January 2010 Blog with Durk and Sandy

Even as a youngster, though, I could not bring myself to believe that if knowledge presented danger, the solution was ignorance. To me, it always seemed that the solution had to be wisdom. You did not refuse to look at danger, rather you learned how to handle it safely … Any technological advance can be dangerous. Fire was dangerous from the start, and so (even more so) was speech—and both are still dangerous to this day—but human beings would not be human without them.— Isaac Asimov (from the foreword to the 1991 Bantam edition of The Naked Sun)

A liberal is a man too broadminded to take his own side in a quarrel.— Robert Frost

An idealist is one who, on noticing that a rose smells better than a cabbage, concludes that it will also make better soup.— H. L. Mencken


The question of how food processing (including cooking) affects important ingredients such as flavonoids, is a subject of many papers. For example, do you get the healthful cocoa flavanols when you eat chocolate cake?

A new paper1 reveals a very interesting finding: a baked chocolate cake with a batter that included baking soda resulted in an increased pH (above 8.3) and was found to contain no detectable monomeric flavanols after baking. However, substituting baking powder for the baking soda resulted in a chocolate cake with a pH of 6.2 with essentially complete retention of antioxidant activity and flavanol content, though with reduced cake heights and lighter cake color.

RECIPE: Here is a recipe (from an advertisement for Ghirardelli’s chocolate) for the best chocolate chip cookies we have ever eaten (so good we eat them with our eyes closed!); note that it contains baking powder. This is very easy to make though a bit messy. (At our house, Sandy makes the cookies and Durk cleans up the mess. That was Durk’s way of maximizing Sandy’s incentive to bake scrumptious chocolate chip cookies.)

We get about 25 cookies per batch.

For a batch, you’ll need:

11.5 oz of bittersweet chocolate chips (since we are chocolate extremists, we use the “Extreme Bittersweet Chocolate Chips” that contain 75% chocolate liquor and are low in sugar, available from King Arthur Flour (The Baker’s Catalogue), 800-827-6836, www.kingarthurflour.com)6 Tbsp (3/4 stick) unsalted butter (we have yet to find a satisfactory substitute for butter in this recipe)3 eggs1 cup Durk & Sandy’s Glycemic Control Erythritol™ (substituted for sugar in the original recipe)1/3 cup Durk & Sandy’s Glycemic Control Barley Flour™1/2 tsp baking powder12 oz semi-sweet chocolate chips (we used the 60% chocolate liquor chocolate chips offered by Ghiardelli the first time and sugar-free semi-sweet chocolate chips the second time; both worked well)1 cup chopped walnuts

Preheat oven to 375°F.

Melt extreme bittersweet chocolate chips and butter in a double boiler (or you can do it in the microwave at reduced power). In a large bowl with electric mixer, beat eggs and erythritol until slightly thickened and well blended. Stir in the chocolate and butter mixture. In a small bowl, stir together the barley flour and baking powder and then stir into the chocolate mixture. Gently mix the semi-sweet chocolate chips and the walnuts into the batter.

The original recipe calls for the resulting mixture to be formed into two logs, each 2 inches in diameter and about 8 inches long, on plastic wrap. The logs are then supposed to be wrapped tightly in the plastic wrap and refrigerated for at least an hour to firm. However, rather than do all that, Sandy just makes patties of the semi-firm batter with her hands (messy, messy and remember you shouldn’t lick off what remains stuck to your hands because it contains uncooked eggs). Each cookie patty (or slice cut from the refrigerated log, if you prefer) should be 2 inches in diameter by 3/4 inch thick. Place cookies on 2 greased (we use Durk & Sandy’s High Oleic Sunflower Oil™) cookie sheets, spaced at least 1 inch apart. Bake 12 to 14 minutes until shiny crust forms on top but interior is still soft. Cool on baking sheet.

Refrigerate any leftovers. Hint: Don’t invite anyone over or you won’t have any cookies left.

