December 2005 Blog with Durk and Sandy

The Constitution is not an instrument for the government to restrain the people, it is an instrument for the people to restrain the government—lest it come to dominate our lives and interests.— Patrick Henry

On every question of construction [of the Constitution, let us] carry ourselves back to the time when the Constitution was adopted, recollect the spirit manifested in the debates, and instead of trying what meaning may be squeezed out of the text, or invented against it, conform to the probable one which it was passed.— Thomas Jefferson, letter to William Johnson, June 12, 1823

Woe to the nation whose literature is cut short by the intrusion of force. This is not merely interference with freedom of the press but the sealing up of a nation’s heart, the excision of its memory.— Alexander Solzhenitsyn

Congress passed and the president signed 269 bills into law in 2002. But, as noted, regulatory agencies issued 4,167 rules. The unelected are doing the bulk of the lawmaking. . . . The way to control regulation is not to merely require agencies to perform cost/benefit analyses but to require Congress to vote on agencies’ final rules before they are binding on the public.— Clyde W. Crews, Jr., “Ten Thousand Commandments, an
Annual Snapshot of the Federal Regulatory State”
Cato Institute, 2003


Though there is no constitutional text describing a right to privacy as such, there is a clear constitutional limit (Fourth Amendment) to government access to an individual’s person, papers, and effects: “The right of the people to be secure in their persons, houses, papers, and effects against unreasonable searches and seizures, shall not be violated, and no Warrants shall issue, but upon probable cause, supported by Oath or affirmation, and particularly describing the place to be searched, and the persons or things to be seized.”

The inclusion of the Fourth Amendment in the Bill of Rights was, among other things, a result of the bad experience of the colonists with British “general warrants,” which were virtually unlimited licenses for government fishing expeditions.

As a result of the War on Drugs and the War on Terror, the courts have restricted the applicability of the Fourth Amendment requirement of a warrant for searches and seizures of private papers and effects to where little is now left of this protection. (The constitutional limits on searches and seizures are undoubtedly inconvenient for law enforcement and for administrative agencies.) For example, any business that is part of a “heavily regulated” industry has been deprived by past court rulings of any Fourth Amendment protection, permitting warrantless searches limited only by their being conducted during regular business hours. (Though there are often said to be “administrative search warrants” that agencies such as the FDA issue on their own behalf, these are not Fourth Amendment warrants.)

On August 25, 2005, we filed an amicus brief (along with Dr. Julian Whitaker’s Freedom of Health Foundation) in the case of U.S. v. Gonsalves (Case No. 04-2316) before the U.S. Court of Appeals for the First Circuit. The central issue of the case was that a warrantless search was made of a doctor’s office, and medical records were seized. We argued that this was a violation of the Fourth Amendment because doctors’ offices are not a “heavily regulated” industry and hence still have Fourth Amendment protection. We believe this is a strong argument, as medical records in doctors’ offices have been the focus of considerable legislative protection. (What we could not argue was that a warrantless search is an inherent violation of the clear meaning of the Fourth Amendment, as earlier courts have seen fit to rule otherwise.) As this is a case before a court of appeals, the decision may take some time.

People really have no idea how quickly the “privacy” of their medical information is slipping away. Without the requirement of a warrant signed by a judge and based upon probable cause, warrantless searches of doctors’ offices become at-will fishing expeditions that spell the end to any private medical information. Yet, who has heard of U.S. v. Gonsalves and knows that perhaps the final nail in the coffin of Fourth Amendment protection of doctors’ offices and records is now being quietly driven?


This recipe is fabulous for its heavenly taste and for its healthful components: blueberries, resistant starch, cinnamon, and ginger. It’s also easy to make.

