Glycation

Glycation (non-enzymatic glycosylation) is the covalent attachment of a sugar to a protein, lipid or nucleic acid molecule.[1] Typical sugars that participate in glycation are glucose, fructose, galactose, and their derivatives. Glycation is the non-enzymatic process responsible for many (e.g. micro and macrovascular) complications in diabetes mellitus[2] and is implicated in other diseases and in aging.[3][4][5]

In contrast with glycation, glycosylation is the enzyme-mediated ATP-dependent attachment of sugars to a protein or lipid.[1] Glycosylation occurs at defined sites on the target molecule. It is a common form of post-translational modification of proteins and is required for the functioning of the mature protein.

## Contents

* 1 Biochemistry
* 2 Biomedical implications
* 3 DNA glycation
* 4 See also
* 5 Additional reading
* 6 References

## Biochemistry

Glycation pathway via Amadori rearrangement (in HbA1c, R is typically N-terminal valine)[6] Imidazolones (R = CH2CH(OH)CH(OH)CH2OH) are typical glycation products. They arise by the condensation of 3-deoxyglucosone with the guanidine group of an arginine residue.[7]

Glycations occur mainly in the bloodstream to a small proportion of absorbed simple sugars. Fructose has approximately ten times the glycation activity of glucose, the primary body fuel.[8] Glycation can occur through Amadori reactions, Schiff base reactions, and Maillard reactions; which lead to advanced glycation end products (AGEs).[1]

## Biomedical implications

Red blood cells have a consistent lifespan of 120 days and are accessible for measurement of glycated hemoglobin. Measurement of HbA1c—the predominant form of glycated hemoglobin—enables medium-term blood sugar control to be monitored in diabetes.

Some glycation products are implicated in age-related chronic diseases, including cardiovascular diseases (endothelium, fibrinogen, and collagen) and Alzheimer's disease (amyloid proteins are side-products of the reactions progressing to AGEs).[9][10]

Long-lived cells (such as nerves and brain cells), long-lasting proteins (such as crystallins of the lens and cornea), and DNA can sustain substantial glycation over time. Damage by glycation results in stiffening of the collagen in blood vessel walls, increasing blood pressure, especially in diabetes.[11] Glycations also cause weakening of the collagen in blood vessel walls,[12] which may lead to micro- or macro-aneurysm; or strokes if in the brain.

A 2025 study reported that a combination of nicotinamide (a form of vitamin B3), ⍺-lipoic acid (ALA), thiamine (vitamin B1), pyridoxamine (a form of vitamin B6), and piperine reduced glycation damage in cell and mice models accompanied by non-muscle weight loss, apparently due to reduced Ghrelin and AMPK production.[13]

## DNA glycation

The term DNA glycation applies to DNA damage induced by reactive carbonyls (principally methylglyoxal and glyoxal) that are present in cells as by-products of sugar metabolism.[14] DNA glycation can cause mutation, breaks in DNA and cytotoxicity.[14] Guanine is the base most susceptible to glycation. Glycated DNA, as a form of damage, appears to be as frequent as oxidative DNA damage. Protein DJ-1 (also known as PARK7), is employed in the repair of glycated DNA bases in humans. DJ-1 Homologs have been identified in bacteria.[14]

## See also

* Advanced glycation end-product
* Alagebrium
* Fructose
* Galactose
* Glucose
* Glycosylation
* Glycated hemoglobin
* List of aging processes

## Additional reading

* "Failure of common glycation assays to detect glycation by fructose". Clin. Chem. 38 (7): 1301–3. July 1992. doi:10.1093/clinchem/38.7.1301. PMID 1623595.
* Vlassara H (June 2005). "Advanced glycation in health and disease: role of the modern environment". Annals of the New York Academy of Sciences 1043 (1): 452–60. doi:10.1196/annals.1333.051. PMID 16037266. Bibcode: 2005NYASA1043..452V.