  1. Stahl et al. Preservation of cocoa antioxidant activity, total polyphenols, flavan-3-ols, and procyanidin content in foods prepared with cocoa powder. J Food Sci74(6):C456-61 (2009).


Cocoa consumption has been associated with improvement in lipid profile, insulin sensitivity, blood pressure, and platelet activity and function.1 In a new study,1researchers examined the effects of cocoa consumption (40 grams of cocoa with 500 mL skim milk per day or the same amount of skim milk without cocoa on various measures of inflammation in 47 high-risk subjects who had diabetes or had 3 or more of the following cardiovascular disease risk factors: tobacco smoking, hypertension, plasma LDL cholesterol ≥ 160 mg/dL, plasma HDL cholesterol ≤ 35 mg/dL, obesity [body mass index (measured as kg/m2) ≥ 30] and/or family history of premature coronary heart disease. Atherosclerosis is now widely considered to be a low-grade inflammatory disease.

One interesting result was a significantly increased level of HDL from baseline in those consuming cocoa and skim milk compared to those consuming skim milk alone. Adhesion molecules CD40, CD36, and VLA-4 found on the surface of monocytes were significantly decreased in the cocoa consuming subjects. Moreover, the soluble adhesion molecules P-selectin and ICAM-1 were significantly decreased in those consuming cocoa. As noted by the authors, the changes in the values for these inflammatory markers was modest as compared to other polyphenol-rich foods, such as wine. “Nonetheless, albeit modest, changes induced by cocoa intake may also contribute to a reduction in cardiovascular disease risk factors in subjects prone to cardiovascular disease.”1

And, besides, cocoa products (chocolate) taste so good!

  1. Monagas et al. Effect of cocoa powder on the modulation of inflammatory biomarkers in patients at high risk of cardiovascular disease. Am J Clin Nutr 90:1144-50 (2009).


A new paper1 reports, among other things, that 80 year old cocoa powder and 116 year old cocoa beans retained high levels of antioxidant activity and flavan-3-ol content. The 80 year old cocoa powder had been in the continuous possession of The Hershey Company stored under office conditions, while the 116 year old cocoa beans were originally displayed at the 1893 Chicago Exposition. Table 1 in the paper showed that the total polyphenol content in the 80 year old cocoa powder was 55.5 mg/g with 1.78 mg/g of flavan-3-ol monomers as compared to a 2008 sample of cocoa powder that contained 58 ± 1 mg/g polyphenols with 2.66 mg/g flavan-3-ol monomers. The 1893 cocoa beans contained 61.7 mg/g total polyphenols and 1.95 mg/g flavan-3-ol monomers.

  1. Hurst et al. Stability of cocoa antioxidants and flavan-3-ols over time. J Agric Food Chem 57:9547-50 (2009).


Adipose (fat) tissue is now known to be much more than a store of fats. Adipose cells release a large variety of active factors called adipocytokines, among which adiponectin is the only one which has been shown to have anti-atherogenic and antiinflammatory properties1,11 and is a potential regulator of lifespan in humans.9 The good news is that increased consumption of n-3 polyunsaturated fatty acids (eicosapentaenoic acid and docosahexaenoic acid, which are found in fatty fish oils) have been shown to significantly increase adiponectin plasma levels in obese humans,1 obese mice,1 and healthy humans.2 In another study of healthy humans,3 a higher ratio of n-3 fatty acids/saturated fats was associated with higher circulating adiponectin levels.

A further paper10 on dietary factors and plasma adiponectin concentrations in men revealed that “[m]oderate alcohol intake is associated with higher adiponectin concentrations, whereas a carbohydrate-rich diet with a high glycemic load is associated with lower adiponectin concentrations in men with no history of cardiovascular disease.”

In another study,13 22 cardiovascular disease patients (12 had had a previous heart attack, while the other ten had stable angina pectoris) drank either Oolong tea or water as the only allowed beverage for a month in a cross-over design. Oolong tea (but not water) consumption resulted in a significant increase in adiponectin levels as compared to baseline.

