Life Extension Magazine®
Live Longer By Changing How You Cook!
A list of over 500 dietary constituents reveals surprising differences in levels of glycation products depending on how foods are prepared. Foods cooked at high temperatures increase cancer risk and accelerate aging because of the harmful mutagens and advanced glycation end products they contain. Glycation reactions can be inhibited in one’s body using carnosine, benfotiamine, and pyridoxal-5-phosphate. Mutation damage is reduced in the presence of chlorophyllin and indole-3-carbinol.
Scientifically reviewed by Dr. Gary Gonzalez, MD, in October 2024. Written by: William Faloon.
There is a simple way to protect against disease, lose weight, and extend healthy life span. This method is not new to longtime Life Extension® members. Recent studies, however, mandate that we re-emphasize our food preparation guidelines.
Put simply, when you ingest foods cooked at high temperature, your body is exposed to dangerous levels of mutagens and advanced glycation end products.1,2
Mutagens damage DNA and increase cancer risk. Glycation products damage your body’s proteins which causes tissues to lose functionality and prematurely age.3-5
This article reveals startling findings about the magnitude of toxic glycation products formed in response to various cooking methods. An example of the impact “cooking methods” have on glycation risk can be seen on the adjacent column.1
| Cooking | Glycation Products |
| Method | (kilounits [kU]/serving) |
| Raw beef | 636 (low) |
| Microwaved beef | 2,418 (moderate) |
| Grilled beef | 6,674 (too high) |
| Pan fried beef | 9,052 (toxic) |
| Broiled beef hot dog | 10,143 (more toxic) |
Foods with high levels of glycation products happen to also have the greatest numbers of mutagens.6,7
The public does not appreciate the damage inflicted by eating high-temperature cooked foods. Since few people consume a “raw food” diet, we’re going to show how one can mitigate the deadly impact of glycation on your body’s living proteins.
In 2003, I described a study published in the Proceedings of the National Academy of Sciences showing that eating foods cooked at high temperature increases the rate at which we age.4 Scientists uncovered back then that ingestion of high-temperature cooked foods results in chronic inflammation and accelerated glycation of our body’s proteins.8
More recent studies confirm these dangers. For example, breast and prostate cancers are sharply increased in those who eat heavily cooked meat such as hamburgers.9-13
When any food is heated to a high temperature (over 300 degrees), chemical changes occur that inflict damage to our cells when we eat that food.14-16
Cooked food contains more advanced glycation end products than raw foods. Be it fat, carbohydrate, or protein, when exposed to high temperatures, toxic compounds form that you don’t want in your body.1
To put this in perspective, a recent study found that men who ate just 1.5 servings or more of processed meat or one or more servings of grilled red meat or well-done red meat a week increased their risk of advanced prostate cancer by 50%.17 Considering that some men eat high-temperature cooked meat every day, is it any wonder that aging men suffer epidemic rates of prostate cancer?
Recall the previous page of this article that shows that pan fried beef registers a toxic 9,052 kilounits of advanced glycation end products per serving.1 This may help explain why heavily cooked beef increases cancer risk.
The number of advanced glycation end products in a serving of bacon comes in higher at 11,905 kilounits.1 If cancer concerns you, I hope the data about more than 500 different foods that we provide at the end of this article will assist you in making healthier food choices.
Shed Fat Pounds By Avoiding High-Temperature Cooked Foods
A fascinating study shows that diabetics who consumed a low-temperature cooked diet lost weight compared to a group that consumed the same numbers of calories, carbohydrates, fats, and protein cooked at higher temperature. Not only did the low-temperature prepared diet facilitate weight loss, but there were also reductions in blood glucose.8
This six-week study showed that eating the same food cooked at low-temperature reduced glycated LDL by 33%, whereas diabetics consuming the same higher temperature prepared foods increased glycated LDL by 32%.8
Researchers have now identified a compound in overcooked foods that plays a major role in the development of abdominal obesity and its related diseases. The name of the compound is methyl-glyoxal. Mice with sustained exposure to methylglyoxal developed significant abdominal weight gain, early insulin resistance, significant inflammation/oxidation, and type II diabetes.18 Methylglyoxal is a type of advanced glycation end product that is produced when food is cooked with dry heat.19-22
Glycation destroys functioning proteins in the body and induces chronic inflammation, which in turn promotes weight gain.23-27
National Library Of Medicine Studies Describe “Glycation”
If one enters the term “advanced glycation end products” into the National Library of Medicine database, over 8,000 studies came up by mid-May 2015.
This includes studies that describe many diseases associated with glycation.28-31 They also reveal how the deadly effects of advanced glycation end products are related to their ability to promote oxidative stress and inflammation by cross-linking with body proteins, which alters protein structure and function.1,32-35
To understand the significance of this, each one of our typical cells has thousands of different proteins that together enable a cell to function and maintain its structure.36 Our enzymes, hormones, antibodies, neurotransmitters, collagen, and hemoglobin are all examples of molecules that must be protected against glycation reactions.37
The most accurate blood test of glucose control is to measure the percentage of glycated hemoglobin contained in red blood cells (i.e. hemoglobin A1c).38-40 While a glycated hemoglobin percentage up to 5.5% is considered normal,41 once it exceeds 6%, vascular disease incidence skyrockets.42 That tiny percentage increase (>0.5%) of glycated hemoglobin increases risk for diabetic complications,43 yet few doctors try to protect their patients against protein glycation other than by achieving tighter glucose control.
Why Are These Data Overlooked?
