The Other Side of the Maillard Reaction

@article{citeulike:2712268, abstract = {The Maillard reaction plays an important role in eye lens aging and cataract formation. Methylglyoxal (MGO) is a metabolic dicarbonyl compound present in the lens. It reacts with arginine residues in lens proteins to form advanced glycation end products (AGEs), such as hydroimidazolones and argpyrimidine. alpha-Crystallin, comprising alphaA- and alphaB-crystallin, is a major protein of the lens and it functions as a chaperone protein. We have found that upon reaction with MGO, human alphaA-crystallin becomes a more effective chaperone. Modification of specific arginine residues to AGEs appears to be the reason. Mutation of these arginine residues to alanine mirrors the effect of MGO, suggesting neutralization of the positive charge on arginine residues as a cause for improved chaperone function. Reaction with MGO also blocks the loss of the chaperone function of alphaA-crystallin caused by nonenzymatic glycation by ascorbate and ribose. These findings suggest that low levels of MGO might help the lens remain transparent during aging.}, author = {Nagaraj, Ram H. and Biswas, Ashis and Miller, Antonia and Ito, Tomoko O. and Bhat, Manjunatha }, citeulike-article-id = {2712268}, doi = {10.1196/annals.1433.045}, journal = {Annals of the New York Academy of Sciences}, number = {1}, pages = {107--112}, posted-at = {2008-04-24 09:40:09}, priority = {2}, title = {The Other Side of the Maillard Reaction}, url = {http://www.blackwell-synergy.com/doi/abs/10.1196/annals.1433.045}, volume = {1126}, year = {2008} }

TY - JOUR ID - citeulike:2712268 L3 - citeulike-article-id:2712268 TI - The Other Side of the Maillard Reaction JF - Annals of the New York Academy of Sciences VL - 1126 IS - 1 SP - 107 EP - 112 N2 - The Maillard reaction plays an important role in eye lens aging and cataract formation. Methylglyoxal (MGO) is a metabolic dicarbonyl compound present in the lens. It reacts with arginine residues in lens proteins to form advanced glycation end products (AGEs), such as hydroimidazolones and argpyrimidine. alpha-Crystallin, comprising alphaA- and alphaB-crystallin, is a major protein of the lens and it functions as a chaperone protein. We have found that upon reaction with MGO, human alphaA-crystallin becomes a more effective chaperone. Modification of specific arginine residues to AGEs appears to be the reason. Mutation of these arginine residues to alanine mirrors the effect of MGO, suggesting neutralization of the positive charge on arginine residues as a cause for improved chaperone function. Reaction with MGO also blocks the loss of the chaperone function of alphaA-crystallin caused by nonenzymatic glycation by ascorbate and ribose. These findings suggest that low levels of MGO might help the lens remain transparent during aging. AU - Nagaraj, Ram AU - Biswas, Ashis AU - Miller, Antonia AU - Ito, Tomoko AU - Bhat, Manjunatha PY - 2008/// UR - http://www.blackwell-synergy.com/doi/abs/10.1196/annals.1433.045 ER -