Health Benefits of Increased Adiponectin

Adiponectin levels are known to be decreased in obese humans.1 High plasma levels of adiponectin have been reported to be associated with reduced risk of heart attack in men,4 to reduce inflammation in adipose tissue,5 and to ameliorate obesity-related hypertension in obese mice treated with adiponectin.6 Decreased plasma concentration of adiponectin levels were reported in hypertensive men with coronary artery disease as compared to normotensive healthy subjects.7 Moreover, low levels of adiponectin were closely associated with endothelial dysfunction in a study of 76 Japanese subjects without a history of cardiovascular disease.8 As macrophages are involved in an important part of the atherosclerosis process (by forming foam cells), the fact that adiponectin has been shown to decrease the release of pro-inflammatory factors by macrophages11 could be, at least in part, one reason that adiponectin is protective against atherosclerosis.

Suppression of Fat Accumulation on a High Fat/High Sucrose Diet

One interesting recent paper12 reports that overexpression of human adiponectin in transgenic mice resulted in suppressed fat accumulation and prevention of premature death from a high-calorie diet. The researchers created a transgenic mouse expressing human full-length adiponectin in the liver to investigate the effects of adiponectin when transgenic and wild-type animals were fed either a normal lab chow diet or a high calorie diet. The mice that had overexpressed human adiponectin, when maintained on a high fat/high sucrose diet had significantly decreased weight gain with less fat accumulation and smaller adipocytes (which have greater insulin sensitivity than large adipocytes) in both visceral and subcutaneous body fat as compared to the wild-type mice on the same diet. Macrophage infiltration into adipose tissue (the source of proinflammatory cytokines) was markedly suppressed by overexpression of adiponectin. Moreover, the mice with overexpressed human adiponectin had an approximately twofold increase in lifespan on the high fat/high sucrose diet as compared to the wild-type mice on the same diet (most wild-type mice fed that diet died at about 1 year of age). The transgenic mice even had a longer lifespan on the conventional low-fat lab chow as compared to the wild-type mice on the same diet.

Possible Effects on Human Lifespan

As mentioned above, adiponectin is a potential regulator of lifespan in humans.9 In the lifespan study,9 researchers studied adiponectin levels in centenarians, their offspring, and unrelated participants. Adiponectin levels were significantly higher in those over 95 as well as in their offspring, suggesting the involvement of genetic factors. The authors report: “Over-representation of two common variants in Adiponectin genes (ADIPOQ) in male long-lived individuals combined with their independent association with elevated plasma adiponectin levels (in men and women) suggests that their presence may promote increased lifespan through the regulation of adiponectin production and/or secretion.”

Do-It-Yourself Adiponectin Therapy: Increased Adiponectin with n-3 Fatty Acids

In the study of the effects of n-3 fatty acid supplementation on adiponectin levels in obese humans,1 for example, the subjects had a significantly increased level of plasma adiponectin concentrations after a 3 month treatment with eicosapentaenoic acid (EPA) (1.8 g per day). In the study of the effects of the ratio of n-6 polyunsaturated fatty acids/n-3 fatty acids on adiponectin levels in healthy humans,2 a ten week intervention resulted in increased adiponectin, reduced LDL, increased burning of fats (lipid oxidation), and reduced plasma levels of TNF-alpha, an inflammatory cytokine. The subjects, who in their usual diets ate less than one fish meal per week, were put on a 10 week dietary intervention that included three fish meals a week and enough canola oil (20 ml a day) to supply 1.7 grams a day of alpha linolenic acid, a shorter chain n-3 fatty acid.

Our Omega-3 HeartFelt™ supplies 1.44 g of EPA and 960 mg of DHA at the highest recommended dose of 8 capsules a day. Both of us take that much. Sandy’s latest lab test for adiponectin was reported as 45, which is very high.