We use a powdered resistant starch flour made from high-amylose cornstarch that contains 60% dietary fiber and only 1.6 kcal/g (carbohydrate and protein contain 4 kcal/g). Resistant starch has a number of beneficial effects in humans, including increased production of fecal short-chain fatty acids (such as butyrate1), which protect against colon cancer and improve insulin sensitivity.2 Resistant starch was also found to improve the plasma glucose and triglyceride responses to a meal in patients with type 2 diabetes.3 In another human study, the addition of resistant starch to white bread reduced the glycemic index (100 without resistant starch to 55 with resistant starch). In fact, 11 human clinical trials have been published testing resistant starch from high-amylose cornstarch (the type we use) and finding improvements in glycemic response.4

Blueberry Gingerbread

  • 3/8 cup vegetable oil (preferably extra virgin olive oil or high-oleic sunflower oil)
  • 1 1/2 cups whole-grain flour (we use rye)
  • 1 1/2 cups resistant starch
  • A little extra flour for dusting baking pan
  • 1 cup sorbitol (this sugar alcohol takes up water, helping to ensure a moist cake)

Or (if you prefer a drier cake):


  • 1/2 cup sorbitol plus 1/2 cup erythritol
  • 1/2 tsp salt
  • 4 tbsp molasses
  • 1 large egg
  • 2 tsp freshly grated ginger (or you can substitute ground ginger)
  • 2 tsp ground cinnamon
  • 1 tsp freshly ground nutmeg (or you can substitute dried ground nutmeg)
  • 1 1/2 tsp baking soda
  • 3–4 cups fresh blueberries (or you can use 2 or 3 15-oz cans of blueberries, draining juices before use)
  • 1 cup buttermilkPreheat oven to 350°F. Grease a 12″ x 7″ baking dish and dust with flour.

    Using an electric mixer (ideally, fitted with a whisk attachment), beat together the oil, sorbitol, salt, and molasses until blended. Add the egg and ginger, and beat to blend. In a separate bowl, sift together the flour, resistant starch, cinnamon, nutmeg, and baking soda. In a medium-sized bowl, combine 2 tablespoons of the sifted mixture with the blueberries, stirring gently to coat. Add one-third of the remaining flour mixture to the oil mixture, and blend together. Add half of the buttermilk, and continue to blend. Repeat with the flour and buttermilk, mixing all. Gently fold in the blueberries.

    Pour the batter into the greased and flour-dusted baking pan. Bake in the center of the oven for 35 to 40 minutes, until the center is firm and a toothpick inserted into the center comes out dry.

    Transfer the pan to a wire rack to cool. Serve slightly warm or at room temperature. If desired, you can heat leftover cooled pieces for a short time (20–30 seconds) in a microwave.

    This cake is a pure delight, and knowing that it is probably one of the healthiest cakes you could possibly make only adds to the pleasure of eating it! Sandy makes it often. (Adapted from the recipe on page 89 of Linda Dannenberg’s True Blueberry, Stewart, Tabori & Chang, New York, 2005.)


    1. Jenkins et al. Physiological effects of resistant starches on fecal bulk, short chain fatty acids, blood lipids and glycemic index. J Am Coll Nutr 17(6):609-16 (1998).
    2. Robertson et al. Insulin-sensitizing effects of dietary resistant starch and effects on skeletal muscle and adipose tissue metabolism. Am J Clin Nutr 82:559-67 (2005).
    3. Giacco et al. Metabolic effects of resistant starch in patients with type 2 diabetes. Diab Nutr Metab 11:330-5 (1998).
    4. See, e.g., Howe et al. Dietary starch composition and level of energy intake after nutrient oxidation in “carbohydrate-sensitive” men. J Nutr 126:2120-9 (1996).



One of the consequences of aging is that more and more cells end up in a senescent state in which they are still viable and metabolically active but are unable to divide. Senescence has recently been discovered to be induced by oncogene (cancer-inducing gene) activation, thus supporting the theory that one function of senescence is to prevent the development of cancer.1

Although the senescent cells are alive and metabolically active, they do not function the same as nonsenescent cells.2 For example, the capacity of endothelial cells (which line blood vessels) to generate nitric oxide decreases in senescence.3 The suppression of oxidative stress or application of NO donors has been shown to delay the onset of replicative senescence in cell culture.3

The authors determined that when human umbilical-vein endothelial cells in culture were incubated with aspirin (100 µM), the activity of beta-galactosidase (a biomarker of senescence) was significantly decreased. In contrast to aspirin, ibuprofen and acetaminophen resulted in significant increases in beta-galactosidase activity. Addition of a nitric oxide synthase inhibitor (L-NAME) to the culture abolished the aspirin-reduced beta-galactosidase activity, demonstrating that the aspirin effect is mediated by nitric oxide.

