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Found 17 results

  1. Celiac.com 03/27/2017 - A number of researchers are looking to provide alternative or adjunct treatments to the gluten-free diet in celiac disease. Meanwhile, a number of companies are currently developing a wide variety of such options, ranging from various kinds of enzyme therapies, to treatments that eliminate celiac disease reactions, even to vaccines to inoculate celiac sufferers against their condition, perhaps allowing for full recovery and a return to non-gluten-free eating habits, as desired. At least, that's one dream. More likely will be the development of enzymes or other treatments that offer celiacs varying degrees of protection from gluten ingestion. Most likely, such treatments would be designed to augment an existing gluten-free diet, and to provide protection against moderate gluten-contamination when eating out. One particular enzyme that shows strong potential in breaking down toxic peptides in A-gliadin, the main culprit in celiac reactions, is caricain. A recent paper discusses the scientific principles behind the use of caricain for enzyme therapy. The paper is based on a recent study, in which a team of researchers set out to review the structures of the toxic peptides in A-gliadin for key sequences of amino acids or motifs related to toxicity, especially with respect to digestive difficulties, or immunogenicity. The research team included Hugh J. Cornell and Teodor Stelmasiak. They are affiliated with the RMIT University, School of Applied Sciences, Melbourne, Australia, and with Glutagen Pty Ltd, Maribyrnong, Victoria, Australia. For their study, they first evaluated structures of synthetic A-gliadin peptides shown to be toxic in the fetal chick assay, both before and after digestion with duodenal mucosa from patients in long remission. They also measured synthetic peptides corresponding to the undigested residues, and compared the key amino acid sequences, to see if they might be related to direct toxicity and immunogenicity of the peptides. They found that the smallest toxic peptides from celiac mucosal digestion were octa-peptides, which they found in greater amounts than similar products from normal digestion. One of those peptides corresponded to residues 12-19 of A-gliadin and contained the key motifs PSQQ and QQQP of De Ritis et al., while the other corresponded to residues 72-79, and contained the key motif PYPQ (extending to PYPQPQ). These key motifs have been noted by other workers, especially those investigating immunological activity over the past two decades. They are present in undigested residues from celiac mucosal digestion These motifs, along with the greater prevalence of these residues, as compared with residues from normal digestion, supports the basic notions underpinning enzyme therapy for celiac disease. This study also supports the basic scientific merits of research and development of the enzyme caricain to break down gliadin peptides with two different types of toxicity, and thus to potentially benefit people with celiac disease. Source: International Journal of Celiac Disease. Vol. 4, No. 4, 2016, pp 113-120. doi: 10.12691/ijcd-4-4-2 Previous study: NCBI
  2. Sandi Star, HHP, CNC, CCMH

    The MTHFR Mutation

    Celiac.com 02/08/2018 - Have you ever considered being tested for a genetic defect called MTHFR? If you have a family history of heart disease or stroke, migraines, trouble getting pregnant or have a child with Autism you might want to consider reading on to learn more. These are just a few of the list of conditions linked to MTHFR mutation. Surprisingly, 60% of our population has this mutation and most do not even know what MTHFR is. I recently came up positive myself for MTHFR A1298C. We will talk more about the two common markers in a bit. This changes everything when it comes to choices and is important to have the knowledge when choosing foods and supplementation. It's also important to monitor your folate levels. More to come. Interestingly, Untreated celiac disease may be associated with hyperhomocysteinemia caused by a combination of vitamin deficiencies and variants in the MTHFR gene. If you are not healing with a gluten free diet this might be a test to consider. [1] So, what is MTHFR? The MTHFR gene (methylenetetrahydrofolate reductase) is an enzyme that plays an important role in processing amino acids, the building blocks of proteins. Now you know why it's an acronym! Methylenetetrahydrofolate reductase is important for