Study links gluten to male problems – sexual and otherwise

Study links gluten to “male problems”

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Study links gluten to male sexual problems

Many people avoid gluten because of its immunogenic properties.

Its proline‐rich components make it more difficult to break down than most proteins.

Ingesting gluten often leads to the absorption of long peptides, with subsequent histamine and interferon-γ release, causing inflammation.

But for those who’d rather eat it, or who cannot avoid it in certain situations…

…there are ways to help break it down.

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The trick is to use specific enzymes which can break down the proline and glutamine regions of the protein.

Your run‐of‐the‐mill enzymes can’t do this.

People have some of these proline enzymes naturally, but they can be downregulated for a variety of reasons.

Mice bred to lack one such proline‐cleaving enzyme – dipeptidyl peptidase – lost weight when they were fed a grain protein.

Other proteins didn’t have that effect, and the animals that had the enzyme naturally did better.

Proline‐cleaving enzymes allow people’s bodies to deal with grains and nuts.

An enzyme supplement of this type should help people who are eating resistant proteins to be healthier.

There is considerable evidence that this actually works.

These enzymes can digest even gluten to the point where it won’t cause interferon-γ release – even in people who are sensitized to gluten:

In this study, researchers analyzed the gluten fragments produced by digestive enzymes.

They mixed these fragments with T-cells from gluten‐sensitized people.

This is perhaps the best way to determine with absolute certainty that the gluten was broken down sufficiently.

“In many cases, PEP alone is enough to achieve complete detoxification of gluten pre-digested by pepsin and the pancreatic enzymes.” 

You would expect that during normal digestion wheat proteins would encounter certain enzymes.

When using only these expected enzymes, wheat protein gave a strong response.

But the addition of the extra proline‐cleaving enzyme almost completely eliminated the immunogenic effect on T‐cells:

The normal digestive enzymes failed to do the job completely… which is exactly why we have so many people responding to grain proteins.

The addition of prolyl endopeptidase (PEP) broke the gluten down into smaller, non‐immunogenic fragments after a few minutes.

It does this predictably. And it is dose‐dependent.

It has even been shown to work in animals as well as humans:

In this study on rats, researchers took predigested gluten (after the action of normal enzymes) and infused it into living rats.

The control group was fed only this. The experimental group was given a proline‐cleaving enzyme in addition, through a separate tube.

“The work presented here has demonstrated the resistance of several immunogenic gliadin peptides to gastric, intestinal brush-border proteolysis.”

The collection tube was placed twenty centimeters downstream.

As they increased the concentration of the proline‐cleaving enzyme, the immunogenic peptides were reduced in length – eventually approaching one or two amino acids in length:

This shortening of the immunogenic peptides would, of course, eliminate the antigenic potential of wheat protein.

If there are no resistant proline‐rich fragments, then there is no release of histamine and interferon‐γ release… and therefore no damaging prostaglandins.

And prostaglandins are linked to male sexual dysfunction, degradation of the testosterone-producing Leydig cells, and more…

“These results clearly illustrate the dramatic effect of prolyl endopeptidase on luminal peptides.”

The enzyme prolyl endopeptidase can make both grain and nut proteins behave like normal vegetable or meat proteins.

Many other studies confirm this effect – and in humans:

Twenty people on a gluten‐free diet were assayed for interferon‐γ beforehand. Then they were given either gluten or gluten acted upon by prolyl endopeptidase.

The response was predictable:

Patients who were given the gluten with the resistant proline bonds broken were essentially free of any response.

The gluten becomes innocuous, just like any normal protein:

This is crucial since interferon‐γ greatly upregulates two enzymes… inducible nitric oxide synthase (iNOS) and phospholipase A₂.

These together increase nitric oxide and prostaglandin levels.

Chronically high levels of these can contribute to asthma, arthritis, and hair loss (among other things).

“In the participants receiving placebo‐treated gluten the mean increase in the interferon‐γ ELISpot response on day 6 compared to day 1 was significant.”

(ELISpot is a method of monitoring immune response.)

Since interferon‐γ was released by gluten – but prevented by proline‐cleaving enzymes – you can be almost certain that histamine was released as well.

Histamine is likely what causes the subtle neurological symptoms behind food reactions.

The brain has mast cells, and histamine can be released from mast cells when large foreign peptides are absorbed.

Histamine is also classified as a neurotransmitter.

Older studies show the enzyme papain, which comes from papaya, to be effective as well.

As it is an available, cheap, and safe enzyme, this has appeal.

These enzymes can cleave proline–glutamine‐rich regions of wheat, corn, oats, peanuts… and any other protein with a resistant proline–glutamine repeat.

This can reduce or eliminate chronic inflammation, while you get to continue eating the foods you’re used to or that you’re socially coerced into eating.

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Matt Cook is editor-in-chief of Daily Medical Discoveries. Matt has been a full time health researcher for 26 years. ABC News interviewed Matt on sexual health issues not long ago. Matt is widely quoted on over 1,000,000 websites. He has over 300,000 daily newsletter readers. Daily Medical Discoveries finds hidden, buried or ignored medical studies through the lens of 100 years of proven science. Matt heads up the editorial team of scientists and health researchers. Each discovery is based upon primary studies from peer reviewed science sources following the Daily Medical Discoveries 7 Step Process to ensure accuracy.
Tye-Din, Jason A. "The effects of ALV003 pre-digestion of gluten on immune response and symptoms in celiac disease in vivo." Clinical immunology (2010) http://www.sciencedirect.com/science/article/pii/S1521661609008651 Piper, Justin L. "Effect of prolyl endopeptidase on digestive-resistant gliadin peptides in vivo." Journal of Pharmacology and Experimental Therapeutics (2004) http://jpet.aspetjournals.org/content/311/1/213.short Marti, Thomas. "Prolyl endopeptidase-mediated destruction of T cell epitopes in whole gluten: chemical and immunological characterization." Journal of Pharmacology and Experimental Therapeutics (2005) http://jpet.aspetjournals.org/content/312/1/19.short Messer. "Studies on the mechanism of destruction of the toxic action of wheat gluten in coeliac disease by crude papain." Gut (1964) http://gut.bmj.com/content/gutjnl/5/4/295.full.pdf

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