The acronym for advanced glycation end products is “AGEs.”1
Diabetics suffer a disproportional higher number of diseases from AGEs because high glucose blood levels are another cause of protein glycation.44
The role of AGEs in disease causation in diabetics and nondiabetics has been sadly overlooked by the medical mainstream, perhaps because there is relatively little they think they can do about it. It was also assumed that AGEs in foods were poorly absorbed. However, studies clearly show that AGEs contained in food are readily absorbed and contribute to formation of toxic advanced glycation end products (AGEs) in the body.45-47
The good news is that health-conscious individuals exert a significant amount of control over how quickly their proteins are destroyed by toxic glycation reactions. They can reduce the amount of simple sugars and starches they ingest and minimize their exposure to overcooked foods.
The availability of nutrients like carnosine,48-53 benfotiamine,54-60 and pyridoxal-5-phosphate61-65 represents a significant medical advance because they function as potent anti-glycation agents. This is important because toxic AGEs form within the body as a part of normal metabolism, and even healthy foods contain some level of advanced glycated end products.1
How Food Makers Mislead Consumers
As I was writing this article, I came across a local news story about a restaurant that was opening which was serving only “naturally raised meats” that would be free of genetic modification, antibiotics, hormones, etc. These healthy meats would then be served as “char-cooked” hamburgers and other burnt foods.66
From what you’ve learned so far, this kind of cooking results in the formation of large numbers of AGEs within these foods. In particular, grilling, broiling, roasting, searing, and frying propagate and accelerate AGEs formation in food.1,67,68 Yet some of these terms (such as “grilling”) are used on restaurant menus to imply these are good ways to prepare food.
A wide variety of common foods are exposed to cooking or thermal processing for reasons of protection against microorganisms and convenience, as well as to enhance flavor, color, and appearance. The large amount of AGEs contained in the modern diet is well-documented.8,67,68
Grilled salmon, for instance, is often labeled as a heart healthy choice, yet it contains lots of AGEs compared to microwaved cooked salmon.1
When mice consume diets high in AGEs, their rate of atherosclerosis69 and kidney disease skyrockets.70 Restriction of dietary AGEs prevents vascular and kidney dysfunction70,71 and diabetes,72 improves insulin sensitivity,73,74 and accelerates wound healing in mice.75
Studies in healthy humans show that dietary AGEs directly correlate with markers of oxidative stress.76 Restriction of AGEs in patients with diabetes8 or kidney disease77 as well as in healthy subjects78 reduces markers of oxidative stress and inflammation.
These findings from animal and human studies suggest that avoidance of AGEs in food helps delay chronic diseases,79 yet processed foods, fast foods, and foods served at even upscale restaurants are laden with AGEs.
Purporting that these foods are healthy to eat is highly misleading. At a minimum, when one has no choice but to consume AGEs-laden or high-glycemic foods, supplementation with anti-glycation nutrients such as carnosine, benfotiamine, and/or pyridoxal-5-phosphate should be considered.
Don’t “Cook” Yourself To Death… Protect Your Genes Against Overcooked Food
It has long been known that heavily cooked foods inflict massive damage to the genes.
A group at the University of Minnesota reported that women who ate overcooked hamburgers had a 50% greater risk of breast cancer than women who ate rare or medium hamburgers. The famous Iowa Women’s Health Study found that women who consistently eat well-done steak, hamburgers, and bacon have a 4.62-fold increased risk of breast cancer than women who consumed these meats rare or medium done.10
Cooking foods at high temperatures causes the formation of gene-mutating heterocyclic amines, which is why deep-fried foods are so dangerous to eat.80 Heterocyclic amines have been linked to prostate, breast, colorectal, esophageal, lung, liver, and other cancers.10,81-91 While health conscious people try to avoid foods that are known carcinogens, even grilled fish contains a potent dose of gene-mutating heterocyclic amines.92
While one can reduce their exposure to cancer-causing heterocyclic amines, it may be impossible to keep them from forming within the body. Enzymatic activities that naturally occur in the liver can inadvertently manufacture heterocyclic amines from otherwise harmless organic compounds.93
Neutralizing Dietary Carcinogens
One of the most important lines of defense against carcinogens consumed in the diet are agents that prevent gene mutation. Many antimutagenic agents have been identified in fruits and vegetables, the most potent being indole-3-carbinol and chlorophyllin.94,95
Life Extension® introduced members to the antimutagenic effects of chlorophyllin back in 1989. The recommendation to supplement with chlorophyllin was based on a study published in the journal Mutation Research96 showing that this plant extract was a highly effective antimutagenic agent.
What impressed us most about the Mutation Research study was that chlorophyllin suppressed the mutagenic activity of carcinogens such as fried pork, diesel emissions, and coal dust by more than 90%!96 We are aware of no other supplement that comes close to chlorophyllin’s ability to inhibit deadly gene mutations. Most Life Extension® members obtain 100 mg of chlorophyllin in a multi-ingredient supplement designed to be taken with the heaviest meal of the day.
The great majority of studies about chlorophyllin’s health benefits concern its antimutagenic and anticarcinogenic properties. Chlorophyllin “traps” heterocyclic hydrocarbon carcinogens by reacting with their “backbone,” making it impossible for them to form adducts with DNA which is a precursor to malignant transformation in cells.97,98
Additional Protection Against Carcinogens
Indole-3-carbinol (I3C) is found in cruciferous vegetables such as cabbage, cauliflower, and broccoli.99 When I3C was administered to rodents given cancer-causing chemicals (carcinogens), the number of tumors was reduced by up to 96%. I3C has been shown to extend the length of the time between exposure to carcinogens and development of tumors by nearly 200%.100
One of the ways I3C protects cells against cancerous changes is by preventing DNA damage.
