AT LAST - WHY SUGAR KILLS!

The BBC* broadcast the following "Discovery" program on the 31 meter
shortwave band, October 10th, 1989. Wholesale Nutrition heard about it
and the BBC kindly provided the following transcript:

DISCOVERY, EDITION 785

STEPHEN HEDGES: Hello and welcome to Discovery. Today we discuss some
ideas about the causes of ageing. I hope you're not enjoying a sticky
bun or drinking a cup of sugary hot chocolate as you listen. If it's a
between-meals snack, you could be in for a shock. Writing in a recent
issue of the New Scientist, researchers based at the University of
Oxford and at the Open University, report that taking sugary snacks
between meals may damage vital body proteins and cause premature
ageing. Their experiments suggest that high levels of sugars in the
blood cause proteins to stick together. Normally special enzymes
unstick the glycated proteins, but if sugar levels are raised between
meals the enzymes can't cope, and the proteins become permanently
damaged. Being partial to the occasional Chelsea bun myself, I took the
train to Oxford and found Dr Anna Furth in her laboratory at the Open
University's research unit. She explained why they think high levels of
sugar damage proteins.

DR ANNA FURTH: Well the damage to the protein takes place in 2 stages
because the first product that's formed by glucose attacking the
protein is called a Schiffs base and that, within a matter of days,
will slowly convert to the next product which is called an Amadory
product and these 2 modified forms of the protein are known as the
early glycation products and there's a lot of discussion as to how
debilitating they are. But, as any protein chemist will tell you,
you've only got to modify the surface of a protein very slightly and
you are likely to alter its reactions with other molecules in the body
because protein reactions are in essence controlled by their surface
shape. So what it could well add up to is a series of minor
disabilities rather than a specific illness. And with short-lived
proteins you do get replacement molecules within a matter of weeks so
you can get fresh molecules that are not glycated. Albumin, once it's
glycated - and 1 in 3 molecules of albumin are glycated, even in normal
people - is much less efficient at carrying long chain fatty acids, and
this you'd expect to have some effect on fat metabolism, however minor.
And there's another protein in the serum, a lipo- protein which is used
to carry cholesterol and if you glycate that in a test tube to the same
extent as you can find it in the body, then it's not picked up by cells
and that is bound to have some effect on the metabolism and the
transport of cholesterol.

HEDGES: Now I believe from what you were saying that diabetics have
more of these glycated proteins. Is there any indication of the sort of
long-term damage that high levels might cause?

FURTH: Most of the interest in long-term damage has been directed at
the long-lived proteins which are there long enough for the final
stages of glycation to take place and that's collagen and crystallin in
the eye lens. It's well known that diabetics are more likely to have
cataracts than non-diabetics. Even short-term damage may be caused by
glycation of basement membrane components. Now, the basement membrane
is a lining underneath capillaries and it's also part of the kidney
filtration mechanism and its function seems to be to filter out large
molecules from the nutrient fluid that comes out of capillaries and
nourishes tissues like the retina and muscles and lots of other
tissues. An unfortunate characteristic of diabetic tissue is that the
basement membrane does get very thick, and that obviously upsets its
filtration properties, and several of the components, notably a
specialised collagen which is used to make a filtration network, and
fibronectin, both of these proteins are more heavily glycated in
diabetics and if you glycate them to the same amount in a test tube,
you can impair their filtration mechanisms and they certainly don't
form a nice network as they would otherwise do.

HEDGES: Are there any ways of preventing this damage? I'm thinking
perhaps of drugs that you might use.