a chemical reaction involving forms of the vitamin folate (also called vitamin B9). This enzyme converts a molecule called 5,10-methylenetetrahydrofolate to a molecule called 5-methyltetrahydrofolate. This reaction is required for the multistep process that converts the amino acid homocysteine to another amino acid, methionine. The body uses methionine to make proteins and other important compounds. [2] Although, there are over fifty known MTHFR variants, two are commonly tested C677T and A1298. Some of the key things methylation process is responsible for are: Cellular Repair – DNA repair is a collection of processes by which a cell identifies and corrects damage to the DNA molecules that encode its genome (genetic material of an organism). Detoxification and Neurotransmitter Production – The interconversion of amino acids. Healthy Immune System Function – Formation and maturation of red blood cells, white blood cells and platelet production. What's the Difference Between the Two Most Common Types? The 677T Variant is associated with heart disease and stroke whereas the 1298C is associated with a variety of chronic illness. Either one however can cause general health problems. Homozygous vs Heterozygous An organism can be homozygous dominant, if it carries two copies of the same dominant allele (allele - one of two or more alternative forms of a gene that arise by mutation and are found at the same place on a chromosome.), or homozygous recessive, if it carries two copies of the same recessive allele. Heterozygous means that an organism has two different alleles of a gene. If you are homozygous (2 abnormal copies) your enzyme efficiency drops to 10% - 20% of normal which can be problematic. A more serious combination is 677T/1298C which has both genetic anomalies. If you are having symptoms and can't quite put your finger on it I would suggest getting tested for the MTHFR. That will help your practitioner determine what supplementation best suits your needs. Diet will also be a factor as with MTHFR the body cannot process synthetic folate which is in fortified foods such as cereal, nutritional yeast (can get unfortified), breads, rice, pastas, flour, etc., This explains why I always got a headache after I ate fortified nutritional yeast. I switched to unfortified and I don't have the headaches. As mentioned above, there are many chronic conditions linked to MTHFR. Here are a few: Alzheimer's Autism Autoimmune Disorders Breast cancer Chronic Fatigue Down's Syndrome Fibromyalgia Heart Disease IBS (irritable bowel syndrome) Infertility in both men and women Mental disorders such as bipolar and schizophrenia Migraines Multiple Sclerosis (MS) Sensitivity to chemicals Stroke The Great Detoxifier Glutathione is the body's main antioxidant and detoxifier. What happens with MTHFR mutation is it can make you susceptible to disease by lowering your body's ability to make glutathione. Most people with MTHFR have low glutathione levels. With low glutathione levels, you are more sensitive to toxins and chemicals including heavy metals. The good news is you can supplement glutathione in the correct methyl form and change up your diet. More to come on this. With oxidative stress, we are more likely to have premature aging as well. Another reason to be aware of MTHFR and maintain a healthy high folate diet along with supporting supplementation. Testing If you have any of the symptoms above or have a family history with MTHFR mutations I highly recommend testing for both C677T and A1298. Testing can be done through a practitioner. You can go to 23andme and order the test or work with your health practitioner. It's inexpensive and well worth it. Also, testing your levels of glutathione and folate would be beneficial so your practitioner knows where your levels are before recommending supplementation. Supplementation for MTHFR If you are taking a B vitamin, make sure it's methyl-B12, methyl-folate. Taking synthetic forms (folic acid) can be more harmful than good because the body cannot do the conversion. It's essential to make sure that your method delivers the antioxidant efficiently to your cells. One of the B vitamins I recommend from Pure Genomics is their B Complex available on our marketplace. Glutathione is also important but hard to absorb so a liposome form is recommended or get one with a precursor called NAC (N-acetyl-cysteine). Glutathione is important for detoxification as mentioned. Here are a few to consider – Liposomal Glutathione by Pure Encapsulations as a liposome form