Literature DB >> 28690125

Carbamylation is a competitor of glycation for protein modification in vivo.

C Nicolas1, S Jaisson2, L Gorisse3, F J Tessier4, C Niquet-Léridon5, P Jacolot5, C Pietrement1, P Gillery6.   

Abstract

AIM: Chronic kidney disease (CKD) and diabetes mellitus are two diseases that accelerate protein molecular ageing through carbamylation and glycation reactions, characterized by the binding of urea-derived isocyanic acid and of sugars on proteins, respectively. These two reactions target the same protein amino groups and, thus, compete with each other. Such competition may arise especially in diabetic patients with nephropathy. This study aimed to evaluate their potential competitive effects in vitro and under conditions reproducing CKD and/or diabetes in vivo.
METHODS: Albumin was incubated in vitro with glucose, urea or cyanate. Carbamylation in vivo was enhanced in normal and diabetic (db/db) mice by either subtotal nephrectomy or cyanate consumption. Homocitrulline, carbamylated haemoglobin and furosine were measured by LC-MS/MS, fructosamine by colorimetric assay and HbA1c by immunological assay.
RESULTS: Reciprocal inhibition between carbamylation and glycation was observed during albumin incubations in vitro. Besides, 5 weeks after induction of CKD in vivo, plasma homocitrulline concentrations were similar in both diabetic and non-diabetic mice, whereas fructosamine and HbA1c were decreased (-23% and -42%, respectively) in diabetic mice with CKD compared with only diabetic ones. Fructosamine and HbA1c were also decreased in cyanate-spiked water-drinking mice compared with plain water-drinking diabetic mice.
CONCLUSION: Carbamylation competes with glycation in vivo, especially under conditions of high glycation. Thus, the classic markers of glycaemic control should be interpreted with caution in diabetic patients with CKD because of this competitive effect.
Copyright © 2017 Elsevier Masson SAS. All rights reserved.

Entities:  

Keywords:  Carbamylation; Chronic kidney disease; Competition; Diabetes mellitus; Glycation; HbA(1c)

Mesh:

Substances:

Year:  2017        PMID: 28690125     DOI: 10.1016/j.diabet.2017.05.006

Source DB:  PubMed          Journal:  Diabetes Metab        ISSN: 1262-3636            Impact factor:   6.041


  7 in total

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3.  Proteasome-dependent degradation of intracellular carbamylated proteins.

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4.  Carbamoylated Nail Proteins as Assessed by Near-Infrared Analysis are Associated with Load of Uremic Toxins and Mortality in Hemodialysis Patients.

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Review 5.  Carbamylated Proteins in Renal Disease: Aggravating Factors or Just Biomarkers?

Authors:  Laëtitia Gorisse; Stéphane Jaisson; Christine Piétrement; Philippe Gillery
Journal:  Int J Mol Sci       Date:  2022-01-05       Impact factor: 5.923

6.  Enrichment of apolipoprotein A-IV and apolipoprotein D in the HDL proteome is associated with HDL functions in diabetic kidney disease without dialysis.

Authors:  Monique F M Santana; Aécio L A Lira; Raphael S Pinto; Carlos A Minanni; Amanda R M Silva; Maria I B A C Sawada; Edna R Nakandakare; Maria L C Correa-Giannella; Marcia S Queiroz; Graziella E Ronsein; Marisa Passarelli
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7.  Carbamylation and glycation compete for collagen molecular aging in vivo.

Authors:  Camille Nicolas; Stéphane Jaisson; Laëtitia Gorisse; Frédéric J Tessier; Céline Niquet-Léridon; Philippe Jacolot; Christine Pietrement; Philippe Gillery
Journal:  Sci Rep       Date:  2019-12-04       Impact factor: 4.379

  7 in total

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