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Author Spotlight: In Silico Creation and Impact of Carbonylated Amino Acids on Protein Structure and Function
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Mechanisms and consequences of carbamoylation
Sigurd Delanghe1, Joris R Delanghe2, Reinhart Speeckaert2
1Department of Nephrology, Ghent University Hospital, De Pintelaan 185, 9000 Ghent, Belgium.
Nature Reviews. Nephrology
|August 1, 2017
Summary
Protein carbamoylation, a modification linked to cardiovascular disease and kidney issues, involves isocyanic acid binding to proteins. This review explores its effects, biomarkers, and strategies to reduce protein carbamoylation levels.
Area of Science:
- Biochemistry
- Pathophysiology
- Immunology
Background:
- Protein carbamoylation is a non-enzymatic post-translational modification.
- Isocyanic acid, derived from urea or thiocyanate, binds to protein amino groups.
- Carbamoylation is distinct from carbamylation, a reversible CO2 interaction.
Purpose of the Study:
- To review the process of protein carbamoylation.
- To evaluate existing biomarkers for carbamoylation.
- To discuss the link between carbamoylation and cardiovascular events in chronic kidney disease patients.
Main Methods:
- Literature review of protein carbamoylation.
- Analysis of pathophysiological effects of carbamoylated proteins.
- Evaluation of carbamoylation biomarkers such as homocitrulline.
Main Results:
- Carbamoylated proteins are associated with atherosclerosis, lipid metabolism, and immune dysfunction.
- Carbamoylated proteins are implicated in renal fibrosis and cardiovascular events.
- Biomarkers include homocitrulline, carbamoylated albumin, hemoglobin, and LDL.
Conclusions:
- Protein carbamoylation has diverse pathophysiological consequences.
- Effective biomarkers and strategies to lower carbamoylation load are crucial.
- Further research is needed to understand and manage carbamoylation's impact on health.
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