With any supplement, you can have adverse effects so make sure you work with a knowledgeable practitioner. Diet and Lifestyle Folic Acid vs. Folate While folic acid and folate may be marketed interchangeably, as mentioned earlier, their metabolic effects can be quite different, especially for those with the MTHFR mutation. Folate is the bioavailable, natural form of vitamin B9 found in a variety of plant and animal foods. Folic acid, on the other hand while readily utilized by the body is synthetic. Folate is found in supplements and fortified foods such as cereals and might I add nutritional yeast. The body is more adept at using folate and regulates healthy levels by discarding excess folate in urine. With MTHFR folic acid can be problematic so make sure you purge the folic acid rich foods and supplements. For those who love the flavor of nutritional yeast and use it in vegan recipes there are a few companies who make unfortified versions you can get off amazon. Daily lifestyle activities such as dry brushing (lymphatic circulation) Epsom salt baths, exercise, sauna's (infrared sauna is amazing) and of course a healthy diet rich in natural forms of folate such as: Beans and lentils Leafy green vegetables including raw spinach Asparagus Romaine Lettuce Broccoli Avocado Bright-colored fruits, such as papaya and orange Here are just a few examples of some folate rich foods. As you can see spinach packs a powerful punch of folate as well as papaya and lentils coming in the highest. [2] Source Spinach Asparagus Papaya Orange Lentils Pinto Beans Sunflower Seeds Serving Size 1 Cup 1 Cup 1 papaya 1 orange 1 Cup 1 Cup ¼ Cup Folate 263 mcg 262 mcg 115 mcg 40 mcg 358 mcg 294 mcg 82 mcg DV % 65% 64% 29% 10% 90% 74% 21% Did you know your liver needs glutathione to produce bile in addition to the detoxification process? Look at addressing health issues such as leaky gut, IBS and Inflammation as these can affect absorption and neurotransmitter levels as well as hormones with MTHFR A1298C mutations. MTHFR mutations are tied to higher mental disorders such as anxiety, depression, bipolar and schizophrenia as well as chronic fatigue and fibromyalgia. It's important to find ways to manage the stressors in addition to healing the gut as symptoms can be heightened with MTHFR. Protect the heart with an anti-inflammatory diet rich in omegas, fiber and plants. Omega 3 and COQ10 supplementation is helpful. A good multi is beneficial as long as you get one with B12 (methyl cobalamin) and Folate (methyl tetrahydrofolate) forms. Drug Interactions to consider You should not use any supplements without first talking to your health care provider. For example, folate should not be taken at the same time as the antibiotic tetracycline because it interferes with the absorption and effectiveness of this medication. Folate is necessary if taking medications for birth control, cholesterol or seizures for example as they may lower folic acid levels in the body. Dosage and timing is important to know. Here are some medications to keep in mind: Antacids, H2 blockers, proton pump inhibitors Bile acid sequestrants Carbamazepine Nonsteroidal anti-inflammatory drugs (NSAIDs) Sulfasalazine Triamterene When taken for long periods of time, these medications, as well as other anti-inflammatory and anti-seizure medicines, can increase the body's need for folic acid. Also consider drugs used for cancer, rheumatoid arthritis and psoriasis as those also reduce the folic acid in the body. Supplementing folic acid can help reduce symptoms of these disorders however with cancer, folic acid may interfere with methotrexates effects on treatment. Talk with your practitioner if you are taking any medications. [3] Knowing your DNA make up is important as is knowing your numbers (blood pressure, cholesterol, etc.) so you can keep a handle on your health and do your best to control stress. Getting tested for the MTHFR mutation is worth knowing whether it comes up or not. It can make all the difference in aging and detoxing and give you a peace of mind. Sources: https://draxe.com/mthfr-mutation/ http://doccarnahan.blogspot.com/2013/05/mthfr-gene-mutation-whats-big-deal.html https://www.jillcarnahan.com/2014/02/23/health-tips-for-anyone-with-a-mthfr-gene-mutation/