Oolong tea is a component of our ShapeShifter Teas.™


  1. Itoh et al. Increased adiponectin secretion by highly purified eicosapentaenoic acid in rodent models of obesity and human obese subjects. Arterioscler Thromb Vasc Biol 27:1918-25 (2007).
  2. Guebre-Egziabher et al. Nutritional intervention to reduce the n-6/n-3 fatty acid ratio increases adiponectin concentration and fatty acid oxidation in healthy humans. Eur J Clin Nutr 62:1287-93 (2008).
  3. Fernandez-Real et al. Circulating adiponectin and plasma fatty acid profile. Clin Chem 51(3):603-9 (2005).
  4. Pischon et al. Plasma adiponectin levels and risk of myocardial infarction in men.JAMA 291(14):1730-7 (2004).
  5. Ajuwon and Spurlock. Adiponectin inhibits LPS-stimulated NF-kappaB and IL-6 production and increases PPARgamma2 expression in adipocytes. Am J Physiol Regul Integr Comp Physiol 288:R1220-25 (2005).
  6. Ohashi et al. Adiponectin replenishment ameliorates obesity-related hypertension. Hypertension 47:1108-16 (2006).
  7. Dzielinska et al. Decreased plasma concentration of a novel anti-inflammatory protein—adiponectin—in hypertensive men with coronary artery disease. Thromb Res 110:365-9 (2003).
  8. Shimabukuro et al. Hypoadiponectinemia is closely linked to endothelial dysfunction in man. J Clin Endocrinol Metab 88(7):3236-40 (2003).
  9. Atzmon et al. Adiponectin levels and genotype: a potential regulator of life span in humans. J Gerontol A Biol Sci Med Sci 63A(5):447-53 (2008).
  10. Pischon et al. Association between dietary factors and plasma adiponectin concentrations in men. Am J Clin Nutr 81:780-6 (2005).
  11. Folco et al. Adiponectin inhibits pro-inflammatory signaling in human macrophages independent of interleukin-10. J Biol Chem 284(38):25569-75 (2009).
  12. Otabe et al. Overexpression of human adiponectin in transgenic mice results in suppression of fat accumulation and prevention of premature death by high-calorie diet. Am J Physiol Endocrinol Metab 293:E210-8 (2007).
  13. Shimada et al. Oolong tea increases plasma adiponectin levels and low-density lipoprotein particle size in patients with coronary artery disease. Diabetes Res Clin Pract 65:227-34 (2004).


More research continues to be published on antiviral effects of tea catechins. In a new paper,1 researchers report that green tea catechins inhibit Influenza A viral endonuclease, an enzyme that is essential for the influenza virus to propagate.1 Tested catechins with a galloyl group (EGCG, epigallocatechin gallate, and ECG, epicatechin gallate) had inhibitory activity, while catechins such as EGC, EC (without galloyl group), and GA (galloyl group only) showed weaker or no inhibition activity compared to the catechins with a galloyl group. The researchers also found that the galloyl group of EGCG attaches to an active pocket of the endonuclease domain of influenza A virus RNA dependent RNA polymerase.

As explained in this paper, much is being learned about how the particular locations of galloyl groups and of hydroxyl groups in tea catechins allow these natural molecules to intervene with specificity in many different aspects of body biochemistry. This understanding is part of a new field called combinatorial chemistry, leading to new, less toxic medical treatments. Now all we need is a new, less toxic FDA to get out of the way.

We include 1.33 grams of green tea extract in the maximum suggested daily dose of our V-Shield.™ Of this, 90% are polyphenols, with EGCG representing 50% of the polyphenols.

  1. Kuzuhara et al. Green tea catechins inhibit the endonuclease activity of influenza A virus RNA polymerase. PLoS Currents Influenza 2009 Oct. 13:RRN1052.