A study from the Medical College of Ohio shows that I3C can cut the rate of DNA damage from chemicals in several organs by up to 95%.101 I3C significantly decreases DNA damage in white blood cells by up to 81%, the colon by up to 86%, and the liver by up to 72%. This would seem almost unbelievable if it hadn’t been confirmed by others who have shown that I3C can reduce DNA damage in other tissues by similar amounts.102
Based on this plethora of evidence, if one happens to eat overcooked food, it makes sense to take at the same time, 100 mg of chlorophyllin and/or 80 to 240 mg of indole-3-carbinol and other cruciferous vegetables extracts. Most Life Extension® members already obtain these nutrients in supplement formulas they take with meals.
Painstaking Development Of Antiglycating Nutrients
Back in 1998, a growing body of literature pointed to the antiglycation effect of a dipeptide nutrient called carnosine.103-106 The two amino acids that comprise carnosine are L-histidine and beta-alanine.
The problem was that the synthesis of histidine and beta-alanine into carnosine was so complicated and expensive that it was unaffordable to the public. We went to great lengths to enhance this method so that meaningful potencies could be obtained by our members.
Back in those early days, dietary supplement companies sold carnosine in 50 mg capsules. To illustrate how trivial this 50 mg dose is, 248 mg of carnosine (from meat) was given to human subjects. Carnosine levels were detected in the blood and steadily increased. However, within 5.5 hours, no carnosine was detected in the blood. The reason carnosine disappears so quickly is that the carnosinase enzyme quickly degrades it.107
With this study in mind, a dose of 50 mg of carnosine would only be expected to remain in the blood at meaningful levels for around one hour. To achieve near 24-hour protection against toxic glycation reactions in the body, it requires about 500 mg of carnosine to be taken twice a day.
When we launched the first high-potency carnosine supplement in the year 2000, it represented a major advance in enabling aging humans to protect their vital proteins from transforming into toxic advanced glycation end products (AGEs).
New Studies Corroborate Carnosine Health Benefits
Diabetics are the group of people most in need of protection from AGEs.
High blood glucose levels create internal glycation reactions that result in massive protein destruction.108
Recent studies reveal broad-spectrum protection in the diabetic model in response to carnosine or its analogs. Carnosine analogs are being patented for potential approval in the lucrative pharmaceutical (drug) marketplace.109
A 2014 study using carnosine in a mouse diabetic model showed huge reductions in measurements of atherosclerosis. The researchers who conducted this study concluded:
“…prolonged carnosine supplementation enhances plasma levels, and has novel and significant effects on atherosclerotic lesion lipid, collagen and macrophage levels. These data are consistent with greater lesion stability, a key goal in treatment of existing cardiovascular disease. Carnosine supplementation may therefore be of benefit in lowering triglyceride levels and suppressing plaque instability in diabetes-associated atherosclerosis.” 110
No one questions the fact that diabetes results in a state of accelerated formation of AGEs and atherosclerosis.111
Nondiabetics may delay this process, but nonetheless will suffer the adverse effects of AGEs unless they take steps to protect their proteins from transforming into advanced glycation end products.
Practical Anti-Glycation Cooking Changes
Foods cooked at high temperature and low moisture strongly induces formation of deadly AGEs (advanced glycation endproducts).2
Cooking the same foods using lower temperatures, high moisture, and/or pre-exposure to an acidified environment will limit new AGEs formation.2, 68
Regrettably, the toxic effects of high-temperature cooking and food processing are still not accepted health considerations, despite irrefutable evidence we presented more than 12 years ago.
Reducing intake of dietary AGEs can be achieved by increasing the consumption of properly prepared fish, legumes, vegetables, fruits, and whole grains and by reducing intake of solid fats, fatty meats, full-fat dairy products, and highly processed foods.
Cooking methods that produce relatively low AGEs levels include poaching, steaming, stewing, and boiling.1 As an example, the high AGE content of broiled chicken can be reduced by at least 80% when the same piece of chicken is boiled.68
The use of acidic marinades, such as lemon juice and vinegar, before cooking also limits AGEs formation in the food.1 These culinary practices are part of Mediterranean, Asian, and other cuisines and can be used to create tasty, easily prepared dishes.
Since most “junk” foods are cooked at extremely high temperatures, it makes sense to avoid french fries, hamburgers, potato chips, fried food, and most snacks. These foods not only contain lots of AGEs, but they also create other metabolic disorders that can induce degenerative disease.
Broad-Spectrum Protection Against Age-Accelerating Glycation
Most Life Extension® members follow a healthy lifestyle that helps prevent glycation and chronic inflammation.
Supplementing with 1,000 mg a day of carnosine,50,52,112 along with benfotiamine (50 to 500 mg per day),113-115 and pyridoxal-5-phosphate (100 to 200 mg per day)53,60,116,117 can further inhibit glycation reactions in the body.
Avoiding foods cooked at high temperature not only reduces pathological glycation processes, but also prevents the formation of gene-mutating toxins that are known carcinogens. When food is cooked at high temperatures, DNA readily mutates.14,118 This results in increased cancer risk.
With overwhelming evidence that overheated food is associated with accelerated aging and cancer, health-conscious individuals have a strong incentive to pay attention to how they prepare their food.
Mainstream doctors should be advising patients on safer ways to cook their food. This message is tragically still not getting out, despite numerous studies published in prestigious scientific journals.
The failure of hurried physicians to inform aging people about the need to protect against toxic AGEs is another reason why consumers need to look out for their own health.
The section after the references to this article lists over 500 common foods and their AGEs content per serving. This list provides practical guidance on what foods are safe, moderately safe and outright deadly.
For additional protection against advanced glycation end products (AGEs), consider daily supplementation of carnosine, benfotiamine and/or pyridoxal-5-phosphate.