  3. Will a new treatment enable people with celiac disease to ditch a gluten-free diet? About one in a hundred people in the United States is affected by celiac disease. If you're one of them, you know how hard it can be to maintain a strict gluten-free diet. Everyone's got their horror stories about trying to simply eat a meal, only to have a tiny amount of gluten wreck havoc on their digestive system. There are currently no therapeutics on the market to treat celiac disease, says Sydney Gordon, a scientist at Ab Initio Biotherapeutics. Sure, there are other over-the-counter enzyme treatments, Gordon adds, but most are slow to act, or don't break down enough gluten to prevent a reaction. "There are no other enzymes on the market for celiac disease," said Justin Siegel, the co-founder of PvP Biologics and an assistant professor of chemistry, biochemistry and molecular medicine at UC Davis. "There is nothing that is approved by the FDA for celiac disease. Nothing has made it through clinical trials. There are pills on the market that cause degradation of gluten, but there is no clinical evidence that they are effective." "We wanted to design an enzyme […] a protein that would act as a therapeutic for celiac disease. We came up with a design using a protein modeling tool called FoldIt," said Ingrid Pultz, a co-founder of PvP Biologics. PvP Biologics enzyme therapy works by targeting the exact triggering molecule, the immunogenic epitope, before it gets to the intestine and causes an immune reaction. To do this, PvP Biologics uses kumamolisin, a naturally occurring enzyme that, unlike some other enzymes, can survive the acidity of the stomach. By modifying the amino acid sequence in the original kumamolisin enzyme, researchers were able to specifically target the epitope causing the reaction. If the therapy proves successful, many celiac patients won't have to worry about minute amounts of cross-contamination when eating outside. Those are pretty strong claims. Many people with celiac disease might likely say that it sounds too good to be true. Still, the company is moving in a direction that few others have gone. No word on if or when we might expect to see a finished treatment come to market. For all the company's claims, there is much to work out, and a long, winding road to get FDA approval. Stay tuned to see if the evidence from trials and from potential consumer use supports those claims. Read more at TheAggie.org. Editor's note: We've received a correction on this story from PvP Biologics, makers of KumaMax, which states that their product is designed for accidental gluten ingestion, and not as a replacement for a gluten-free diet in people with celiac disease. Their enzyme could lessen the effects of accidental consumption of small amounts of gluten.
  4. Celiac.com 07/25/2017 - Enzymes are playing an increasing part in both the treatment of celiac disease, and in the manufacture of gluten-free baked goods. DSM recently showcased their new rice-based baker's enzyme, Bakezyme, at the annual meeting of Institute of Food Technologists (IFT) in Las Vegas. The product took DSM two years to develop and perfect, and promises to improve the softness and moistness of gluten-free bread. Bakezyme is so good, says DSM, and leaves gluten-free bread so soft and so moist that it can compete with wheat-based breads in texture. Designed to meet an array of manufacturer needs, Bakezyme is available in five different enzyme classes–amylase, protease, xylanase, glucose oxidase and amyloglucosidase. The version with amylase, an anti-staling enzyme, for example, will retain the softness for at least nine days. Fokke Van den Berg, DSM global business manager for baking says that Bakezyme grew out of DSM's efforts to tackle the two biggest consumer complaints about gluten-free bread, the hardness, and the dryness. While most baker's enzymes are derived from wheat, Bakezyme is made of fermentation-derived microorganisms added to rice flour, making it suitable for people with celiac disease and gluten intolerance. Because the enzymes are deactivated during baking, Bakezyme is regarded as a processing aid and thus is not required to be listed as an ingredient. DSM tested Bakezyme on two types of dough, oat and a mixture of potato and rice, with each requiring a slightly different formulation for similar results. Beyond the slight costs of ensuring that Bakezyme is gluten-free, its overall price is on par other enzyme ingredients, partly because such a small amount is needed. One kilo of Bakezyme is enough to produce 10,000 kilos of bread. The company expects most demand to come from the US and UK as well as other European countries, but the gluten-free trend is also spreading to Brazil, Turkey and Morocco, said Van den Berg. Read more at FoodNavigator.com.