A new paper1 reports finding that the data developed in their experiments “strongly implicate reduced L-arginine availability as a key factor in the pathogenesis of I-R [ischemia/reperfusion] injury.” I-R occurs when oxygen supply is reduced (hypoxia) and then restored (reperfusion), such as occurs in heart attacks, strokes, or in obstructive sleep apnea. Although restoration of blood flow protects against further injury resulting from reduced oxygen supply, additional injury occurs that is believed to be due to the production of reactive oxygen species (ROS) during reperfusion. The ROS during the early stages of myocardial reperfusion is thought to be involved in the arrythmias, ventricular fibrillation, tachycardia, premature beating, and contractile dysfunction that can occur at that time.1

In this very interesting paper, the authors tested the hypothesis that “the I-R process induces a state of insufficient L-arginine availability for NO [nitric oxide] biosynthesis, and that this is pivotal in the development of myocardial I-R damage.”1

It is known that insufficient amounts of arginine (the precursor to nitric oxide) can cause the enzyme eNOS (endothelial nitric oxide synthase) to become “decoupled” from the production of NO, and to generate superoxide radicals instead. This means not only that less nitric oxide is produced, but that excess superoxide radicals are produced and the latter chemically interact with the available nitric oxide to form the potent oxidant peroxynitrite. The authors1 cite two earlier studies in animal models in which researchers found improved post-ischemic myocardial function and smaller infarct sizes (fewer heart cells died) following the infusion of L-arginine during reperfusion. Their purpose in doing this new research was to investigate mechanisms to explain the L-arginine cardioprotection as well as the role of CAT1 (the L-arginine transporter) in I-R injury. The studies were done on Sprague-Dawley rat neonatal ventricular cardiomyocytes (NVCM heart muscle cells) and in isolated mouse hearts.

Several experiments were performed. In one, NVCMs that were infected with adenovirus expressing the CAT1 L-arginine transporter (and, thus, overexpressing the CAT1 gene) and NVCMs supplemented with 1 mmol/L L-arginine during hypoxia-reoxygenation had significantly reduced ROS generation, significantly improved mitochondrial membrane potentials and significantly increased NO production (all p<0.001), while L-arginine deprived NVCMs had significantly worsened responses to hypoxia-reoxygenation. In the isolated mouse hearts, the authors found that “infusion of 1 mmol/L L-arginine in hearts during reperfusion significantly improved recovery when compared to that of untreated hearts” for measures that indicated improved ventricular relaxation and reduced diastolic stiffness. Protein oxidation by peroxynitrite in the mouse hearts (as measured by nitrotyrosine) was significantly lower (P<0.001) in L-arginine infused hearts as compared to untreated controls. The researchers found that there was reduced L-arginine transport during both hypoxia and in reoxygenation.

One of the possible mechanisms to explain these beneficial effects of L-arginine infusion was the observation that the extent of phosphorylation (activation) of Akt was increased significantly in L-arginine infused hearts after I-R. Akt has important anti-apoptotic (prevents a form of programmed cell death) properties and has been found when overexpressed to prolong survival, prevent cardiac remodeling (pathogenic changes) and improved contractile performance in infarcted hearts.1 Moreover, other studies have reported increased Akt signalling as a result of ischemic preconditioning (in which exposure to a small ischemic stress can protect against a larger ischemic stress later during a specific period of time).

The authors conclude that “[r]estoration of L-arginine availability may therefore be a valuable strategy to ameliorate I-R injury.”

Obstructive Sleep Apnea

As we mentioned above, obstructive sleep apnea is a significant cause of ischemia-reperfusion injury because of repeated episodes of discontinued breathing following by restoration of breathing during sleep. At present, there are no really satisfactory treatments except for uncomfortable masks that deliver compressed air to the sufferer’s airways during sleep. The use of arginine supplements could be a way to help reduce or prevent I-R damage that would otherwise occur during sleep apnea. We hope to see published research on this, but human studies are expensive to do and are governed by many rules and regulations. We do not know if there are good animal models for obstructive sleep apnea.