FURTH: The only drug that's been, as it were, designed to prevent
glycation has been developed by Professor Cerami's group at the
Rockefeller Institute in the States, and this is called amino-
guanidin, and it was aimed to block the most reactive glucose modified
protein called the Amadory product and it is said that if you feed it
to diabetic rats, it does stop their basement membranes from thickening
but that takes 5 months of feeding and it stops their aortic collagen
from getting cross-linked. It has been tried on humans for 2 weeks with
apparently no ill effects but there has been no large-scale clinical
trial and at the moment they have taken out a patent to use it for
preventing ageing in food proteins and in animals. So that's
amino-guanidin. Surprisingly, the most effective drug seems to be
aspirin - I say surprisingly because it wasn't intended as an
anti-glycation drug, but studies by John Harding in Oxford, and his
collaborators, have shown that if you take a group of people who have
got cataracts and another group of comparable age, and ask them if they
have taken any drug for more than 4 months continuously at any time in
their life, you find that if they've taken aspirin or Paracetamol or
Neurofen, there's a distinct so-called protective effect against
cataracts. In other words, statistically they are less likely to
develop cataracts than if they haven't taken these drugs over this
period. And there's not been a deliberate clinical trial but it seems
that if you take even just 1 aspirin a day for 18 months, you might
protect against cataract. But cataract is largely due to glycation of
the eye lens protein which is unusual in that it's never replaced, or
virtually never - it's a very long-lived protein. And the big question
is, of course, whether aspirin will have a similar protective effect
against other proteins, particularly, say, the basement membrane
proteins.

HEDGES: Is it known how these anti-inflamatory drugs like aspirin and
Neurofen might be having this effect?

FURTH: Well it's originally thought with aspirin that it reacted itself
with the protein at the same site that would otherwise be attacked by
glucose. But then it was realised that some of these other
anti-inflamatory drugs don't have quite the same structure as aspirin
so they couldn't affect the proteins in the same way. So I think the
answer is that no-one is very clear how the drugs work and maybe it is
simply an effect through a rather complex series of reactions that
actually lower the blood glucose.

HEDGES: Does the body itself have any way of preventing the cross-
linking of these glucose modified proteins?

FURTH: Well it used to be thought not, but fairly recently a group in
South Carolina, led by John Baines, have found a derivative of proteins
called carboxylmethyl lysine which is much more pronounced in diabetics
and has come from the breakdown of products that have been modified
glucose, but have then oxidised to convert the glucose, add-up to
something which is comparatively harmless because it can't cross-link.
And the nice thing would be, of course, if you could encourage this
oxidation reaction but at the moment naturally it only breaks down
about 10% of the glucose modified proteins so on its own it doesn't
help you very much.

HEDGES: Are all researchers agreed about the way that sugar damages
proteins, or are there some scientists who have rather different ideas?

FURTH: I think most people agree that the route for the damage is that
a glucose molecule attaches to a protein and then becomes irreversibly
attached through an internal re-arrangement and may then go on to
cross-linking. But there is a group at University College in London,
led by Simon Wolff, who feel that it is not so much the glucose itself
that attacks the protein but the oxidation products of glucose and that
this can actually fragment proteins and therefore conditions which
enhance oxidation are the ones to be avoided.

HEDGES: Now if Dr Wolff is right, what can you actually do about it? Is
there some other way of preventing the damage?

FURTH: Well, there's a lot of interest in taking anti-oxidants like
vitamin C and vitamin E, and if he's right that this oxidative
fragmentation is the major route by which glucose damages proteins then
possibly vitamin C or vitamin E would help but I have to point out that
the body's own mechanism for getting rid of glucose- damaged protein
seems to be the route discovered by John Baines which is an oxidation
in itself. So if you go around taking a lot of vitamin C you would be
tending to depress that reaction maybe. It's far more complicated than
that. I would also point out that vitamin C in the test tube, if you
leave it sitting with a protein, it will cross- link it and form the
same sort of undesirable products very nicely.

HEDGES: Finally, what would your advice to people be to avoid this
long-term protein damage? Do we have to take drugs or are there other
things that we might do?

