Sciencemadness Discussion Board

A.G.E. content of foods

Various - 1-10-2009 at 05:24

Hi all,

I would like to find out how much of any AGE's (advanced glycation endproducts) are in commonly available foods. There days people are saying that AGE's are common in caramelized foods but I wonder what the actual numbers are e.g. such-and-such milligrams of this or that AGE per 100 grams of food. This is important because AGE's are believed to increase the rate of aging.

Does anyone here know where I might find actual data on this?

Thanks.

hissingnoise - 1-10-2009 at 06:20

If you eat only foods with bland unappetising flavours you'll live longer, save on food-bills (won't want to eat much) and time will seem to pass more slowly---a win-win situation. . .
I'm done for, I love foods cooked at unnaturally high temperatures just for that taste.
Quick search on AGEs gave over 2million hits!
Raw data on AGEs may be scarce as the AGE content of foods seems dependant on fat, protein, and sugar content, and on cooking times and temperatures.

[Edited on 1-10-2009 by hissingnoise]

kclo4 - 1-10-2009 at 11:33

Are you sure that eating them plays a roll in aging? I thought it was their formation in the body that really caused the problems.

Various - 1-10-2009 at 14:14

Quote: Originally posted by kclo4  
Are you sure that eating them plays a roll in aging? I thought it was their formation in the body that really caused the problems.


That's still an unknown, last I heard. If it turned out that eating them had no effect on health, I'd be all for it.

Ozone - 1-10-2009 at 16:01

AGEs are especially bad when they form in-vivo. That is, lysine-arginine dimers (pentosidine), Ne-carboxymethyllysine, argpyrimidine, etc. These serve to crosslink, amoung other things, collagen. This results in lowered tissue elasticity and, amoung other things, amyloidosis, hardened arteries and cataracts.

A study (if I can find it) found an equivalent amount of collagen crosslinking in a 27 year old uncontrolled diabetic and a 70 year hold.

In these cases, the blood sugar is forming AGEs with the free (usually N-e-NH2 lysine and Arginine) amino groups of nearby proteins. Maillard reaction (browning of food) happens at low temperatures, it just takes a long time, a high sugar titre, or both.

The analytical methods would involve the quantification of thing like pentosidine dimers. There is, IIRC a polyclonal antibody with a fluorescent tag which has been developed.

Cheers,

O3

OK, see the Who's Who of Maillard reaction, in-vivo, which should get you started!

Extracted from a presentation I gave on this in grad. school (carbohydrate chemistry is my thing):

* Friedman, E.A. (1999). Advanced Glycosylated End Products and Hyperglycemia in the Pathogenesis of Diabetic Complications. Diabetes Care. 22 (suppl. 2.) B65-B71.

* Sasaki, N., Fukatsu, R., Tsuzuki, K., Hayashi, Y., Yoshida, T., Fujii, N. Koike, T., Wakayama, I., Amano, N. and Makita, Z. (1998). Advanced Glycation End Products in Alzheimer’s Disease and Other Neurodegenerative Diseases. J. Am. Pathol. 153 (4), pp. 1149-1155.

* Ranjan, M., Nayak, S. and Rao, B.S. (2006). Immunochemical detection of glycated b- and g- crystallins in lens and their circulating autoantibodies (IhG) in streptozocin induced diabetic rat. Molecular Vision 12, pp. 1077-1085.

* Grandee, S.K. and Monnier, V.M. (1991). Mechanism of Formation of the Maillard Protein Cross-Link Pentosidine. J. Biol. Chem. 266 (18), pp. 11649-

* Sato, T., Shigamoto, N., Wu, X., Kikuchi, S., Yamagishi, S-i. and Takeuchi, M. (2006). Toxic Advanced Glycation End Products (TAGE) Theory in Alzheimer’s Disease. Am. J. Alzheimer’s Disease & Other Dementias. 21 (3), pp. 197-207.

* Kessel, L., Kalinin, S., Nagaraj, R.H., Larsen, M., Johansson, L.B.A. (2002). Time-resolved Steady-State Fluorescence Spectroscopic Studies of the Human Lens with comparison to Argpyrimidine, Pentosidine and 3-OH-kynurenine. Photochem. Photobiol. 76 (5), pp. 549-554.

* Monnier, V.M. and Cerami, A. (1981). Nonenzymatic Browning in vivo: Possible Process for Aging of Long-Lived proteins. Science, 211, pp. 491-493.

