From:
Guy R. Schenker, D.C.
October, 1997


Dear Doctor,

     In last month's Letter you learned that with the    
magical ...

                     ABRACADABRA ZAP ...

you give your patients with Oxy A-Plus and Oxy D-Plus, along 
with the unique combination of ingredients in Oxy A and Oxy D, 
there is no anaerobic/dysaerobic clinical challenge you cannot 
meet.

     But, believe it or not,

            THERE IS EVEN MORE YOU CAN DO FOR YOUR
                ANAEROBIC/DYSAEROBIC PATIENTS.

Your QRG lists several amino acids which can take your 
clinical results from excellent to spectacular.  On the 
dysaerobic side of your QRG you will note that it is often 
beneficial to give your patients the amino acids histidine and 
glutamine above and beyond what is already contained in their 
Oxygenic D.

     We already covered histidine in our discussion several 
months ago of electrolyte stress imbalance.  Histidine was 
recommended for those patients who have a dysaerobic oxidative 
stress as a major part of their cardiovascular disease.  We 
noted in that Letter that histidine has a specific protective 
effect on the arterial intima.  It is also a vaso-dilator and 
thus decreases blood pressure.  We also noted that Histidine 
has been shown to decrease angina pain.

     These and all the other beneficial effects of histidine 
are associated with its unique antioxidant activity.  
Histidine is the most effective naturally occurring singlet 
oxygen scavenger.  That makes it the most important 
antioxidant found in our diets.
                            - 2 -


     What exactly does it mean to be a singlet oxygen 
scavenger?  A classic free radical contains an unpaired 
electron which makes it highly reactive.  There is, however, a 
reactive, highly unstable oxygen species called singlet oxygen 
that contains a pair of electrons (and so technically cannot 
be classified as a free radial itself).  But since the two 
electrons exist in unstable form, this molecule participates 
in reactions that generate free radicals.  One example is the 
super oxide radical.  Deactivating singlet oxygen with 
histidine prevents the formation of the super oxide radical.  
(The other common singlet oxygen quencher in our diet is beta 
carotene, though it is not nearly as powerful as histidine.)

     Histidine has been found to be particularly effective in 
the following conditions (frequently found in dysaerobic 
patients):  rheumatoid arthritis, anemia, allergies, and 
nausea (including nausea of pregnancy), and upper GI ulcers.

     Regarding rheumatoid arthritis, it has been shown that 
both NSAIDS and steroids lower plasma histidine.  So, while 
affording temporary relief, they actually exacerbate the 
condition.

     Aging is largely a cumulative effect of excessive 
oxidative free radical damage in the body.  A chronic 
dysaerobic imbalance is always associated with tissue 
destruction and premature aging.  It is interesting to note 
that low histidine levels are strongly correlated with aging.

     Your other powerfully anti-dysaerobic amino acid is 
glutamine.  There is so much to be said about this amazing 
amino acid and its anti-dysaerobic effects that I don't know 
how I can cover it in less than 10 pages.  But here goes:

     The specialized biological activities of glutamine can 
all be attributed to two distinctive qualities it possesses:

1.  It is the one amino acid that contains two nitrogens, not 
just one.  Therefore, it functions throughout the body as a 
nitrogen shuttle.  Its role as a nitrogen shuttle is the basis 
of all glutamine's metabolic effects outside the GI tract.    

2.  In the GI tract glutamine is used directly by the cells of 
the GI lining for food.  Glutamine is absorbed by enterocytes
where it is broken down to eventually yield 5 ATP for every 
glutamine molecule.  You must understand (and this is 
important because almost no other clinicians understand this) 
that almost no glucose is utilized by enterocytes for energy.
In other words, glutamine is the source of fuel which the 
intestinal tract uses to perform its functions and to maintain 
itself structurally.
                            - 3 -


     Let us talk about the GI functions of glutamine first.
You note that ulcerative colitis, mucus colitis and certain 
other GI ulcers are typical of your dysaerobic patients.  
Glutamine is even more essential for the GI tract of the 
dysaerobic patient than for the rest of us.  Glutamine is 
essential for the maintenance of GI cell metabolism, for the 
maintenance of its structure and for the maintenance of GI 
epithelial function.