Citrulline May Increase Arginine Supply Even Better Than Arginine3

As we have reported before, studies have shown that the amino acid citrulline is part of a salvaging cycle in which arginine is used by nitric oxide synthase to make NO, with citrulline as a byproduct. Citrulline is then recycled to arginine.2 It is for this reason that we include small catalytic amounts of citrulline in our InnerPower Plus™ arginine supplement.

  1. Venardos et al. Reduced L-arginine transport contributes to the pathogenesis of myocardial ischemia-reperfusion injury. J Cell Biochem 108:156-168 (2009).
  2. Hecker et al. The metabolism of L-arginine and its significance for the biosynthesis of endothelium-derived relaxing factor: cultured endothelial cells recycle L-citrulline to L-arginine. Proc Natl Acad Sci USA 87:8612-6 (1990).
  3. Kuhn et al. Oral citrulline effectively elevates plasma arginine levels for 24 hours in normal volunteers. Circulation 206(Suppl II):11-339 (2002).


Another important health protecting molecule that is being intensively investigated is paraoxonase 1 (PON 1), an enzyme associated with high-density lipoprotein (HDL) that is mainly secreted by the liver.1 The many health effects of PON 1 include:1 importantly, prevention of the oxidation of HDLs (which can destroy HDL’s protective properties such as its anti-oxidative and anti-inflammatory effects);* prevention of the oxidation of LDL (which promotes atherosclerosis); and hydrolysis of platelet-activating factor, which is involved in vascular disease and other inflammatory conditions. As the authors1suggest: “Therefore, pharmacological modulation of PON-1 activity or PON-1 gene expression could constitute a useful approach for the prevention of CVD [cardiovascular disease] and OP [organophosphate poisons] intoxication.” OPs are found in some insecticides (parathion, chlorpyrifos) and also some chemical warfare agents. PON-1 can hydrolyze (and, thus, detoxify) OPs.1


* For example “HDL fractions isolated from PON 1(-/-) [PON 1 knockout] mice were unable to prevent LDL oxidation in cultured arterial tissue, in contrast to the HDL obtained from control mice.”2


Low activity of PON 1 has been reported in disease conditions that include renal (kidney) disease, diabetes, HDL deficiencies, and liver cirrhosis.1 High fat diets have been reported to decrease PON 1 activity, while moderate alcohol consumption increased it.1 PON 1 is significantly decreased (and remained lower than baseline for up to 8 hours) in humans after a meal rich in used cooking fat (such as fat used to deep-fry foods prepared at fast food restaurants).3 The latter study was conducted with 12 healthy male subjects aged 22 to 63 who were randomized to receive a milkshake containing either fat that had been used for deep-frying (yuck!) or the same type of fat that had not been previously used. PON 1 has been shown to be protective in oxidative stress (including cardiovascular disease), Alzheimer’s disease, metabolic syndrome, and liver diseases.2

Dietary Factors That Increase PON 1

PON 1 is increased following consumption of polyphenol-rich diets.1 Wine consumption and some polyphenols present in wine or fruit juice were reported to increase PON 1 in humans and mice.1 In one study,1 naringenin, flavone, and quercetin increased PON 1 mRNA about twofold in cell culture, but catechin was a poor inducer. In another paper,2oleic acid (usually consumed in the form of olive oil, but high oleic sunflower oil contains considerably more oleic acid) was reported effective in an in vitro study in protecting PON 1 activity from oxidative stress. Moderate alcohol (40 g/day in men and 30 g/day in women) had a modest effect, increasing serum HDL cholesterol by 6.5% and PON 1 by 3.7%.4 A daily consumption of pomegranate juice for 1 year by patients with carotid artery blockage induced an increase in serum PON 1 activity and also decreased the amount of oxidized LDL and progression of atherosclerosis (measured by the degree of carotid intima-media thickness).5 Resveratrol has also been reported to induce PON 1 gene expression in a human hepatocyte (liver) primary culture and in the HuH7 hepatoma cell line6 and in other human cell lines,7 as well as in apolipoprotein E-deficient mice (a commonly used animal model of atherosclerosis).8