Shortening of telomeres and decrease of telomerase is another mechanism that induces senescence. Aspirin increased telomerase activity significantly, compared to control, while ibuprofen and acetaminophen significantly reduced telomerase activity. Again, addition of the nitric oxide synthase inhibitor L-NAME to the culture with aspirin significantly blocked the effect of aspirin on telomerase activity, showing that nitric oxide mediates the effect.

The authors speculated, “It is conceivable and supported by recent observations that aspirin stimulates NO formation through its unique ability to trigger the synthesis of 15-epi-lipoxin A4. Aspirin is known to acetylate COX-2 within the endothelium, thus triggering 15-epi-lipoxin A4, which, in turn, elicits NO synthesis from both eNOS [endothelial nitric oxide synthase] and iNOS [inducible nitric oxide synthase].”3

We would expect this effect to be increased by use of an arginine supplement, especially if it contained choline and vitamin B5, because the latter two nutrients can be used to make acetylcholine, which activates eNOS conversion of arginine to nitric oxide.


  1. See, e.g., Braig et al. Oncogene-induced senescence as an initial barrier in lymphoma development. Nature 436:660-5 (2005); and Campisi. Suppressing cancer: the importance of being senescent. Science 309:886-7 (2005).
  2. See, e.g., Kletsas et al. The proinflammatory phenotype of senescent cells. Ann NY Acad Sci 1019:330-2 (2004).
  3. Bode-Boger et al. Aspirin reduces endothelial cell senescence. Biochem Biophys Res Commun 334:1226-32 (2005).


Earlier, we reported in this newsletter on a paper1 showing that repeated mild heat shock delays aging in cultured human skin fibroblasts. A new paper2 reports that mild heat stress also protects rats from the very significant loss of muscle mass that occurs when the animals are immobilized.

Rats were divided into three groups: a control group, an immobilized group, and an immobilized group that was heat-treated. The heat treatment consisted of warming the animals to 41–41.5ºC (about 106ºF) for 30 minutes on alternating days. The findings showed that the immobilization induced a significant increase in oxidative damage in the animals’ immobilized muscles, but this damage was significantly reduced by heating. This is strong evidence that mild heat stress protects against muscle-disuse atrophy. Great news for people who don’t like to exercise!

The heat-treated animals with relatively preserved muscle mass had higher heat-shock protein 72 (HSP72) levels. It has been proposed that HSP72 is necessary for maintenance of protein synthesis in the heated hind limbs of animals with hind-limb unweighting (suspension). In addition, it has been proposed that HSP72 protects proteins from degradation by proteolysis by refolding damaged proteins. In another study cited in the paper, scientists reported that a single bout of heat for 60 minutes was sufficient to detect an increase in HSP72 8 days later, with muscle atrophy reduced in the heated-suspended group by about 32%. This suggests that daily heating may not be necessary, as the increased levels of HSP72 (at least in rats, and probably in humans) remain for several days.


In another paper,3 enhanced expression of HSP72 as a result of heating in male rats attenuated oxidative stress and neointimal thickening in induced inflammatory arterial lesions, suggesting that increasing HSP72 by mild heat stress can provide protection against atherosclerosis. In a different study,4 scientists report that heat-shock-induced manganese superoxide dismutase (the mitochondrial version of superoxide dismutase) enhanced the tolerance of cultured cardiac myocytes to hypoxia-reoxygenation (ischemia-reperfusion) injury.


A separate study5 of 50 subjects (25 of these served as controls) that was controlled but not randomized found that immunological changes (such as increases in immunoglobulins and leukocytes) induced in people who used sauna baths resulted in a statistically significant reduction in common colds, as compared to controls. The average frequency of sauna bathing was 26.8 ± 5.5 during 6 months. As influenza viruses generate large amounts of reactive oxygen species,6 both directly and through induction of immune cells, a treatment, such as mild heat stress, that decreases oxidative damage may be a useful prophylactic against influenza-damage severity.


