Archives for: March 2011
I have difficulty losing weight and was interested in perhaps taking Deflect to "scrub" my body clean of all those nasty lectins adhering to my insulin receptor sites (they are probably all wheat lectins). Anyway, I read your article on Deflect, describing how it contains sacrificial carbohydrates to which lectins attach. My question is this....how do you know that a lectin happily sitting on a fat cell's insulin receptor site will want to move to a sacrificial carbohydrate? Why would it prefer the sacrificial carbohydrate over my fat cell?
ANSWER: To understand the answer to this question we should understand the nature of lectin binding. Lectins bind to carbohydrates reversibly or irreversibly. This is dependent on the shape characteristics of both the sugar that they are specific for and nature of the amino acid residues to which the sugar is linked to the cells wall. Small changes in the structure of the sites, such as the substitution of only one or two amino acids, also result in marked changes in specificity and avidity (the degree, or force of the attraction). Thus, although the sugar is the point of specificity, the amino acid 'stalk' determines much of the particular binding characteristics. (1) Some evidence also indicates that coordination with metal ions may occasionally play a role too.
The sugar is linked to the lectin mainly through charge attraction via covalent (electron sharing) bonds. The individual electron within these clouds of electrons are always moving.
Sometimes the one area of the cloud is more dense than another. This leads to the formation of a transient dipole within the molecule. The transient dipole can induce a dipole in an nearby molecule, by attracting its electrons. The attraction between the two oppositely oriented dipoles is termed a van der Walls interaction. In essence, van der Walls forces tend to 'push' the molecules towards each other, while shape conformity tends to 'pull' them towards each other.
Thus the attraction between lectins and carbohydrates is determined by both shape and charge.
One factor which influences agglutination is the zeta potential which surrounds the negatively-charged surface of the cell. Almost all particles in contact with a liquid acquire an electronic charge on their surfaces. Because of the large amount of sialic acids on the cell membrane the zeta potential is a bit more neutral compared to the charge on particles in suspension which are a bit more negatively charged. Most lectins are very highly positively charged.(3) Thus two amino sugars of similar shape can have two different levels of lectin avidity due to differences in their relative charge.
If we add to this slight structural differences in the amino acid residues between carbohydrates embedded in the cell membrane matrix and free carbohydrate in suspension, we get the force difference necessary to overcome the rather weak covalent bonds and van der Walls forces.
Just how 'hot' is this concept? Here's a summary from a just-published article:
"It is thus justified to compare crucial carbohydrate epitopes with the postal code ensuring correct mail routing and delivery. In view of the functional relevance of lectins the design of high-affinity reagents to occupy their carbohydrate recognition domains offers the perspective for an attractive source of new drugs. Their applications can be supposed to encompass the use as cell-type-selective determinant for targeted drug delivery and as blocking devices in anti-adhesion therapy during infections and inflammatory disease." (2)
Although completely unrelated, two other reasons amino sugars can be of use in weight management therapies:
1. They bind dietary fat. (4)
2. They increase production of the 'anti-fat' hormone, leptin (5) Leptin* acts on receptors in the hypothalamus of the brain where it inhibits food intake counteracts the effects of neuropeptide Y (a potent feeding stimulant secreted by cells in the gut and in the hypothalamus).
Click here for more information on DEFLECT products and lectin binding.
1. Sharon N, Lis H. Related Articles Lectins--proteins with a sweet tooth: functions in cell recognition. Essays Biochem. 1995;30:59-75. Review.
2. Rudiger H, Siebert HC, Solis D, Jimenez-Barbero J, Romero A, von der Lieth CW, Diaz-Marino T, Gabius HJ. Medicinal chemistry based on the sugar code: fundamentals of lectinology and experimental strategies with lectins as targets. Curr Med Chem. 2000 Apr;7(4):389-416. Review.
3. Monsigny M, Roche AC, Sene C, Maget-Dana R, Delmotte F. Sugar-lectin interactions: how does wheat-germ agglutinin bind sialoglycoconjugates? Eur J Biochem 1980 Feb;104(1):147-53
4. Han LK, Kimura Y, Okuda H. Reduction in fat storage during chitin-chitosan treatment in mice fed a high-fat diet.Int J Obes Relat Metab Disord 1999 Feb;23(2):174-9
5. McClain DA, Alexander T, Cooksey RC, Considine RV. Hexosamines stimulate leptin production in transgenic mice. Endocrinology 2000 Jun;141(6):1999-2002
* Not lectin!
QUESTION: As a type O I am using Fucus vessiculosis (Bladderwack) and the results have been superb. Now I have convinced my husband (as I, also a medical doctor) to to follow your diet, I wish to know if he may go onto Bladderwrack too, as he has H. pylori? Your response would be appreciated.