As we have long noted, advances in understanding of the physiological effects of foods and food components has resulted in the development of a virtual parallel medical system (parallel that is to the FDA’s xenobiotic drugs-only system enforced by FDA censorship of truthful information on the labels and advertising of dietary supplements and foods). Keep yourself informed! Also, you can follow our latest involvement in suing the FDA over its egregious suppression of the First Amendment guarantee of free speech (“Congress shall make NO law . . . abridging the freedom of speech”) (emphasis added) at www.emord.com.* We have been very lucky in getting good judges in our earlier cases against the FDA (especially, the landmark decision in Pearson v. Shalala, U.S. Circuit Court of the D.C. Circuit, 1999) and can only hope that it happens again, especially at the Court of Appeals level.


* Also, see “A Bitter Pill: 15 year battle over vitamin health claims is back in court” by Jenna Greene, pp. 21, 24, 26 The National Law Journal 28 Sept. 2009.



  1. Gouedard et al. Dietary polyphenols increase paraoxonase 1 gene expression by an aryl hydrocarbon receptor-dependent mechanism. Mol Cell Biol 24(12):5209-22 (2004).
  2. Camps et al. Pharmacological and lifestyle factors modulating serum paraoxonase-1 activity. Mini Rev Med Chem 9:911-20 (2009). [This paper also reported increased PON 1 in some human clinical studies of statins and fibrates, as well as a study of orlistat (a gastrointestinal lipase inhibitor) in obese humans.]
  3. Sutherland et al. Reduced postprandial serum paraoxonase activity after a meal rich in used cooking fat. Arterioscler Thromb Vasc Biol 19:1340-7 (1999).
  4. Sierksma et al. Kinetics of HDL cholesterol and paraoxonase activity in moderate alcohol consumers. Alcohol Clin Exp Res 26:1430-5 (2002).
  5. Aviram et al. Pomegranate juice consumption for 3 years by patients with carotid stenosis reduces common carotid intima-media thickness, blood pressure and LDL oxidation. Clin Nutr 23:423-33 (2004).
  6. Gouedard et al. Induction of the paraoxonase-1 gene expression by resveratrol. Arterioscler Thromb Vasc Biol 24:2378-83 (2004).
  7. Curtin et al. Resveratrol induces catalytic bioscavenger paraoxonase 1 expression and protects against chemical warfare nerve agent toxicity in human cell lines. J Cell Biochem 103:1524-35 (2008).
  8. Do et al. Long-term effects of resveratrol supplementation on suppression of atherogenic lesion formation and cholesterol synthesis in apo E-deficient mice. Biochem Biophys Res Commun 374:55-9 (2008).

He that hath eyes to see and ears to hear may convince himself that no mortal can keep a secret. If his lips are silent, he chatters with his fingertips, betrayal oozes out of him at every pore.— Sigmund Freud, 1905


The economics paper of the above title was published in the 23 October 2009 Science. The authors proposed that if only the government had complete information by knowing what everybody’s actual evaluation of their benefit from public goods was, then the government would be able to calculate the socially optimal level of the public good to produce and then tax group members in proportion to the benefits that they receive in order to finance the cost of the good. In this way, the group’s net benefit would be maximized and every individual’s benefit would be greater than the cost he or she has to pay. An economic game, where subjects made decisions regarding their valuation of various abstract public goods while being evaluated by fMRI, made it possible to detect truthful from nontruthful reporting of how much participants “really” valued the public goods.