For longer life,
William Faloon
References
- Uribarri J, Woodruff S, Goodman S, et al. Advanced glycation end products in foods and a practical guide to their reduction in the diet. J Am Diet Assoc. 2010 Jun;110(6):911-16.e12.
- Spivey A. A matter of degrees: advancing our understanding of acrylamide. Environ Health Perspect. 2010 Apr;118(4):A160-7.
- Ahmed N, Thornalley PJ. Advanced glycation endproducts: what is their relevance to diabetic complications? Diabetes Obes Metab. 2007 May;9(3):233-45.
- Fleming TH, Humpert PM, Nawroth PP, Bierhaus A. Reactive metabolites and AGE/RAGE-mediated cellular dysfunction affect the aging process: a mini review. Gerontology. 2011;57(5):435-43.
- Luevano-Contreras C, Chapman-Novakofski K. Dietary advanced glycation end products and aging. Nutrients. 2010 Dec;2(12):1247-65.
- Wuenschell GE, Tamae D, Cercillieux A, Yamanaka R, Yu C, Termini J. Mutagenic potential of DNA glycation: miscoding by (R)- and (S)-N2-(1-carboxyethyl)-2’-deoxyguanosine. Biochemistry. 2010 Mar 9;49(9):1814-21.
- Tamae D, Lim P, Wuenschell GE, Termini J. Mutagenesis and repair induced by the DNA advanced glycation end product N2-1-(carboxyethyl)-2’-deoxyguanosine in human cells. Biochemistry. 2011 Mar 29;50(12):2321-9.
- Vlassara H, Cai W, Crandall J, et al. Inflammatory mediators are induced by dietary glycotoxins, a major risk factor for diabetic angiopathy. Proc Natl Acad Sci U S A. 2002 Nov 26;99(24):15596-601.
- Deitz AC, Zheng W, Leff MA, et al. N-Acetyltransferase-2 genetic polymorphism, well-done meat intake, and breast cancer risk among postmenopausal women. Cancer Epidemiol Biomarkers Prev. 2000 Sep;9(9):905-10.
- Zheng W, Gustafson DR, Sinha R, et al. Well-done meat intake and the risk of breast cancer. J Natl Cancer Inst. 1998 Nov 18;90(22):1724-9.
- Sinha R, Gustafson DR, Kulldorff M, Wen WQ, Cerhan JR, Zheng W. 2-amino-1-methyl-6-phenylimidazo[4,5-b]pyridine, a carcinogen in high-temperature-cooked meat, and breast cancer risk. J Natl Cancer Inst. 2000 Aug 16;92(16):1352-4.
- Cross AJ, Peters U, Kirsh VA, et al. A prospective study of meat and meat mutagens and prostate cancer risk. Cancer Res. 2005 65(24):11779-84.
- Sinha R, Park Y, Graubard BI, et al. Meat and meat-related compounds and risk of prostate cancer in a large prospective cohort study in the United States. Am J Epidemiol. 2009 170(9):1165-77.
- Jägerstad M, Skog K. Genotoxicity of heat-processed foods. Mutat Res. 2005 Jul 1;574(1-2):156-72.
- Birlouez-Aragon I, Saavedra G, Tessier FJ, et al. A diet based on high-heat-treated foods promotes risk factors for diabetes mellitus and cardiovascular diseases.Am J Clin Nutr . 2010 May;91(5):1220-6.
- Available at: http://www.cancer.gov/cancertopics/factsheet/risk/cooked-meats. Accessed March 11, 2015.
- John EM, Stern MC, Sinha R, Koo J. Meat consumption, cooking practices, meat mutagens, and risk of prostate cancer. Nutr Cancer. 2011 63(4):525-37.
- Cai W, Ramdas M, Zhu L, Chen X, Striker GE, Vlassara H. Oral advanced glycation endproducts (AGEs) promote insulin resistance and diabetes by depleting the antioxidant defenses AGE receptor-1 and sirtuin 1. Proc Natl Acad Sci U S A. 2012 Sep 25;109(39):15888-93.
- Available at: http://lancastria.net/blog/tag/methylglyoxal. Accessed May 15, 2015.
- Lederer MO, Klaiber RG. Cross-linking of proteins by Maillard processes: characterization and detection of lysine-arginine cross-links derived from glyoxal and methylglyoxal. Bioorg Med Chem. 1999 Nov;7(11):2499-507.
- Mosquera JA. Role of the receptor for advanced glycation end products (RAGE) in inflammation. Invest Clin. 2010 Jun;51(2):257-68.
- Vlassara H, Uribarri J. Advanced glycation end products (AGE) and diabetes: cause, effect, or both? Curr Diab Rep. 2014 Jan;14(1):453.
- Uribarri J, Cai W, Sandu O, Peppa M, Goldberg T, Vlassara H. Diet-derived advanced glycation end products are major contributors to the body’s AGE pool and induce inflammation in healthy subjects. Ann N Y Acad Sci. 2005 Jun;1043:461-6.
- Invitti C. Obesity and low-grade systemic inflammation. Minerva Endocrinol. 2002 Sep;27(3):209-14.
- Engström G, Hedblad B, Stavenow L, Lind P, Janzon L, Lindgärde F. Inflammation-sensitive plasma proteins are associated with future weight gain. Diabetes. 2003 Aug;52(8):2097-101.
- Xu H, Barnes GT, Yang Q, et al. Chronic inflammation in fat plays a crucial role in the development of obesity-related insulin resistance. J Clin Invest. 2003 Dec;112(12):1821-30.
- Fogarty AW, Glancy C, Jones S, Lewis SA, McKeever TM, Britton JR. A prospective study of weight change and systemic inflammation over 9 y. Am J Clin Nutr. 2008 Jan;87(1):30-5.
