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Systematic Review Article

Proatherogenic Importance of Carbamylation-induced Protein Damage and Type 2 Diabetes Mellitus: A Systematic Review

Author(s): Bahadir Simsek, Karolin Yanar and Ufuk Çakatay*

Volume 16, Issue 6, 2020

Page: [608 - 618] Pages: 11

DOI: 10.2174/1573399816666200107102918

Price: $65

Abstract

Introduction & Background: Protein carbamylation is a non-enzymatic and irreversible posttranslational process. It affects functions of numerous enzymes, hormones and receptors playing several roles in diabetes pathogenesis by changing their native structures. Detrimental consequences of oxidative protein damage comprise, but are not limited to glyoxidation, lipoxidation and carbonylation reactions. Since the carbamylated plasma proteins are strongly related to the glycemic control parameters of diabetes, they may have an additive value and emerge as potential biomarkers for the follow up, prognosis and treatment of diabetes mellitus.

Methods & Results: To conduct our systematic review, we used PubMed and Semantic Scholar, and used ‘Protein carbamylation and diabetes’ and ‘Protein carbamylation and atherosclerosis’ as keywords and looked into about five hundred manuscripts. Manuscripts that are not in English were excluded as well as manuscripts that did not mention carbamylation to maintain the focus of the present article. Similar to glycation, carbamylation is able to alter functions of plasma proteins and their interactions with endothelial cells and has been shown to be involved in the development of atherosclerosis.

Conclusion: At this stage, it seems clear that protein carbamylation leads to worse clinical outcomes. To improve patient care, but maybe more importantly to improve healthcare-prevention, we believe the next stage involves understanding how exactly protein carbamylation leads to worse outcomes and when and in what group of people anti-carbamylation therapies must be employed.

Keywords: Carbamylation, carbamylated proteins, diabetes, myeloperoxidase, thiocyanates, atherosclerosis.

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