There are a number of problems with this approach, including the following:

  1. People might not want to allow the government to scan their brains to determine their “true” valuation of public goods.
  2. Even for people who did agree to undergo testing to reveal their “true” valuations, the test would reveal a mere snapshot of those evaluations. Anytime after taking the test, new data or new personal circumstances could change that “true” valuation to a different one. Hence, even if the government had complete information of everybody’s true value of a public good at moment 1, at moment 2 they would be in the dark again.
  3. You cannot trust the government when it tells you that a public good will cost a certain amount of money. In fact, in order for this test to be symmetrical, government officials should be required to take fMRI scans so that you can see if they are lying about the cost of public goods. But even that is not good enough since any particular government official, even if truthful, cannot know everything that affects costs or how costs will change even in the near-term. She/he might tell you everything they know about costs at moment 1, but what does that tell you about moment 2?
  4. There are a great many so-called public goods for which the two of us have a true negative value (i.e., to us they are public bads). A good example is the FDA, where we have spent hundreds of thousands of dollars of our own money to try to stop just their production of censorship, a purported public good. Hence, we would need to be paid hundreds of thousands of dollars if our benefits are to exceed the costs we incurred in the case of FDA censorship alone. Is the government going to send us a check?

In short, we don’t think this concept solves anything. We welcome other comments. Please send them to us c/o Life Enhancement Products.


The famous Sirt1 (sirtuin 1), a gene that plays a role in aging1 in several species including mice (in yeast and nematodes, it is Sirt2, of which Sirt1 is the mammalian ortholog, that is a longevity gene), has been shown to not only be a cancer suppressor,2but also to be importantly involved in DNA repair.2b Caloric restriction has been found to increase Sirt1 protein levels (but not necessarily in all tissues).3 In a new paper,1 Sirt1 has been found to be essential for the maintenance of T cell tolerance in mice. In the abstract for this paper, the authors suggest that “activators of Sirt1 may be useful as therapeutic agents for the treatment and/or prevention of autoimmune diseases.” As explained in the paper, resveratrol is a Sirt1 activator.4

Self reactive T cells are supposed to be eliminated by the thymus to prevent autoimmunity. Mice with a knockout of Sirt1 have “elevated immune responses and fail to maintain peripheral tolerance to autoantigens, as exemplified by the presence of anti-nuclear antibodies, systemic lymphocyte infiltration, and increased susceptibility to experimental autoimmune encephalomyelitis [a model of the autoimmune disease multiple sclerosis].” Sirt1 regulates a large number of proteins (such as the cancer suppressors p53 and FOXO3)2 as well as histones,1 which control access to DNA (and, thus, whether genes are turned on or off), by removing acetyl groups; Sirt1 is a type III histone deacetylase. Resveratrol, found in red wine, tea, and other foods, is a Sirt1 activator.4 The authors of this paper1 in fact, suggest that, though the mechanisms of action of resveratrol are still under debate (this paper was published in October 2009), resveratrol may provide “a potential avenue for treatment of autoimmune diseases as well as allograft rejections”1 since “its interference with immune function is well established.”1

“The fact that CD4+ T cells of Sirt1–/– [Sirt1 knockouts] mice were unable to be tolerized suggests that Sirt1 could function as an anergic factor in T cells.”1 The researchers found that anergic T cells expressed Sirt1 mRNA (messenger RNA) by 4- to 5-fold as compared to naive (non-activated) T cells but was increased only slightly in already activated T cells. The authors1 report that Sirt1 inhibits T cell activation by suppressing the acetylation of c-Jun, a regulatory molecule.


1. Zhang et al. The type III histone deacetylase Sirt1 is essential for maintenance of T cell tolerance in mice. J Clin Invest 119(10):3048-58 (2009).

2. Kabra et al. SirT1 is an inhibitor of proliferation and tumor formation in colon cancer. J Biol Chem 284(27):18210-17 (2009).

2b. Oberdoerffer et al. SIRT1 redistribution on chromatin promotes genomic stability but alters gene expression during aging. Cell 135:907-18 (2008).

3. Chen et al. Tissue-specific regulation of SIRT1 by calorie restriction. Genes Dev1;22(13):1753-7 (2008).

4. Borra et al. Mechanism of human SIRT1 activation by resveratrol. J Biol Chem280(17):17187-95 (2005).

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