- Nawale RB, Mourya VK, Bhise SB. Non-enzymatic glycation of proteins: a cause for complications in diabetes. Indian J Biochem Biophys. 2006 Dec;43(6):337-44.
- Cárdenas-León M, Díaz-Díaz E, Argüelles-Medina R, Sánchez Canales P, Díaz-Sánchez V, Larrea F. Glycation and protein crosslinking in the diabetes and ageing pathogenesis. Rev Invest Clin. 2009 Nov-Dec;61(6):505-20.
- Münch G, Thome J, Foley P, Schinzel R, Riederer P. Advanced glycation endproducts in ageing and Alzheimer’s disease. Brain Res Brain Res Rev. 1997 Feb;23(1-2):134-43. Review.
- Goldin A, Beckman JA, Schmidt AM, Creager MA. Advanced glycation end products: sparking the development of diabetic vascular injury. Circulation. 2006 Aug 8;114(6):597-605. Review.
- Eble AS, Thorpe SR, Baynes JW. Nonenzymatic glucosylation and glucose-dependent cross-linking of protein. J Biol Chem. 1983 Aug 10;258(15):9406-12.
- Vlassara H. The AGE-receptor in the pathogenesis of diabetic complications. Diabetes Metab Res Rev. 2001 Nov-Dec;17(6):436-43.
- Schmidt AM, Yan SD, Wautier JL, Stern D. Activation of receptor for advanced glycation end products: a mechanism for chronic vascular dysfunction in diabetic vasculopathy and atherosclerosis. Circ Res. 1999 Mar 19;84(5):489-97.
- Singh VP, Bali A, Singh N, Jaggi AS. Advanced Glycation End Products and Diabetic Complications. Korean J Physiol Pharmacol. 2014;18(1):1-14.
- Nagaraj N, Wisniewski JR, Geiger T, et al. Deep proteome and transcriptome mapping of a human cancer cell line. Mol Syst Biol. 2011;7:548.
- Available at: http://www.medicalnewstoday.com/articles/196279.php. Accessed March 13, 2012.
- Haddadinezhad S, Ghazaleh N. Relation of fasting and postprandial and plasma glucose with hemoglobinA1c in diabetics. Int J Dev Ctries. 2010;30(1):8-10.
- Chalew SA, McCarter RJ, Thomas J, Thomson JL, Hempe JM. A comparison of the Glycosylation Gap and Hemoglobin Glycation Index in patients with diabetes. J Diabetes Complications. 2005 Jul-Aug;19(4):218-22.
- International Expert Committee. International Expert Committee report on the role of the A1C assay in the diagnosis of diabetes. Diabet Care 2009 Jul;32(7):1327-34.
- Edelman D, Olsen MK, Dudley TK, Harris AC, Oddone EZ. Utility of hemoglobin A1c in predicting diabetes risk. J Gen Int Med. 2004;19(12):1175-80.
- Ghazanfari Z, Haghdoost AA, Alizadeh SM, Atapour J, Zolala F. A comparison of HbA1c and fasting blood sugar tests in general population. Int J Preven Med 2010;1(3):187-94.
- Zhang X, Gregg EW, Williamson DF, et al. A1C Level and Future Risk of Diabetes: A Systematic Review. Diabet Care. 2010;33(7):1665-73.
- Negre-Salvayre A, Salvayre R, Augé N, Pamplona R, Portero-Otín M. Hyperglycemia and glycation in diabetic complications. Antioxid Redox Signal. 2009 Dec;11(12):3071-109.
- Cai W, He JC, Zhu L, et al. Oral glycotoxins determine the effects of calorie restriction on oxidant stress, age-related diseases, and lifespan. Am J Pathol. 2008 Aug;173(2):327-36.
- Koschinsky T, He CJ, Mitsuhashi T, et al. Orally absorbed reactive glycation products (glycotoxins): an environmental risk factor in diabetic nephropathy. Proc Natl Acad Sci U S A. 1997 Jun 10;94(12):6474-9.
- He C, Sabol J, Mitsuhashi T, Vlassara H. Dietary glycotoxins: inhibition of reactive products by aminoguanidine facilitates renal clearance and reduces tissue sequestration. Diabetes. 1999 Jun;48(6):1308-15.
- Reddy VP, Garrett MR, Perry G, et al. Carnosine: a versatile antioxidant and antiglycating agent. Sci Aging Knowledge Environ. 2005 May 4;2005(18):pe12.
- Brownson C, Hipkiss AR. Carnosine reacts with a glycated protein. Free Radic Biol Med. 2000 May 15;28(10):1564-70.
- Seidler NW, Yeargans GS. Effects of thermal denaturation on protein glycation. Life Sci. 2002 Mar 1;70(15):1789-99.
- Hobart LJ, Seibel I, Yeargans GS, Seidler NW. Anti-crosslinking properties of carnosine: significance of histidine. Life Sci. 2004 Jul 30;75(11):1379-89.
- Alhamdani MS, Al-Azzawie HF, Abbas FK. Decreased formation of advanced glycation end-products in peritoneal fluid by carnosine and related peptides. Perit Dial Int. 2007 Jan-Feb;27(1):86-9.
- Pietkiewicz J, Bronowicka-Szydełko A, Dzierzba K, Danielewicz R, Gamian A. Glycation of the muscle-specific enolase by reactive carbonyls: effect of temperature and the protection role of carnosine, pyridoxamine and phosphatidylserine. Protein J. 2011 Mar;30(3):149-58.