  1. Rattan. Repeated mild heat shock delays ageing in cultured human skin fibroblasts. Biochem Molec Biol Int 45(4):753-9 (1998).
  2. Selsby, Dodd. Heat treatment reduces oxidative stress and protects muscle mass during immobilization. Am J Physiol Regul Integr Comp Physiol 289:R134-9 (2005).
  3. Okada et al. Thermal treatment attenuates neointimal thickening with enhanced expression of heat shock protein 72 and suppression of oxidative stress. Circulation 109:1763-8 (2004).
  4. Nobushige, Yamashita, et al. Heat shock-induced manganese superoxide dismutase enhances the tolerance of cardiac myocytes to hypoxia-reoxygenation injury. J Mol Cell Cardiol 29:1805-13 (1997).
  5. Ernst et al. Regular sauna bathing and the incidence of common colds. Ann Med22:225-7 (1990).
  6. Han et al. Effect of long-term dietary antioxidant supplementation on influenza virus infection. J Gerontol: Biol Sci 55A(10):B496-503 (2000)


An exciting new paper1 reports that in mice calorically restricted for 3 or 12 months, there was an increase in endothelial nitric oxide synthase (eNOS) expression and 3′,5′-cyclic guanosine monophosphate (cGMP, the second messenger for nitric oxide that signals downstream chemical pathways). The enhanced eNOS was accompanied by mitochondrial biogenesis (creation of new mitochondria), increased oxygen consumption and ATP production, and an enhanced expression of SIRT1 (a gene believed to regulate lifespan). In animals genetically engineered to lack eNOS (eNOS-/-), caloric restriction was unable to induce significant mitochondrial biogenesis in a number of tissues, including white adipose tissue. The CR-induced increase in oxidative metabolism and ATP production was blunted in eNOS-/- animals. SIRT1 was increased in calorically restricted eNOS-/- animals, but the increase (in white adipose tissue) was only 30% of that in calorically restricted animals with normal (wild type) eNOS gene expression.

Thus, upregulation of endothelial nitric oxide synthase may account for much of the effects of caloric restriction, at least in mice. Interestingly, in a cell-culture experiment done as part of the above study, the authors found: “SIRT1 mRNA [messenger RNA] and protein were ~threefold higher in cultured white adipocytes exposed either to NO donors . . . or to a cGMP analog . . . than in untreated cells and ~80% lower in WAT [white adipose tissue] of eNOS-/- mice when compared with wild-type animals. Thus expression of SIRT1 in WAT during CR might be partly mediated by NO acting via cGMP.”

These findings are very exciting, because it is possible through nutritional means (particularly supplementation with arginine) to increase nitric oxide. It would be interesting to see the results of lifespan studies in calorically restricted and ad libitum-fed mice given a diet enriched in arginine. Note that addition of choline and vitamin B5 to an arginine supplement provides more material for acetylcholine synthesis; acetylcholine activates eNOS to release NO derived from arginine.


  1. Nisoli et al. Calorie restriction promotes mitochondrial biogenesis by inducing the expression of eNOS. Science 310:314-7 (2005).


Like many other diseases of aging, atherosclerosis is an inflammatory disease.1 C-reactive protein, an inflammatory marker, is a commonly measured risk factor for cardiovascular disease. Some ways to reduce C-reactive protein levels include high-fiber diets2 and supplements of vitamin E, DHEA, and fish oil.

A new paper1 now reports that the likelihood of having a high level of CRP (>3.0 mg/L) was lower in individuals with a higher dietary arginine intake. “In the adjusted regression [after correcting for factors associated with CRP], subjects in the highest level (90th percentile) of arginine intake were 30% less likely to have a CRP above 3.0 mg/L than were subjects with a median arginine intake (odds ratio = 0.70, 95% confidence interval = 0.56 to 0.88).” The authors conclude that “Individuals may be able to lower their risk for cardiovascular disease by consuming more arginine-rich foods, such as nuts and fish.”

The study was an analysis of the Third National Health Nutrition and Examination Survey, a national public use dataset collected between 1988 and 1994, which included the 13,401 participants 25 years and older who were part of this study.

