upon the ability of GLP1 to bind and activate its receptor. Upon subcutaneous administration (SC), the GLP1-HL-ABD fusion binds to endogenous albumin and exhibits an extended half-life of ≈44 h in mice. In a diabetic (db/db) mouse model, a single SC injection of GLP1-HL-ABD affords up to 7 d of glycemic control, which is significantly longer than the ≈12 h duration of glucose control provided by liraglutide, an albumin binding fatty acid derivative of GLP1 currently on the market for treatment of type 2 diabetes.

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Glycation of human serum albumin impairs binding to the glucagon-like peptide-1 analogue liraglutide

Cited by 30 publications

References 66 publications

Evaluation of Vitamin D Metabolism in Patients with Type 1 Diabetes Mellitus in the Setting of Cholecalciferol Treatment

Evaluation of Vitamin D Metabolism in Patients with Type 1 Diabetes Mellitus in the Setting of Cholecalciferol Treatment

Antirhea borbonica Aqueous Extract Protects Albumin and Erythrocytes from Glycoxidative Damages

Recombinant Fusion of Glucagon‐Like Peptide‐1 and an Albumin Binding Domain Provides Glycemic Control for a Week in Diabetic Mice

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