- Stirban A, Negrean M, Stratmann B, et al. Benfotiamine prevents macro- and microvascular endothelial dysfunction and oxidative stress following a meal rich in advanced glycation end products in individuals with type 2 diabetes. Diabetes Care. 2006 Sep;29(9):2064-71.
- Pomero F, Molinar Min A, La Selva M, Allione A, Molinatti GM, Porta M. Benfotiamine is similar to thiamine in correcting endothelial cell defects induced by high glucose. Acta Diabetol. 2001 38(3):135-8.
- Katare RG, Caporali A, Oikawa A, Meloni M, Emanueli C, Madeddu P. Vitamin B1 analog benfotiamine prevents diabetes-induced diastolic dysfunction and heart failure through Akt/Pim-1-mediated survival pathway. Circ Heart Fail. 2010 Mar;3(2):294-305.
- Hammes HP, Du X, Edelstein D, et al. Benfotiamine blocks three major pathways of hyperglycemic damage and prevents experimental diabetic retinopathy. Nat Med. 2003 Mar;9(3):294-9.
- Balakumar P, Rohilla A, Krishan P, Solairaj P, Thangathirupathi A. The multifaceted therapeutic potential of benfotiamine. Pharmacol Res. 2010 Jun;61(6):482-8.
- Kihm LP, Müller-Krebs S, Klein J, et al. Benfotiamine protects against peritoneal and kidney damage in peritoneal dialysis. J Am Soc Nephrol. 2011 May;22(5): 914-26.
- Syngle A, Vohra K, Garg N, Kaur L, Chand P. Advanced glycation end-products inhibition improves endothelial dysfunction in rheumatoid arthritis. Int J Rheum Dis. 2012 Feb;15(1):45-55.
- Voziyan PA, Hudson BG. Pyridoxamine as a multifunctional pharmaceutical: targeting pathogenic glycation and oxidative damage. Cell Mol Life Sci. 2005 Aug;62(15):1671-81.
- Higuchi O, Nakagawa K, Tsuzuki T, Suzuki T, Oikawa S, Miyazawa T. Aminophospholipid glycation and its inhibitor screening system: a new role of pyridoxal 5’-phosphate as the inhibitor. J Lipid Res. 2006 May;47(5):964-74.
- Voziyan PA, Metz TO, Baynes JW, Hudson BG. A post-Amadori inhibitor pyridoxamine also inhibits chemical modification of proteins by scavenging carbonyl intermediates of carbohydrate and lipid degradation. J Biol Chem. 2002 Feb 1;277(5):3397-403.
- Chetyrkin SV, Zhang W, Hudson BG, Serianni AS, Voziyan PA. Pyridoxamine protects proteins from functional damage by 3-deoxyglucosone: mechanism of action of pyridoxamine. Biochemistry. 2008 Jan 22;47(3):997-1006.
- Onorato JM, Jenkins AJ, Thorpe SR, Baynes JW. Pyridoxamine, an inhibitor of advanced glycation reactions, also inhibits advanced lipoxidation reactions. Mechanism of action of pyridoxamine. J Biol Chem. 2000 Jul 14;275(28):21177-84.
- Available at: http://www.sun-sentinel.com/features/deals-shopping/fl-frankeys-hallandale-beach-20150225-story.html. Accessed March 6, 2015.
- O’Brien J, Morrissey PA. Nutritional and toxicological aspects of the Maillard browning reaction in foods. Crit Rev Food Sci Nutr. 1989 28(3):211-48.
- Goldberg T, Cai W, Peppa M, et al. Advanced glycoxidation end products in commonly consumed foods. J Am Diet Assoc. 2004 Aug;104(8):1287-91.
- Lin RY, Choudhury RP, Cai W, et al. Dietary glycotoxins promote diabetic atherosclerosis in apolipoprotein E-deficient mice. Atherosclerosis. 2003 Jun;168(2):213-20.
- Zheng F, He C, Cai W, Hattori M, Steffes M, Vlassara H. Prevention of diabetic nephropathy in mice by a diet low in glycoxidation products. Diabetes Metab Res Rev. 2002 May-Jun;18(3):224-37.
- Lin RY, Reis ED, Dore AT, et al. Lowering of dietary advanced glycation endproducts (AGE) reduces neointimal formation after arterial injury in genetically hypercholesterolemic mice. Atherosclerosis. 2002 Aug;163(2):303-11.
- Peppa M, He C, Hattori M, McEvoy R, Zheng F, Vlassara H. Fetal or neonatal low-glycotoxin environment prevents autoimmune diabetes in NOD mice. Diabetes. 2003 Jun;52(6):1441-8.
- Hofmann SM, Dong HJ, Li Z, et al. Improved insulin sensitivity is associated with restricted intake of dietary glycoxidation products in the db/db mouse. Diabetes. 2002 Jul;51(7):2082-9.
- Sandu O, Song K, Cai W, Zheng F, Uribarri J, Vlassara H. Insulin resistance and type 2 diabetes in high-fat-fed mice are linked to high glycotoxin intake. Diabetes. 2005 Aug;54(8):2314-9.
- Peppa M, Brem H, Ehrlich P, et al. Adverse effects of dietary glycotoxins on wound healing in genetically diabetic mice. Diabetes. 2003 Nov;52(11):2805-13.
- Uribarri J, Cai W, Peppa M, et al. Circulating glycotoxins and dietary advanced glycation endproducts: two links to inflammatory response, oxidative stress, and aging. J Gerontol A Biol Sci Med Sci. 2007 Apr;62(4):427-33.
- Harcourt BE, Sourris KC, Coughlan MT, Walker KZ, et al. Targeted reduction of advanced glycation improves renal function in obesity. Kidney Int. 2001. Jul;80(2):190-8.