As the authors note, “recent research has shown that arginine administration has anti-inflammatory effects,” such as decreasing the formation of clotting factors, reducing blood viscosity, inhibiting oxidative stress, and reducing nonenzymatic glycosylation.3

The authors mention that the differences between the four dose levels of dietary arginine were not very large. They suggest that individuals can increase their daily consumption of arginine by 2.5 g a day by consuming 100 g (3.6 ounces) of walnuts. Unfortunately, nuts contain a lot of fat, which means a lot of calories. The 3.6 ounces of walnuts contain about 630 calories, with about 540 of those calories from fat.


  1. Ross. Atherosclerosis—an inflammatory disease. NEJM 340(2):115-26 (1999).
  2. Ajani et al. Dietary fiber and C-reactive protein: findings from National Health and Nutrition Examination Survey data. J Nutr 134:1181-5 (2004).
  3. Wells et al. Association between dietary arginine and C-reactive protein. Nutrition21:125-30 (2005).


Phosphatidylserine is a major constituent of cell membranes and is used as a dietary supplement for its potential neuroprotective effects.1 A new paper2 reports that, acting via the Akt signaling pathway, docosahexaenoic acid (DHA) increases phosphatidylserine concentrations in neuronal cell membranes, thereby acting as a protectant against apoptosis (programmed cell death).

The authors explain that DHA is highly enriched in neuronal membranes and promotes neuron survival by facilitating membrane translocation/activation of Akt via DHA’s ability to increase phosphatidylserine. They found that in vivo reduction of DHA by dietary depletion resulted in decreased hippocampal phosphatidylserine and increased neuronal susceptibility to apoptosis in culture. Moreover, the authors write, “. . . DHAenrichment partially prevented the reduction of Akt phosphorylation and activity caused by serum starvation, suggesting that DHA promoted cell survival by assisting in the maintenance of basal Akt activity under an adverse condition.”


  1. Nolan et al. Evidence of a protective effect of phosphatidylserine-containing liposomes on lipopolysaccharide-induced impairment of long-term potentiation in the rat hippocampus. J Neuroimmunol 151:12-23 (2004).
  2. Akbar et al. Docosahexaenoic acid: a positive modulator of Akt signaling in neuronal survival. Proc Natl Acad Sci USA 102(31):10858-63 (2005).


As important as research into the mechanisms of potential health benefits of flavonoids (such as the anthocyanin pigments found in fruits such as berries and grapes, vegetables, and wines) is research into their bioavailability. Anthocyanins, for example, are quickly detected in plasma after ingestion, but at very low levels.1 A new study1 was done to determine whether and to what extent anthocyanins are able to enter the brain. The study was done with male Wistar rats.

The authors used a solution of pure anthocyanins extracted from grapes, which was administered to rats intragastrically through a surgical procedure. Each rat was administered what corresponded to about 2.3 grams of grapes. The authors calculate that this amounts to about 597 grams of Cabernet Sauvignon grape (or 284 grams of Teroldego grape) for a person of 65 kg.

They detected the appearance of the anthocyanin malvidin-3-glucoside in the plasma of the anesthetized rats only 6 minutes after administration of the grape solution in the stomach. What the authors call the “real novelty” of their work was finding significant amounts of anthocyanins in the brain (removed immediately after 10 minutes of intragastric administration of the grape solution). They found the average amounts of malvidin-3-glucoside and its p-coumarate ester in the brain at similar or nearly 10-fold higher concentrations, respectively, than in the plasma. The authors cite evidence that anesthesia per se does not disrupt the blood-brain barrier.


  1. Passamonti et al. Fast access of some grape pigments to the brain. J Agric Food Chem 53:7029-34 (2005).


New information on regulatory pathways controlling inflammation in arthritis and atherosclerosis appears in a new paper.1

One source of inflammation to chondrocytes (cells in joints that produce cartilage) and endothelial cells (which line blood vessels) is fluid shear, the stress of fluids moving against adjacent cells. As the paper explains, high shear is protective to endothelial cells by inducing antioxidant and phase 2 detoxifying genes. In joints, however, high shear causes irreversible matrix erosion and chondrocyte apoptosis. In fact, high shear in joints causes an upregulation of COX-2 expression, hence the use of COX-2 inhibitors to treat arthritis inflammatory pain. “Phase 2 inducers and to a lesser extent specific inhibitors of COX-2 negate the shear-mediated repression of ARE [antioxidant response element] regulated enzyme activity and apoptosis.”