     Leaky gut syndrome (which is associated with chronic 
allergic symptoms as well as absorption of bacterial and viral  
toxins) can be reversed with glutamine supplementation.  The 
negative impact of disease/stress is far greater and occurs 
far earlier in the GI tract than any other organ.  Further-  
more, the recovery time from disease or stress is much longer 
in the GI tract than in other organs.  (Fibromyalgia is one 
example of a stress-related disease that has a GI component 
and is always associated with leaky gut syndrome.)

     Secretory IgA is the most abundant immunoglobulin in the 
intestinal immune barrier.  The synthesis and expression of 
secretory IgA requires adequate glutamine.

     Regarding GI ulcers, glutamine supplementation results in 
complete healing within four weeks of 92% of ulcer patients.

     Glutamine supplementation has been shown to be beneficial 
in patients with inflammatory bowel disease.  The glutamine 
helps decrease inflammation, helps repair the epithelial 
tissue, and helps decrease the excess mucosal permeability, 
thus decreasing the absorption of enterotoxins.  Glutamine 
supplementation is therefore indicated in therapeutic doses 
for all your dysaerobic patients with irritable bowel syndrome 
and inflammatory bowel disease and chronic diarrhea.  (It is 
also beneficial for viral diarrhea for any patient.)

     Glutamine has also been shown to prevent and eliminate 
gall stones.  Glutamine achieves this by increasing bile flow 
and by decreasing the ionized calcium concentration of the 
bile.

     Consider now the other unique biological activity of 
glutamine -- its ubiquitous presence as a nitrogen shuttle.
As part of the body's stress reaction, muscle tissue breaks 
down and amino acids are liberated.  (This catabolic state is 
exaggerated in your dysaerobic patients.)  Glutamine comprises 
33% of the amino acids liberated from muscle breakdown during 
stress.  What is more, 60% of the free amino acids in the 
intracellular amino acid pool (mostly found in muscles) 
consists of glutamine.  This amino acid pool is reserved to be 
mobilized into plasma when amino acids (particularly
                            - 4 -


glutamine) are needed at other organ sites.  So we see that 
muscle tissue is first a storage depot for glutamine, and 
second, a synthesizer of glutamine.

     In response to stress (either emotional or disease 
related) glutamine synthesis increases by 200 to 400%, yet the 
glutamine level in muscles decreases by 50% and the glutamine 
level in the blood decreases by 30%.  How is it that glutamine 
levels decrease while synthesis is actually increased by two 
to four times?  It is decreased simply because glutamine is 
utilized for tissue repair throughout the body and especially 
to maintain the GI mucosa.  The muscle wasting that occurs 
when a person is sick or under chronic stress is virtually 
100% due to a glutamine deficiency.

     Following is a list of other glutamine functions related 
to its nitrogen shuttle capacity, and which are particularly 
relevant to your dysaerobic patients:

1.  Low glutamine levels decrease the activity of lymphocytes, 
decrease phagocytosis, and decrease the levels of 
immunoglobulin A, thus crippling immune function.  One study 
showed that among animals made septic with massive doses of 
bacteria, 21 of 38 died, yet when given glutamine for one week 
prior only 3 out of 38 died.  Another study showed that when
animals were given an enzyme to destroy glutamine they all 
became rapidly immuno-suppressed; all developed necrotizing 
enterocolitis and died.

2.  In burn patients glutamine levels were shown to drop by
58% and remained far below normal for 21 days.  This relates 
to the immuno-suppression that occurs in burn patients.  It 
was further found that the chance of infection in a burn is 
inversely proportional to the glutamine levels.  From a 
NUTRI-SPEC perspective, burns are a dysaerobic lesion.  (Note 
that Oxygenic D-Plus is extremely effective when used 
topically on burns for the first three days.  The effect on 
healing is unbelievable until you have seen it yourself.)

3.  Auto-immune diseases are typified by the presence of 
excess cytokines.  (Rheumatoid arthritis patients have 50%
more than normal.)  Glutamine has a dramatic impact on
decreasing cytokine production.  (NOTE:  On the DYSAEROBIC 
page of your QRG, add rheumatoid arthritis to the conditions 
for which glutamine supplementation is indicated.)

4.  When an athlete over-trains (and they all do) glutamine 
levels decrease 9% below normal.  This is due to muscle 
catabolism that exceeds the anabolic rebuilding capacity.  The 
glutamine is also pulled out of muscles to be sent to the 
kidneys to help eliminate the acids produced during exercise.
                            - 5 -


The low glutamine levels from over-training decrease the 
athlete's resistance to infection and decreases the healing of
wounds and athletic injuries.