ANSWER: In ER4YT, I've written of the utility of Fucus (Bladderwrack) in helping to keep thyroid function normal in blood type O's and discussed the potential usefulness of this plant for preventing the adherence of some unwanted microorganisms (H. pylori for example) to the cells lining the digestive tract in blood type O's.
There is actually a good reason for my deference to this plant with regards to blood type O. As you might recall form ER4YT, blood type O is characterized by the presence of a terminal fucose sugar on its antigen. Things in nature (like lectins, bacteria, Candida, etc) with a preference for or a "sweet tooth" for fucose, will always have an affinity for and a greater impact on blood type O's. Since bladderwrack is such excellent food source of fucose and fucose containing sugar chains, it can actually bind many of the more problematic blood type O lectins, bacteria, and microorganisms.
One of the emerging fields of research with regards to microorganisms (and lectins) centers about an idea of adherence and anti-adherence. Basically, an unwanted organism can only produce a problem for you to the degree it can attach to or anchor itself to your cells. Lectin damage follows a similar pattern. Recognizing this simple concept of adhesion, you will readily recognize the usefulness of the concept of anti-adhesion, or blocking strategies. The question then becomes what foods might provide an anti-adhesion advantage for your blood type. One of the answers for blood type O is bladderwrack (Note: kelp also has a high amount of fucose sugars so is another answer). Basically, the fucose in bladderwrack can act as a false decoy, binding the unwanted blood type O environmental debris and sweeping it away before it can bind to or irritate the tissue.
Because A's, B's and AB's also usually contain some anchoring sites (but proportionately substantially less than an O) for fucose specific lectins and microorganisms, bladderwrack can also act as a form of anti-adhesion food for these blood types as well. However, they also have additional specific blocking sugars they can place at their disposal.
So, although you did not include the ABO group of your husband, Bladderwrack is a smart choice as a simple, safe anti-adhesion therapy for H. pylori.
Read More About Fucus
1. Nishino T, Nishioka C, Ura H, Nagumo T. Isolation and partial characterization of a novel amino sugar-containing fucan sulfate from commercial Fucus vesiculosus fucoidan. Carbohydr Res 1994;255:213-224.
2. Patankar MS, Oehninger S, Barnett T, et al. A revised structure for fucoidan may explain some of its biological activities. J Biol Chem 1993;268:21770-21776.
3. Nishino T, Nishioka C, Ura H, Nagumo T. Isolation and partial characterization of a novel amino sugar-containing fucan sulfate from commercial Fucus vesiculosus fucoidan. Carbohydr Res 1994;255:213-224.
QUESTION: Many thanks for your wonderful work. I think I can speak for the hundreds of thousands of people who have been so helped by your great work. I discussed your theory with the dietician who works at the university clinic where I am treated for inflammatory bowel disease who just scoffed at the theory that my improvement could have been the result of following the type B diet. In particular she said that there was no evidence that corn contained any lectin that specifically agglutinated type B blood. I am 80% better -and off of most of my medicines- thanks to your book. God Bless.
I've found most dieticians to be quite unaware (ignorant) of the large lectin literature to be found on such easily accessed venues such as MEDLINE or OVID. My suspicion is that because their education is insufficient in the basic rudiments of immunology and hematology, they cannot appreciate much of the lectin literature since it is quite complex. Sadly, your interaction is typical of the reaction of most "ADA-droids" when a little intellectual curiosity could have opened up new pathways of thinking.
That corn lectins (Zea Mays Agglutinin) is a d-galactose specific lectin has been known for over 25 years (1). The results of serological studies of Zea mays everta seed extracts with anti-B specificity showed the lectin will agglutinate type B and AB red blood cells. Interestingly corn lectin agglutinated A1B red blood cells significantly more weakly than A2B red blood cells.
"There are some people that if they don't know, you can't tell 'em." - Louis Armstrong
Prodanov P, Atanasova N. An anti-B lectin from Zea mays everta.Folia Haematol Int Mag Klin Morphol Blutforsch 1984;111(1):84-5
QUESTION: Firstly, FYI - followed type A diet and my tumour markers in blood dropped first time in 4 years after tumuour removed. Thank you!!! Second - type 'A' what do I need for obsessive thoughts?
ANSWER: That is great news, and yet again demonstrates the power of choosing foods by blood type versus the 'macromolecular' (fat-phobic/ fat-philic; protein-phobic/ protein-phillic) theories, which usually do no more than contradict themselves. With the blood type diet, you can make a difference in areas of your health not normally thought to be responsive to diet.