As the authors further explain, “. . . recent evidence that the shear-induced upregulation of phase 2 genes in human aortic endothelial cells is attenuated by COX-2 specific inhibitors may contribute to their cardiovascular side effects. Whereas COX-2 inhibitors reduce inflammation in cartilage, their presence in the vasculature prevents the accumulation of COX-2-derived 15d-PGJ2, which is associated with the atheroprotective nature of laminar flow. Consequently, phase 2 inducers represent an attractive and safe alternative to COX-2 inhibitors based on their anti-inflammatory potential and their highly beneficial antioxidative properties. [Emphasis added]

“Phase 2 proteins, mainly enzymes, include the classical ones, such as NAD(P)H:quinone oxidoreductase 1, glutathione-S-transferases, UDP-glucuronosyl transferases, as well as the more recently defined proteins ferritin H, metallothioneins, cystine/glutamate antiporter, and L-gamma-glutamyl-L-cysteine ligase. Phase 2 protein genes are coordinately upregulated through activation of an antioxidant response element (ARE) . . .”7

Dietary ingredients that induce phase 2 enzymes include curcumin,2,3 extracts of broccoli, green onion, green cabbage, purple cabbage, black cabbage, and cauliflower,4as well as asparagus, celery, and eggplant,5 and green tea.6 As one study7 explained, “A potent phase 2 protein inducer is sulforaphane, the isothiocyanate metabolite of the glucosinolate glucoraphanin. Glucosinolates are beta-thioglucoside N-hydroxysulfates present in 16 families of higher plants with the distribution in the family Brassicaceae, particularly the genus Brassica . . .” Brassica vegetables include broccoli, cauliflower, and related cruciferous types. Seabuckthorn8 was also reported to be a phase 2 inducer. Quercetin was reported9 to induce glutathione concentration and the activity of the phase 2 enzyme gamma-glutamylcysteine synthetase, the rate-limiting enzyme of glutathione synthesis. Although not a natural dietary ingredient, BHT is also an inducer of phase 2 enzymes. Copper and zinc induce metallothioneins.


  1. Healy et al. Divergent responses of chondrocytes and endothelial cells to shear stress: cross-talk among COX-2, the phase 2 response, and apoptosis. Proc Natl Acad Sci USA 102(39):14010-5 (2005).
  2. Sharma et al. Antioxidant role of glutathione-S-transferases: protection against oxidant toxicity and regulation of stress-mediated apoptosis. Antiox Redox Signal6(2):289-300 (2004).
  3. Iqbal, Sharma, et al. Dietary supplementation of curcumin enhances antioxidant and phase 2 metabolizing enzymes in ddY male mice: possible role in protection against chemical carcinogenesis and toxicity. Pharmacol Toxicol 92:33-8 (2003).
  4. Laso et al. Induction of NAD(P)H quinone oxidoreductase by vegetables widely consumed in Catalonia, Spain. Nutr Cancer 52(1):49-58 (2005).
  5. Yeh, Yen. Effect of vegetables on human phenolsulfotransferases in relation to their antioxidant activity and total phenolics. Free Rad Res 39(8):893-904 (2005).
  6. Lin et al. Hypolipidemic effect of green tea leaves through induction of antioxidant and phase 2 enzymes including superoxide dismutase, catalase, and glutathione-S-transferase in rats. J Agric Food Chem 46(5):1893-9 (1998).
  7. Noyan-Ashraf et al. Dietary approach to decrease aging-related CNS inflammation. Nutr Neurosci 8(2):101-10 (2005).
  8. Padmavathi et al. Chemoprevention by Hippophae rhamnoides: effect on tumorigenesis, phase 2 and antioxidant enzymes, and IRF-1 transcription factor. Nutr Cancer 51(1):59-67 (2005).
  9. Schart et al. Enhancement of glutathione and gamma-glutamylcysteine synthetase, the rate-limiting enzyme of glutathione synthesis, by chemoprotective plant-derived food and beverage components in the human hepatoma cell line HepG2. Nutr Cancer 45(1):74-83 (2003).