  5. Celiac.com 09/25/2017 - There are currently several efforts underway to develop successful commercial enzyme treatments for celiac disease. Efforts include looking at the digestive enzymes in plants, such as the papaya and star fruits, including such predatory plants, such as the pitcher plant. One focus has been on developing enzymes that can break down gluten before it can trigger an immune reaction. This could prove helpful to many people with celiac disease. One such enzyme under development is Latiglutenase, formerly known as ALV003. Latiglutenase is a new name for an enzyme therapy designed to be taken with meals. The idea is that a person with celiac disease would take an enzyme tablet with a meal. If the meal had mild gluten contamination, the enzyme’s two recombinant proteins would break gluten into fragments that are not toxic to the immune system, thereby preventing exposure, and symptoms. But the stomach is a notoriously difficult environment to work in, so what seems like a simple idea quite a challenge from a science and biology perspective. Seeking to explore the ability of Latiglutinase to improve symptoms, a team of researchers recently set out to test latiglutenase on celiac patients who are seropositive despite following a gluten-free diet. The research team included Jack A. Syage, Joseph A. Murray, Peter H. R. Green and Chaitan Khosla. They are variously affiliated with the Division of Gastroenterology and Hepatology, Mayo Clinic, Rochester USA, the Celiac Disease Center at Columbia University, New York, USA, the Departments of Chemical Engineering and Chemistry, Stanford University, USA, and with ImmunogenX, Newport Beach, USA. "Though the ALV003-1221 trial was inconclusive regarding histologic improvement from latiglutenase, the evidence for symptom benefit, which is more quickly achieved, is quite convincing and clinically relevant," Joseph Murray, MD, of the Mayo Clinic in Rochester, Minn., said in a press release. In these trials, patients with celiac disease who were seropositive despite following a gluten-free diet saw major improvement in symptoms when taking latiglutenase with meals, according to a post hoc analysis of the CeliAction study. The team was really hoping to see histological improvement, but they feel satisfied that this trial shows, says Dr. Murray, that a "therapy to help patients struggling with symptoms due to celiac disease is now within reach." Stay tuned for more on efforts to develop effective enzyme treatments for celiac disease. Read more: Dig Dis Sci. 2017 Doi:10.1007/s10620-017-4687-7.
  6. Celiac.com 10/23/2015 - Just as I finished writing about the failure of current commercial enzymes to effectively degrade gluten, an interesting study on another enzyme suggests that there may be help on the horizon, at least for people without celiac disease. According to the latest press release, in lab conditions, aspergillus niger prolyl endoprotease (AN-PEP) efficiently degrades gluten molecules into non-immunogenic peptides. But so what? If AN-PEP is to be effective in people with celiac disease or gluten-sensitivity, which would seem to be the whole point of an anti-gluten enzyme, it must effectively digest gluten in "non-healthy" subjects. A team of researchers recently set out to assess AN-PEP on gluten degradation in a low and high calorie meal in healthy subjects. The research team included B.N. Salden, V. Monserrat, F.J. Troost, M.J. Bruins, L. Edens, R. Bartholomé, G.R. Haenen, B. Winkens, F. Koning, A.A. Masclee. They are variously affiliated with the Division of Gastroenterology-Hepatology in the Department of Internal Medicine at NUTRIM, Maastricht University Medical Center, Maastricht, the Department of Immunohematology and Blood Transfusion at Leiden University Medical Centre in Leiden, the DSM Biotechnology Centre, Delft, the Department of Pharmacology and Toxicology, CARIM, at Maastricht University in Maastricht, and with the Department of Methodology and Statistics, CAPHRI, Maastricht University Medical Center in Maastricht, all in The Netherlands. The team conducted a randomized, double-blind, placebo-controlled, cross-over study in which 12 healthy volunteers attended to four test days. Each volunteer received a liquid low or high calorie