As far as obsessive thought patterns, this is not an easy answer. Some forms of obsessive behavior can be so severe as to hinder the performanace of routine actions. In many of these individuals, medication can help, at least initially. In type A individuals, the efficient modulation of the hormone cortisol can help temper obsessive-type thoughts. Strategies include tai chi, yoga, martial arts and meditation. Adaptogens can help improve stress response--try Korean or Siberian ginseng. The Ayurvedic herbs Ashwgandha, Brahmi (Bacopa) and Boerhaavia (Cortiguard is one formula) are well suited to type A's when under stress.
QUESTION: Disease susceptibility per ABO group has been based on information on subjects, as far as we know, who did not eat right for their blood type. How much do you project that these statistics will change for people who DO eat right for their type? Such as the high Cancer rate in blood type A's.
ANSWER: It has been speculated that 35% of all cancers are the result of genetic outcome, 35 percent the result of diet, and 30 percent the result of environment, principally smoking. If we assume that most(say 80%)of the dietary causes will have been eliminated (if you are type A, you are using soy products, aren't you?); that you don't smoke; and that understanding blood type susceptibilities (such as stress links) allows you to circumvent about 25% of the genetically determined cancers, we get:
You don't smoke: environmental causes go down to 5-8%.
You follow the blood groups A diet: diet causes goes down to about 7%
You control for effects of blood type on other suceptibilities: genetic causes go down to about 28-29%
The residuals: 8%(remaining environmental)+ 7%(remaining diet) +29% (remaining genetic) =44% total versus 100%
It would seem that folowing the blood group A diet should cut the rate of all cancers in that blood group by approximately one-half, which interestingly is about what I have documented in my practice.
QUESTION: I am a type A and have been trying to incorporate more of the recommended grains. I purchased amaranth and cooked as described however, it turned into a slimy goo. Is this the way it is supposed to be?
ANSWER: Amaranth is a broad-leafed plant which produces multi-headed flowerets containing grain-like seed of extremely high nutritional value. The tiny seeds are a creamy tan in color and are about 1/32" in diameter. Each plant produces 40,000-60,000 seeds. The amaranth seeds are used in their whole grain form, milled into flour or puffed into miniature kernels.
For centuries, the Aztecs and American Indians have known the benefits and diverse uses for amaranth.
Not only is amaranth higher in protein than most commonly used grains, that protein, containing high levels of lysine and methionine, is better balanced and more complete. Amaranth, with 13-19% protein, scores closer to a perfect 100 on a theoretical protein score chart than do other grains. For example, amaranth's 75 is significantly higher than wheat at 56.9, corn at 44, soybeans at 68 or even cow's milk at 72.5.
Amaranth possesses a potent lectin that has been shown to identify colon cancer cells which are in the early stages of mutation.(1) As such a diet high in amaranth may well be protective against this common cancer, which is known to have a significantly higher incidence in blood group A.
Here's a great recipe that uses amaranth flour to make a grain free bread:
Grain-Free Boston Brown Bread
Yield: 1 loaf
1 cup plus 2 tablespoons amaranth flour 1/4 cup arrowroot 1 teaspoon baking soda 1/2 teaspoon powdered ginger 1/2 cup currants 1/2 cup walnuts 3/4 cup boiling unsweetened fruit juice or water 1/4 cup honey or molasses 1 tablespoon lemon juice.
Generously oil a 1-quart mold or 1 pound coffee can. Fill a Dutch oven or stockpot with about 5 inches of water. Bring the water to a boil while you prepare the batter.
In a large bowl, combine the flour, arrowroot, baking soda and ginger. Stir in the currants.
In a blender, grind the walnuts to a fine powder. Add the juice or water, and blend 20 seconds. If the ingredients in the blender don't reach the 1 -cup mark, add a little more liquid. With the blender running on low, add the honey or molasses and lemon juice.
Pour the liquid mixture into the flour bowl. Stir quickly to blend; do not overmix. Transfer to the prepared mold orcan. Cover with a square of foil or wax paper; tie the wax paper securely with a piece of string.
Place the mold in the boiling water. (It should come halfway up the sides.) Cover the pot tightly, and steam for 2 hours over medium-low heat. Do not remove the cover during that time.
Remove the mold from the pot. Cool the bread in the mold for 15 minutes, then turn out onto a wire rack to cool completely. For the best results, cut with a serated knife with a gentle sawing motion.
Variations: Replace the honey or molasses with 1/3 cup maple syrup. Instead of the currants, use dried unsweetened pineapple, apples, prunes or ther dried fruit; use the corresponding juice as the liquid.
(1)Boland CR, Chen YF, Rinderle SJ, Resau JH, Luk GD, Lynch HT. Use of the lectin from Amaranthus caudatus as a histochemical probe of proliferating colonic epithelial cells. Cancer Res. 1991 Jan 15;51(2):657-65.