- Vlassara H, Cai W, Goodman S, et al. Protection against loss of innate defenses in adulthood by low advanced glycation end products (AGE) intake: role of the antiinflammatory AGE receptor-1. J Clin Endocrinol Metab. 2009 Nov;94(11):4483-91.
- Vlassara H, Uribarri J. Glycoxidation and diabetic complications: modern lessons and a warning? Rev Endocr Metab Disord. 2004 Aug;5(3):181-8. Review.
- Sinha R, Kulldorff M, Chow WH, Denobile J, Rothman N. Dietary intake of heterocyclic amines, meat-derived mutagenic activity, and risk of colorectal adenomas. Cancer Epidemiol Biomarkers Prev. 2001 May;10(5):559-62.
- Koutros S, Berndt SI, Sinha R, et al. Xenobiotic metabolizing gene variants, dietary heterocyclic amine intake, and risk of prostate cancer. Cancer Res. 2009 Mar 1;69(5):1877-84.
- De Stefani E, Ronco A, Mendilaharsu M, Guidobono M, Deneo-Pellegrini H. Meat intake, heterocyclic amines, and risk of breast cancer: a case-control study in Uruguay. Cancer Epidemiol Biomarkers Prev. 1997 Aug;6(8):573-81.
- Cross AJ, Freedman ND, Ren J, et al. Meat consumption and risk of esophageal and gastric cancer in a large prospective study. Am J Gastroenterol. 2011 Mar;106(3):432-42.
- Thorgeirsson UP, Gomez DE, Lindsay CK, Sinha CC, Adamson RH. Liver tumors and possible preneoplastic lesions, induced by a food-derived heterocyclic amine in cynomolgus monkeys; a study of histology and cytokeratin expression. Liver. 1996 Apr;16(2):71-83.
- Sugimura T, Wakabayashi K, Ohgaki H, Takayama S, Nagao M, Esumi H. Heterocyclic amines produced in cooked food: unavoidable xenobiotics. Princess Takamatsu Symp. 1990;21:279-88.
- Ward MH, Sinha R, Heineman EF, Rothman N, et al. Risk of adenocarcinoma of the stomach and esophagus with meat cooking method and doneness preference. Int J Cancer 1997 mar 28;71(1):14-9.
- Available at: http://www.cancer.gov/cancertopics/causes-prevention/risk/diet/cooked-meats-fact-sheet. Accessed March 13, 2015.
- Sinha R, Chow WH, Kulldorff M, Denobile J, Butler J, Garcia-Closas M, Weil R, Hoover RN, Rothman N. Well-done, grilled red meat increases the risk of colorectal adenomas. Cancer Res. 1999 Sep 1;59(17):4320-4.
- Sinha R, Kulldorff M, Swanson CA, Curtin J, Brownson RC, Alavanja MC. Dietary heterocyclic amines and the risk of lung cancer among Missouri women. Cancer Res. 2000 Jul 15;60(14):3753-6.
- Ferrucci LM, Sinha R, Ward MH. Meat and components of meat and the risk of bladder cancer in the NIH-AARP Diet and Health Study. Cancer. 2010 Sep 15;116(18):4345-53.
- Stolzenberg-Solomon RZ, Cross AJ, Silverman DT. Meat and meat-mutagen intake and pancreatic cancer risk in the NIH-AARP cohort. Cancer Epidemiol Biomarkers Prev. 2007 Dec;16(12):2664-75.
- Gross GA, Gruter A. Quantitation of mutagenic/carcinogenic heterocyclic aromatic amines in food products. J Chromatogr. 1992 Feb 21;592(1-2):271-8.
- Guengerich FP, Shimada T, Bondon A, Macdonald TL. Cytochrome P-450 oxidations and the generation of biologically reactive intermediates. Adv Exp Med Biol. 1991;283:1-11.
- Negishi T, Rai H, Hayatsu H. Antigenotoxic activity of natural chlorophylls. Mutat Res. 1997 May 12;376(1-2):97-100.
- Weng JR, Tsai CH, Kulp SK, and Chen CS. Indole-3-carbinol as a chemopreventive and anti-cancer agent. Cancer Lett. 2008. Apr 18;262(2):153-63.
- Ong TM, Whong WZ, Stewart J, Brockman HE. Chlorophyllin: a potent antimutagen against environmental and dietary complex mixtures. Mutat Res. 1986 Feb;173(2):111-5.
- Hernaez J, Xu M, Dashwood R. Effects of tea and chlorophyllin on the mutagenicity of N-hydroxy-IQ: studies of enzyme inhibition, molecular complex formation, and degradation/scavenging of the active metabolites. Environ Mol Mutagen. 1997 30(4):468-74.
- Dashwood R, Yamane S, Larsen R. Study of the forces of stabilizing complexes between chlorophylls and heterocyclic amine mutagens. Environ Mol Mutagen. 1996 27(3):211-8.
- Perez-Chacon G, de Los Rios C, Zapata JM. Indole-3-carbinol induces cMYC and IAP-family downmodulation and promotes apoptosis of Epstein-Barr virus (EBV)-positive but not of EBV-negative Burkitt’s lymphoma cell lines. Pharmacol Res. 2014 Nov;89:46-56.
- Grubbs CJ, Steele VE, Casebolt T, et al. Chemoprevention of chemically-induced mammary carcinogenesis by indole-3-carbinol. Anticancer Res. 1995 May- Jun;15(3):709-16.
- He YH, Friesen MD, Ruch RJ, Schut HA. Indole-3-carbinol as a chemopreventive agent in 2-amino-1-methyl-6-phenylimidazo[4,5-b]pyridine (PhIP) carcinogenesis: inhibition of PhIP-DNA adduct formation, acceleration of PhIP metabolism, and induction of cytochrome P450 in female F344 rats. Food Chem Toxicol. 2000 Jan;38(1):15-23.