     Many athletes supplement with substances purported to be 
anabolic aids.  Most of them are an ineffective waste of 
money.  If there is one anabolic aid that would really work 
for athletes it would be glutamine.  Glutamine has been shown 
to stimulate human muscle glycogen synthesis following 
exercise.  Glutamine administration has been shown to increase 
circulating plasma growth hormone concentration.

     Also note that glutamine is extremely heat labile and is 
thus destroyed in over-cooked foods.  Note further that 
glutamine is not a part of the protein powders taken as 
supplements by many athletes, yet it is the one component of 
protein that they really may need in supplement form.

5.  Glutamine is the most abundant amino acid in the cerebro- 
spinal fluid.  Glutamine is a precursor to glutamic acid (an 
excitory neuro transmitter which does not cross the 
blood/brain barrier), and, glutamine is a precursor to GABA 
(an inhibitory neuro transmitter).   Supplementation with only 
250-1000 milligrams per day of glutamine has been shown 
effective as an antidepressant and a mood elevator.  Keep this 
in mind for your dysaerobic patients.  (In fact, you may add 
this to your QRG page as a dysaerobic condition for which you 
give additional glutamine.)  Other brain effects of glutamine  
include improved problem solving on continuous performance 
tests -- and the effect here was immediate.  Glutamine has 
also been shown to decrease anger and decrease fatigue.

6.  Glutamine reverses the catabolic effect on muscles due to 
glucocorticoids.  Glutamine thus eliminates the muscle atrophy 
typical in patients taking glucocorticoids.

7.  Glutamine is effective in treating impotence.

8.  Low levels of glutamine (like histidine) are strongly 
correlated with aging.

     How's that for an impressive list of credentials?  
Certainly you see the many uses you have for histidine and 
glutamine supplementation in your dysaerobic patients.

     Now look at the anaerobic side of your anaerobic/ 
dysaerobic QRG page.  Three amino acids are listed as 
frequently beneficial for your anaerobic patients -- tyrosine, 
methionine and taurine.  We covered the benefits of tyrosine
in our discussion of electrolyte insufficiency imbalance in 
our March Letter.  Rather than repeat that discussion, suffice
                            - 6 -


it to say that tyrosine is compatible with an anaerobic body 
chemistry.  It elevates depressed levels of certain brain 
transmitters.  Tyrosine also has specific antihistamine 
activity and specifically strengthens thyroid function.  In 
terms of symptoms, it can be used for all your anaerobic 
patients with somnolence, fatigue, allergies or depression.

     Methionine is an essential amino acid that is powerfully 
anti-anaerobic by virtue of its sulfhydril group.  (Also note 
that methionine is the most heat labile of the amino acids and 
therefore is easily destroyed in over-cooked food.)  Via its 
active sulfur group methionine assists in detoxification.  
Methionine facilitates liver function and increases the 
production of lecithin in the liver.

     Methionine is lipotrophic -- helping the liver process 
and eliminate cholesterol and other fat.  Methionine also 
decreases histamine levels and is thus beneficial for your 
anaerobic patients with allergies.  Methionine has also been 
found beneficial in many cases of schizophrenia (and this is 
speculated to perhaps be due to its anti-histamine effect).

     Methionine also shows its anti-anaerobic activity in its 
effect on anaerobic cancers.  According to a study published 
in Nutrition and Cancer, it may prevent and even reverse 
certain cancers by permitting the remethylation of DNA 
methylation inhibited by a carcinogen.

     Our final anti-anaerobic amino acid is taurine, which you 
read about extensively in our May Letter regarding its use for  
your electrolyte stress patients.  The only clinical effect of 
taurine we did not cover in that discussion is its effect on 
the nervous system.  Taurine enhances brain function in many 
ways and has demonstrated a particular beneficial effect on 
seizure disorders.  It is important to note that virtually all 
seizure patients are anaerobic.

     In summary:  The majority of your patients have an 
anaerobic/dysaerobic component to their health problem.  (If 
the imbalance doesn't show up on initial testing it often will 
on a follow-up.)  With Oxy A & A+, Oxy D & D+, and the amino 
acids histidine, glutamine, tyrosine, methionine and taurine, 
you are equipped to empower these patients like no other 
clinician can.


                           Sincerely,



                           Guy R. Schenker, D.C.

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