FURTH: Well there is a much simpler method which is to avoid taking
glucose in the first place and obviously one can't be too glib about
this because we rely on glucose for food and energy. I think it's
important to point out that the body has no means of controlling this
particular reaction unlike all the other reactions that go on, and are
controlled by enzymes, and the only controls are the concentration of
glucose that the protein is exposed to, and the length of time it's
exposed. And obviously both those things tend to be greater in
diabetics but I think that what people have not emphasised is that as
you get older, every time you take a carbohydrate-containing meal, your
blood glucose does go up and it's a perfectly normal phenomenon, but
the older you get, the higher it goes and the longer it takes to come
down. And if you're looking for small cumulative changes in your
proteins, which is exactly what we think happens in ageing, this
glycation after a meal could contribute and so if you wanted to reduce
the likelihood of glycation, you clearly can't stop eating, but I think
you can minimise the exposure by perhaps cutting down on snacks that
contain carbohydrate.

HEDGES: Dr Anna Furth of the Open University. And the message would
clearly seem to be, cut out those sugary between-meals snacks, even
when you're listening to Discovery in the World Service of the BBC.

* British Broadcasting Corporation World Service, Stephen Hedges -
Science, Industry & Export Unit, Bush House, Strand, London WC2B 4PH,
England.

STILL LIKE SUGAR? WELL HERE'S A PARAGRAPH OF WHOLESALE NUTRITION'S MAY
'84 NEWSLETTER #18:

VITAMIN C AND SUGAR: Ascorbic Acid (AA) and Dehydroascorbic Acid (DHA)
are on opposite sides of a chemical equation that expresses an
important reaction that's continually going on in our body. Depending
on conditions, the reaction can go from left to right or from right to
left, that is, AA and DHA are two forms of the same chemical that are
constantly being transformed back and forth. Now we all know that AA
(vitamin C) is extremely important to our health, but few of us know
that DHA can be deadly. DHA, for instance, is thought to be involved in
deterioration of the circulatory system, heart attacks, cancer, and
birth defects. Also, and what may be most important, DHA has a
lympholytic effect which reversibly atrophies the thymus and thus
suppresses the immune system. It's known that stress will cause AA to
convert into DHA and may be the reason why stress is implicated in all
of the above conditions. It's very important, therefore, to maintain a
high AA/DHA ratio (of at least 10/1). It's thought that the body may
have developed a method of doing this for us by taking a certain amino
acid precursor (found in high levels in raw or lightly cooked broccoli,
cauliflower, Brussels sprouts and cabbage) and using it to make a
tri-peptide amino acid, called glutathione, which then, inside every
cell of our body, and as soon as the DHA enters the cell, converts the
DHA back to AA. Unfortunately, when you eat sugar, you interfere with
this whole delicate process by inhibiting the transport of DHA through
the cell wall. Whatever type or form of sugar (including honey and
fructose) or rapidly hydrolyzable starches (such as white rice, bread
and potatoes) we eat, it's all converted by our body into glucose, and,
since it's our only source of energy, is given 1st priority by the
cells. The glucose then proceeds to occupy all of a cell's receptor
sites and prevents the entrance into the cell of DHA, and, as a result,
the DHA doesn't get converted back to AA by the glutathione in the
cell. The best method of determining whether your average sugar intake
is excessive is to test (for about $20) your blood for glycosylated
hemoglobin A1C ("A-one-C"). Although the "normal" range is said to be
from 5 to 9, Dr John Ely, of the Univ. of Washington in Seattle,
strongly suggests your A1C must be less than 7. For instance, in a
study of 114 pregnant women, those having an A1C greater than 8.5
during early pregnancy showed a 22% chance of giving birth to a
markedly abnormal baby (malformed body, undeveloped brain). But it
dropped to 0% for those whose A1C was less than 7.

So, the bottom line is, in addition to taking your normal vitamin C, to
eat plenty of those vegetables mentioned above, avoid stress, and above
all, TO AVOID SUGAR!! I want to thank Dr Ely for all of the above,
since much of it is proprietary pre-publication information that he's
allowing me to break to you first.

To subscribe / unsubscribe:  chrisgupta@alumni.uwaterloo.ca
List information is at: http://tinyurl.com/2xohw
ARCHIVES: http://www.newmediaexplorer.org/chris/archives.htm
Share The Wealth: http://www.newmediaexplorer.org/chris/
Communication Agents: http://www.communicationagents.com/
Council Member: Friends of Freedom - http://www.friendsoffreedom.org