meal (4 g gluten) with AN-PEP or placebo administered into the stomach. Using a triple-lumen catheter the team was able to sample gastric and duodenal aspirates, as polyethylene glycol (PEG)-3350 was continuously infused. Acetaminophen in the meals tracked gastric emptying time. The team used gastric and duodenal samples to calculate 240-min area under the curve (AUC0-240 min ) of α-gliadin concentrations. The team calculated absolute α-gliadin AUC0-240 min using duodenal PEG-3350 concentrations. The teams data showed that AN-PEP lowered α-gliadin concentration AUC0-240 min, compared to placebo, from low and high calorie meals in stomach (low: 35 vs. 389 μg × min/mL; high: 53 vs. 386 μg × min/mL; P < 0.001) and duodenum (low: 7 vs. 168 μg × min/mL; high: 4 vs. 32 μg × min/mL; P < 0.001) and absolute α-gliadin AUC0-240 min in the duodenum from low (2813 vs. 31 952 μg × min; P < 0.001) and high (2553 vs. 13 095 μg × min; P = 0.013) calorie meals. In the placebo group, the high compared to low calorie meal slowed gastric emptying and lowered the duodenal α-gliadin concentration AUC0-240 min (32 vs. 168 μg × min/mL; P = 0.001). These results confirm that AN-PEP significantly enhanced gluten digestion in the stomach of healthy volunteers, while increasing caloric density prolonged gastric residence time of the meal. According to the authors, these results suggest that AN-PEP shows promise as an anti-gluten digestive enzyme for people with celiac disease, but further study is clearly needed. Still, the fact that AN-PEP can effectively break down gluten in the stomach of healthy volunteers is a good start, but it means little if AN-PEP can’t do the same in people with celiac disease, which remains to be seen. Stay tuned for more developments. Source: Aliment Pharmacol Ther. 2015 Aug;42(3):273-85. doi: 10.1111/apt.13266. Epub 2015 Jun 4.
  7. Celiac.com 10/02/2015 - Many people with celiac disease or gluten-intolerance take digestive enzymes, hoping for some protection against accidental gluten-contamination. Post-proline cutting enzymes have been shown to effectively degrade the immunogenic gluten peptides and have been proposed as oral supplements. Several existing digestive enzyme supplements also claim to aid in gluten degradation. However, not all gluten proteins are the same. The gluten proteins that are particularly active in triggering an adverse immune reaction in celiac disease are known as immunogenic 33-mer from α-gliadin and a 26-mer from γ-gliadin. So, how effective are currently available digestive enzyme supplements ineffective in breaking down these specific gliadins that triggers immune reactions in people with celiac disease? A team of researchers recently set out to determine the effectiveness of such existing enzyme supplements in comparison with a well characterized post-proline cutting enzyme, Prolyl EndoPeptidase from Aspergillus niger (AN-PEP). The research team included G.Janssen, C. Christis, Y. Kooy-Winkelaar, L. Edens, D. Smith, P. van Veelen, and F. Koning. They are variously affiliated with the Department of Immunohematology and Blood Transfusion at Leiden University Medical Centre in Leiden, The Netherlands, DSM Food Specialties, Delft, The Netherlands, and DSM Food Specialties in South Bend, Indiana, USA. For their study, the team subjected each of the five commercially available digestive enzyme supplements along with purified digestive enzymes to 1) enzyme assays and 2) mass spectrometric identification. Gluten epitope degradation was monitored by 1) R5 ELISA, 2) mass spectrometric analysis of the degradation products and 3) T cell proliferation assays. Their findings show that, due to the high proline content of gluten molecules, gastrointestinal proteases are unable to fully degrade them leaving large proline-rich gluten fragments intact, including an immunogenic 33-mer from α-gliadin and a 26-mer from γ-gliadin. Basically, none of the currently available digestive enzyme supplements are effective in degrading immunogenic gluten epitopes. This means that these enzymes are not likely to be helpful to people with celiac disease. Share your thoughts in our comments section below. Source: PLoS One. 2015 Jun 1;10(6):e0128065. doi: 10.1371/journal.pone.0128065. eCollection 2015.
