Nonenzymatic post-translational modification derived products: New biomarkers of protein aging
During their biological life, proteins are exposed in a cumulative way to irreversible nonenzymatic posttranslational modifications that are responsible for their molecular aging and generate specific by-products called 'posttranslational modification derived products' (PTMDPs). PTMDPs are...
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| Format: | Article |
| Language: | English |
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Society of Medical Biochemists of Serbia, Belgrade
2011-01-01
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| Series: | Journal of Medical Biochemistry |
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| Online Access: | https://scindeks-clanci.ceon.rs/data/pdf/1452-8258/2011/1452-82581103201G.pdf |
| _version_ | 1828397217319223296 |
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| author | Gillery Philippe |
| author_facet | Gillery Philippe |
| author_sort | Gillery Philippe |
| collection | DOAJ |
| description | During their biological life, proteins are exposed in a cumulative way to irreversible nonenzymatic posttranslational modifications that are responsible for their molecular aging and generate specific by-products called 'posttranslational modification derived products' (PTMDPs). PTMDPs are involved in the pathogenesis of various diseases such as diabetes mellitus, renal insufficiency and atherosclerosis, and are potential biomarkers in clinical practice. Nonenzymatic glycation refers to the spontaneous binding of glucose and reducing sugars to free amino groups and is amplified by oxidative processes (referred to as 'glycoxidation'). It generates many reactive by-products such as aldehydes and leads to the formation of 'advanced glycation end products' (AGEs). AGEs accumulate in vivo, alter tissue organization and activate membrane receptors such as RAGE, which triggers inflammatory responses. Carbamylation is due to the binding of isocyanic acid, formed in vivo either by spontaneous dissociation of urea or by action of myeloperoxidase on thiocyanate, and generates homocitrulline from lysine groups. Carbamylation leads to alteration of the structural and biological properties of proteins, and favors inflammation and atherosclerosis. PTMDPs may be assayed by different methods, among others LC-MS/MS or immunoassays, constitute a promising field of investigation in basic research and are potential major biomarkers in laboratory medicine. |
| first_indexed | 2024-12-10T08:42:48Z |
| format | Article |
| id | doaj.art-868703d6a668442d9f6f080960ba4f8f |
| institution | Directory Open Access Journal |
| issn | 1452-8258 1452-8266 |
| language | English |
| last_indexed | 2024-12-10T08:42:48Z |
| publishDate | 2011-01-01 |
| publisher | Society of Medical Biochemists of Serbia, Belgrade |
| record_format | Article |
| series | Journal of Medical Biochemistry |
| spelling | doaj.art-868703d6a668442d9f6f080960ba4f8f2022-12-22T01:55:47ZengSociety of Medical Biochemists of Serbia, BelgradeJournal of Medical Biochemistry1452-82581452-82662011-01-013032012061452-82581103201GNonenzymatic post-translational modification derived products: New biomarkers of protein agingGillery Philippe0Laboratory of Pediatric Biology and Research, University Hospital of Reims, France + Laboratory of Medical Biochemistry and Molecular Biology, Faculty of Medicine of Reims, FranceDuring their biological life, proteins are exposed in a cumulative way to irreversible nonenzymatic posttranslational modifications that are responsible for their molecular aging and generate specific by-products called 'posttranslational modification derived products' (PTMDPs). PTMDPs are involved in the pathogenesis of various diseases such as diabetes mellitus, renal insufficiency and atherosclerosis, and are potential biomarkers in clinical practice. Nonenzymatic glycation refers to the spontaneous binding of glucose and reducing sugars to free amino groups and is amplified by oxidative processes (referred to as 'glycoxidation'). It generates many reactive by-products such as aldehydes and leads to the formation of 'advanced glycation end products' (AGEs). AGEs accumulate in vivo, alter tissue organization and activate membrane receptors such as RAGE, which triggers inflammatory responses. Carbamylation is due to the binding of isocyanic acid, formed in vivo either by spontaneous dissociation of urea or by action of myeloperoxidase on thiocyanate, and generates homocitrulline from lysine groups. Carbamylation leads to alteration of the structural and biological properties of proteins, and favors inflammation and atherosclerosis. PTMDPs may be assayed by different methods, among others LC-MS/MS or immunoassays, constitute a promising field of investigation in basic research and are potential major biomarkers in laboratory medicine.https://scindeks-clanci.ceon.rs/data/pdf/1452-8258/2011/1452-82581103201G.pdfpost-translational modificationsglycationcarbamylationagingdiabetes mellituschronic renal failure |
| spellingShingle | Gillery Philippe Nonenzymatic post-translational modification derived products: New biomarkers of protein aging Journal of Medical Biochemistry post-translational modifications glycation carbamylation aging diabetes mellitus chronic renal failure |
| title | Nonenzymatic post-translational modification derived products: New biomarkers of protein aging |
| title_full | Nonenzymatic post-translational modification derived products: New biomarkers of protein aging |
| title_fullStr | Nonenzymatic post-translational modification derived products: New biomarkers of protein aging |
| title_full_unstemmed | Nonenzymatic post-translational modification derived products: New biomarkers of protein aging |
| title_short | Nonenzymatic post-translational modification derived products: New biomarkers of protein aging |
| title_sort | nonenzymatic post translational modification derived products new biomarkers of protein aging |
| topic | post-translational modifications glycation carbamylation aging diabetes mellitus chronic renal failure |
| url | https://scindeks-clanci.ceon.rs/data/pdf/1452-8258/2011/1452-82581103201G.pdf |
| work_keys_str_mv | AT gilleryphilippe nonenzymaticposttranslationalmodificationderivedproductsnewbiomarkersofproteinaging |