## References

1. ↑ 1.0 1.1 1.2 Lima, M.; Baynes, J. W. (2013-01-01), Lennarz, William J.; Lane, M. Daniel, eds. (in en), Glycation, Waltham: Academic Press, pp. 405–411, doi:10.1016/b978-0-12-378630-2.00120-1, ISBN 978-0-12-378631-9, http://www.sciencedirect.com/science/article/pii/B9780123786302001201, retrieved 2020-12-16
2. ↑ Yan, S. F.; D'Agati, V.; Schmidt, A. M.; Ramasamy, R. (2007). "Receptor for Advanced Glycation Endproducts (RAGE): a formidable force in the pathogenesis of the cardiovascular complications of diabetes & aging". Current Molecular Medicine 7 (8): 699–710. doi:10.2174/156652407783220732. PMID 18331228.
3. ↑ Glenn, J.; Stitt, A. (2009). "The role of advanced glycation end products in retinal ageing and disease". Biochimica et Biophysica Acta (BBA) - General Subjects 1790 (10): 1109–1116. doi:10.1016/j.bbagen.2009.04.016. PMID 19409449.
4. ↑ Semba, R. D.; Ferrucci, L.; Sun, K.; Beck, J.; Dalal, M.; Varadhan, R.; Walston, J.; Guralnik, J. M. et al. (2009). "Advanced glycation end products and their circulating receptors predict cardiovascular disease mortality in older community-dwelling women". Aging Clinical and Experimental Research 21 (2): 182–190. doi:10.1007/BF03325227. PMID 19448391.
5. ↑ Semba, R.; Najjar, S.; Sun, K.; Lakatta, E.; Ferrucci, L. (2009). "Serum carboxymethyl-lysine, an advanced glycation end product, is associated with increased aortic pulse wave velocity in adults". American Journal of Hypertension 22 (1): 74–79. doi:10.1038/ajh.2008.320. PMID 19023277.
6. ↑ Yaylayan, Varoujan A.; Huyghues-Despointes, Alexis (1994). "Chemistry of Amadori Rearrangement Products: Analysis, Synthesis, Kinetics, Reactions, and Spectroscopic Properties". Critical Reviews in Food Science and Nutrition 34 (4): 321–69. doi:10.1080/10408399409527667. PMID 7945894.
7. ↑ Bellier, Justine; Nokin, Marie-Julie; Lardé, Eva; Karoyan, Philippe; Peulen, Olivier; Castronovo, Vincent; Bellahcène, Akeila (2019). "Methylglyoxal, a Potent Inducer of AGEs, Connects between Diabetes and Cancer". Diabetes Research and Clinical Practice 148: 200–211. doi:10.1016/j.diabres.2019.01.002. PMID 30664892.
8. ↑ "Role of fructose in glycation and cross-linking of proteins". Biochemistry 27 (6): 1901–7. March 1988. doi:10.1021/bi00406a016. PMID 3132203.
9. ↑ Münch, Gerald (27 February 1997). "Influence of advanced glycation end-products and AGE-inhibitors on nucleation-dependent polymerization of β-amyloid peptide". Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease 1360 (1): 17–29. doi:10.1016/S0925-4439(96)00062-2. PMID 9061036.
10. ↑ Munch, G; Deuther-Conrad W; Gasic-Milenkovic J. (2002). "Glycoxidative stress creates a vicious cycle of neurodegeneration in Alzheimer's disease — a target for neuroprotective treatment strategies?". Ageing and Dementia Current and Future Concepts. Journal of Neural Transmission. Supplementa. 62. pp. 303–307. doi:10.1007/978-3-7091-6139-5_28. ISBN 978-3-211-83796-2.
11. ↑ Soldatos, G.; Cooper ME (Dec 2006). "Advanced glycation end products and vascular structure and function". Curr Hypertens Rep 8 (6): 472–478. doi:10.1007/s11906-006-0025-8. PMID 17087858.
12. ↑ Lee, J. Michael; Samuel P. Veres (2019-04-02). "Advanced glycation end-product cross-linking inhibits biomechanical plasticity and characteristic failure morphology of native tendon". Journal of Applied Physiology 126 (4): 832–841. doi:10.1152/japplphysiol.00430.2018. PMID 30653412.
13. ↑ Wimer, Lauren A.; Kaneshiro, Kiyomi R.; Ramirez, Jessica; Bose, Neelanjan; Valdearcos, Martin; Shanmugam, Muniesh Muthaiyan; Farrera, Dominique O.; Singh, Parminder et al. (2025-10-28). "Glycation-lowering compounds inhibit ghrelin signaling to reduce food intake, lower insulin resistance, and extend lifespan" (in English). Cell Reports 44 (10). doi:10.1016/j.celrep.2025.116422. ISSN 2211-1247. PMID 41086114. PMC 12626231. https://www.cell.com/cell-reports/abstract/S2211-1247(25)01193-3.
14. ↑ 14.0 14.1 14.2 Richarme G, Liu C, Mihoub M, Abdallah J, Leger T, Joly N, Liebart JC, Jurkunas UV, Nadal M, Bouloc P, Dairou J, Lamouri A. Guanine glycation repair by DJ-1/Park7 and its bacterial homologs. Science. 2017 Jul 14;357(6347):208-211. doi: 10.1126/science.aag1095. Epub 2017 Jun 8. PMID 28596309

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