- Goeger DE, Shelton DW, Hendricks JD, Bailey GS. Mechanisms of anti-carcinogenesis by indole-3-carbinol: effect on the distribution and metabolism of aflatoxin B1 in rainbow trout. Carcinogenesis. 1986 Dec;7(12):2025-31.
- Hipkiss AR. Carnosine, a protective, anti-ageing peptide? Int J Biochem Cell Biol. 1998 Aug;30(8):863-8.
- Preston JE, Hipkiss AR, Himsworth DT, Romero IA, Abbott JN. Toxic effects of beta-amyloid(25-35) on immortalised rat brain endothelial cell: protection by carnosine, homocarnosine and beta-alanine. Neurosci Lett. 1998 Feb 13;242(2):105-8.
- Hipkiss AR, Chana H. Carnosine protects proteins against methylglyoxal-mediated modifications. Biochem Biophys Res Commun. 1998 Jul 9;248(1):28-32.
- Hipkiss AR, Worthington VC, Himsworth DT, Herwig W. Protective effects of carnosine against protein modification mediated by malondialdehyde and hypochlorite. Biochim Biophys Acta. 1998 Mar 12;1380(1):46-54.
- Park YJ, Volpe SL, Decker EA. Quantitation of carnosine in humans plasma after dietary consumption of beef. J Agric Food Chem. 2005 Jun 15;53(12):4736-9.
- Peppa M, Uribarri J, and Vlassard H. Glucose, advanced glycation end products, and diabetes complications: what is new and what works. Clin Diabetes 2003. Oct;21(4):186-7.
- Babizhayev MA, Guiotto A, Kasus-Jacobi A. N-Acetylcarnosine and histidyl-hydrazide are potent agents for multitargeted ophthalmic therapy of senile cataracts and diabetic ocular complications. J Drug Target. 2009 Jan;17(1):36-63.
- Brown BE, Kim CH, Torpy FR, et al. Supplementation with carnosine decreases plasma triglycerides and modulates atherosclerotic plaque composition in diabetic apo E(-/-) mice. Atherosclerosis. 2014 Feb;232(2):403-9.
- Basta G, Schmidt AM, and De Caterina R. Advanced glycation end products and vascular inflammation: implications for accelerated atherosclerosis in diabetes. Cardiovasc Res 2004. Sep 1;63(4):582-92.
- Rashid I, van Reyk DM, Davies MJ. Carnosine and its constituents inhibit glycation of low-density lipoproteins that promotes foam cell formation in vitro. FEBS Lett. 2007 Mar 6;581(5):1067-70.
- Stirban A, Negrean M, Stratmann B, et al. Benfotiamine prevents macro- and microvascular endothelial dysfunction and oxidative stress following a meal rich in advanced glycation end products in individuals with type 2 diabetes. Diabetes Care. 2006 Sep;29(9):2064-71.
- Haupt E, Ledermann H, Köpcke W. Benfotiamine in the treatment of diabetic polyneuropathy–a three-week randomized, controlled pilot study (BEDIP study). Int J Clin Pharmacol Ther. 2005 Feb;43(2):71-7.
- Babaei-Jadidi R, Karachalias N, Ahmed N, Battah S, Thornalley PJ. Prevention of incipient diabetic nephropathy by high-dose thiamine and benfotiamine. Diabetes. 2003 Aug;52(8):2110-20.
- Nakamura S, Li H, Adijiang A, Pischetsrieder M, Niwa T. Pyridoxal phosphate prevents progression of diabetic nephropathy. Nephrol Dial Transplant. 2007 Aug;22(8):2165-74.
- Nakamura S, Niwa T. Pyridoxal phosphate and hepatocyte growth factor prevent dialysate-induced peritoneal damage. J Am Soc Nephrol. 2005 Jan;16(1):144-50.
- Sugimura T, Wakabayashi K, Nakagama H, Nagao M. Heterocyclic amines: Mutagens/carcinogens produced during cooking of meat and fish. Cancer Sci. 2004 95(4):290-9.
Advanced Glycation End Product Content Of Common Foods and Drinks
Epidemiological studies associate consumption of unhealthy foods with structural changes to the proteins in our bodies.
When one ingests foods/drinks processed or cooked at high temperature, the advanced glycation end products (AGEs) in these foods/drinks inflict glycation changes to the body’s own proteins.
The result is an accumulation of non-functional (AGEs) structures throughout the body that are associated with normal aging.
The following pages reveal the number of advanced glycation end products (AGEs) per serving of over 500 different foods and drinks.
A correlation can be seen by the heating process involved in processing or cooking the food and the number of AGEs they contain.
Bacon, for instance, has the highest levels of AGEs per serving at 11,905 compared to only 407 in tuna canned in water.
A consistent finding in this listing of 549 dietary items is that food cooked at higher temperatures has far more AGEs than the same food served raw or prepared at lower temperature. Some foods, however, have naturally higher levels of AGEs.
What may surprise you are foods that are considered healthy, but may have modest to relatively high AGE levels per serving.
The take home lesson from the following pages is that it is impossible to completely avoid consuming AGEs in your diet. AGEs also form in your body as a result of normal metabolism.
To achieve maximum reduction of AGEs, you should minimize intake of high glycemic sugars/starches, consume foods in the lower AGEs range (as revealed on the following chart), along with appropriate nutrients.
The advanced glycation end product (AGE) content of the following foods is based on their carboxymethyllysine content:*
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*Source: J Am Diet Assoc. 2010 Jun; 110(6): 911–16.e12.
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