* Dyer, D.G., Dunn, J.A., Thorpe, S.R., Bailie, K.E., Lyons, T.J., McCance, D.R. and Baynes, J.W. (1993). Accumulation of Maillard Reaction Products in Skin Collagen in Diabetes and Aging. Am. Soc. Clin. Invest. 91, pp. 2463-2469.

* Farboud, B., A-K, A., Miyata, T., Hjelmeland, L.M. and Handa, J.T. (1999). Development of a Polyclonal Antibody with Broad Epitope Specificity for Advanced Glycation Endproducts and Localization of these Epitopes in Bruch’s Membrane of the Aging Eye. Mol. Vis. 5:11. Http://www. Molvis.org/molvis/v5/p11>







[Edited on 2-10-2009 by Ozone]

Various - 2-10-2009 at 08:36

Great, thanks for info.
Quote: Originally posted by Ozone  
AGEs are especially bad when they form in-vivo. That is, lysine-arginine dimers (pentosidine), Ne-carboxymethyllysine, argpyrimidine, etc. These serve to crosslink, amoung other things, collagen. This results in lowered tissue elasticity and, amoung other things, amyloidosis, hardened arteries and cataracts.

A study (if I can find it) found an equivalent amount of collagen crosslinking in a 27 year old uncontrolled diabetic and a 70 year hold.

In these cases, the blood sugar is forming AGEs with the free (usually N-e-NH2 lysine and Arginine) amino groups of nearby proteins. Maillard reaction (browning of food) happens at low temperatures, it just takes a long time, a high sugar titre, or both.

The analytical methods would involve the quantification of thing like pentosidine dimers. There is, IIRC a polyclonal antibody with a fluorescent tag which has been developed.

Cheers,

O3

OK, see the Who's Who of Maillard reaction, in-vivo, which should get you started!

Extracted from a presentation I gave on this in grad. school (carbohydrate chemistry is my thing):

* Friedman, E.A. (1999). Advanced Glycosylated End Products and Hyperglycemia in the Pathogenesis of Diabetic Complications. Diabetes Care. 22 (suppl. 2.) B65-B71.

* Sasaki, N., Fukatsu, R., Tsuzuki, K., Hayashi, Y., Yoshida, T., Fujii, N. Koike, T., Wakayama, I., Amano, N. and Makita, Z. (1998). Advanced Glycation End Products in Alzheimer’s Disease and Other Neurodegenerative Diseases. J. Am. Pathol. 153 (4), pp. 1149-1155.

* Ranjan, M., Nayak, S. and Rao, B.S. (2006). Immunochemical detection of glycated b- and g- crystallins in lens and their circulating autoantibodies (IhG) in streptozocin induced diabetic rat. Molecular Vision 12, pp. 1077-1085.

* Grandee, S.K. and Monnier, V.M. (1991). Mechanism of Formation of the Maillard Protein Cross-Link Pentosidine. J. Biol. Chem. 266 (18), pp. 11649-

* Sato, T., Shigamoto, N., Wu, X., Kikuchi, S., Yamagishi, S-i. and Takeuchi, M. (2006). Toxic Advanced Glycation End Products (TAGE) Theory in Alzheimer’s Disease. Am. J. Alzheimer’s Disease & Other Dementias. 21 (3), pp. 197-207.

* Kessel, L., Kalinin, S., Nagaraj, R.H., Larsen, M., Johansson, L.B.A. (2002). Time-resolved Steady-State Fluorescence Spectroscopic Studies of the Human Lens with comparison to Argpyrimidine, Pentosidine and 3-OH-kynurenine. Photochem. Photobiol. 76 (5), pp. 549-554.

* Monnier, V.M. and Cerami, A. (1981). Nonenzymatic Browning in vivo: Possible Process for Aging of Long-Lived proteins. Science, 211, pp. 491-493.

* Dyer, D.G., Dunn, J.A., Thorpe, S.R., Bailie, K.E., Lyons, T.J., McCance, D.R. and Baynes, J.W. (1993). Accumulation of Maillard Reaction Products in Skin Collagen in Diabetes and Aging. Am. Soc. Clin. Invest. 91, pp. 2463-2469.

* Farboud, B., A-K, A., Miyata, T., Hjelmeland, L.M. and Handa, J.T. (1999). Development of a Polyclonal Antibody with Broad Epitope Specificity for Advanced Glycation Endproducts and Localization of these Epitopes in Bruch’s Membrane of the Aging Eye. Mol. Vis. 5:11. Http://www. Molvis.org/molvis/v5/p11>







[Edited on 2-10-2009 by Ozone]