The United Nations Codex Alimentarius Commission is working steadily to develop an international regulatory regime for dietary supplements, including health claims. While theoretically the rules developed by the Codex would apply only to international trade and could not be required of purely domestic trade within the United States (except via new legislation passed by Congress), the workings of the World Trade Organization, which would administer the Codex rules to international trade, are complex, and one can never be sure that there isn’t a gotcha (now or later) that could be used to force these standards upon the U.S. Hence, vigilance is important to keep track of what Codex is doing and especially to learn of any attempts to impose this on the domestic U.S. market. (Just what we need: another layer of top-down, unaccountable, meddling bureaucracy between us and the ability to purchase what we want and to get the information we desire.)

We report here a few of the U.S.’s official statements in the U.S. Draft Position as of October 14, 2005, on the “Codex Committee on Nutrition and Foods for Special Dietary Uses, 27th Session.” The U.S. agrees that:

  • Claims should be prohibited if they cannot be substantiated. (p. 68)

Comment: The U.S. already has clear laws and court rulings specifying that health claims can be prohibited only if they are inherently misleading (that is, no disclaimer can correct for potential misleadingness in the claim). Moreover, “substantiation” for health claims is defined under U.S. law and may have little to do with “substantiation” as understood by the Codex Commission, which is, after all, an international body made up of a large number of countries. The commission, in fact, is dominated by Europe and its anti-health claim philosophy.

  • Health claims should be consistent with national health policy, including nutrition policy, and support such policies where applicable. (p. 68)

Comment: This is a purely political policy, having nothing to do with the scientific basis of a health claim. In the consideration of acceptance (or not) of health claims, the truth of the health claim should be all that matters. In the United States, denial of a health claim that is scientifically accurate is a violation of the First Amendment.

  • This preliminary assessment [of a proposed health claim] may serve as a basis for identifying prohibited health claims (e.g., if the claim is about treatment of a disease), and for selecting studies to evaluate a health claim. [Emphasis added] (p. 73)

Comment: As we have noted before, there is no constitutional or statutory authority for the FDA to prohibit health claims about the treatment of disease, provided the claim is truthful and not misleading. There is ongoing legal action by us and others on this point, as the legal monopoly of pharmaceutical drugs on “treatment” claims is at stake and worth billions. Also, the fact that treatment claims are given as an example of prohibited claims implies that there are others.

  • The expected beneficial effects and, if appropriate, its adverse effects, which may appear after long-term consumption of the [food(s) bearing a health claim] should be considered. (p. 76)

Comment: Here, the FDA proposes to grant itself the authority to do risk/benefit analyses on dietary supplements, as is done on drugs, which has not been authorized under Congressional statute. Dietary supplements are, according to U.S. statute, to be treated as foods, which are not required to provide evidence of benefits before sale and are not subject to FDA risk/benefit analysis.

The July 2005 official version of the “Proposed Draft Recommendations on the Scientific Basis of Health Claims at Step 3” of the “Codex Committee on Nutrition and Foods for Special Dietary Uses, 27th Session” includes additional threats to freedom of informed choice. The Codex Committee proposes that safety requirements include:

  • The expected level of consumption shall not exceed any relevant internationally recognized level of safe intake (e.g., ADI, if an ADI has been set), for any constituent present in the food. (p. 4)

Comment: This is outrageous! The U.S. would be expected to comply (at least in international trade) with a standard set internationally (that is, largely by other countries). All such issues are covered under United States law.

  • The risk from a change in the dietary pattern of the consumer, triggered by the emphasis on the product, resulting in its excessive consumption, leading to nutritional imbalance. (p. 4)

Comment: There is a great deal of interpretation and judgment to be made here, with an inherent risk of excessive and unreasonable regulation, especially when “proper” nutritional intake is based upon political policies. (An example of a political food policy: the USDA beef-grading system assigns the highest ranking to “prime,” which is the meat highest in fat content. Thanks a lot, federales.)

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