Glycation

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Glycate
)
Not to be confused with Glycosylation.

Glycation (non-enzymatic glycosylation) is the

diabetes mellitus.[5]

In contrast with glycation, glycosylation is the enzyme-mediated ATP-dependent attachment of sugars to 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.

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 the absorbed simple sugars:

advanced glycation end products (AGEs).[1]

Biomedical implications

Red blood cells have a consistent lifespan of 120 days and are accessible for 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 many age-related chronic diseases, including cardiovascular diseases (the endothelium, fibrinogen, and collagen are damaged) and Alzheimer's disease (amyloid proteins are side-products of the reactions progressing to AGEs).[9][10]

Long-lived cells (such as nerves and different types of brain cell), long-lasting proteins (such as

lens and cornea), and DNA can sustain substantial glycation over time. Damage by glycation results in stiffening of the collagen in the blood vessel walls, leading to high blood pressure, especially in diabetes.[11] Glycations also cause weakening of the collagen in the blood vessel walls,[12]
which may lead to micro- or macro-aneurysm; this may cause strokes if in the brain.

DNA glycation

The term DNA glycation applies to

PARK7), is employed in the repair of glycated DNA bases in humans, and homologs of this protein have also been identified in bacteria.[13]

See also

Additional reading

  • Ahmed N, Furth AJ (July 1992). "Failure of common glycation assays to detect glycation by fructose". Clin. Chem. 38 (7): 1301–3.
    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.
    S2CID 20952378
    .

References

  1. ^
    ISBN 978-0-12-378631-9
    , retrieved 2020-12-16
  2. PMID 19409449
    .
  3. PMID 19448391
    .
  4. PMID 19023277
    .
  5. PMID 18331228
    .
  6. PMID 7945894
    .
  7. S2CID 58631777
    .
  8. PMID 3132203
    .
  9. PMID 9061036
    .
  10. PMID 12456073
    .
  11. S2CID 31239347
    .
  12. PMID 30653412
    .
  13. ^ a b c 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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