  8. Celiac.com 02/07/2008 - Are we close to finding a way for people with gluten intolerance and celiac disease to safely break down and properly digest wheat gluten and protein? An article recently published in the medical journal Gut describes the results of laboratory experiments in which doctors duplicated a human digestive tract and isolated an enzyme that degrades wheat gluten and protein. Moreover, the results show that the enzyme also eliminated the toxic response to the wheat gluten and protein common in folks with gluten intolerance and celiac disease. According to the researchers, if a full-scale trial confirms the results, people with gluten intolerance and celiac disease might be able to safely stray from their strict gluten-free diets on occasion. The enzyme is prolyl endoprotease isolated from Aspergillus niger and shows the power to quickly and effectively break down gluten peptides and proteins in a simulated human digestive tract. The enzyme has a similar pH level to that of the stomach, and remains intact in the stomach’s strongly acidic conditions. The research team, led by Dr. C. Mitea from Leiden University Medical Center in the Netherlands tested the enzyme in a controlled system built to function in way that is nearly identical with the human gastrointestinal tract. According to the report, the enzyme increased the digestion speed of the glutenins and gliadins that are found in white bread, and which people with gluten intolerance and celiac disease cannot properly break down. After 90 minutes, the gluten proteins treated with the enzyme were undetectable, whereas those glutens not treated with the enzyme, remained in the stomach for at least two hours. The research team obtained similar results when they repeated the test on a fast food meal rather than just white bread alone, and showed that the enzyme treated food samples also eliminated adverse T-cell stimulatory activity that occurred in untreated samples. The tests showed that, in the same amount of time that food normally remains in the stomach, the enzyme brought about the total elimination of T-cell stimulatory peptides of gliadins and glutenins. From the test results, the research team concluded that the enzyme is a solid choice for clinical trials to determine if it can eliminate 100% of gluten toxicity. They also noted that the enzyme is readily available in industrial quantities, and thus easy to tailor into a suitable treatment should trials prove fruitful. Gut, Jan 2008; 57: 25 - 32. Editor's Note: This is not a therapy that is designed to allow celiacs to eat gluten on a daily basis. At best it will allow them to not worry about cross-contamination when eating out.
  9. Celiac.com 10/14/2013 - A team of researchers recently set out to assesses the safety and efficacy of Aspergillus niger prolyl endoprotease (AN–PEP) to mitigate the effects of gluten in celiac patients. For their study, the researchers included celiac patients with positive serology and subtotal or total villous atrophy on duodenal biopsies, who follow a strict gluten-free diet (GFD) resulting in normalised antibodies and mucosal healing classified as Marsh 0 or I were included. Prior to this randomized double-blind placebo-controlled pilot study, the team measured complaints, quality-of-life, serum antibodies, immunophenotyping of T-cells and duodenal mucosa immunohistology. They then had patients consume approximately 7 grams of gluten per day as toast, along with AN-PEP for a two week safety phase. The team put subjects through a two week washout phase where they followed their usual gluten-free diets. The team then randomly assigned 14 patients to receive gluten, with either AN-PEP or placebo, for a two week efficacy phase. They also collected patient questionnaires on serum and quality of life during and after the safety, washout and efficacy phase. They conducted duodenal biopsies after both the safety phase and the efficacy phase. Change in histological evaluation according to the modified Marsh classification served as the primary endpoint. In all, 16 adults participated in the study. No serious adverse events occurred during the trial and no patients withdrew during the trial. The average score for the gastrointestinal subcategory of the celiac disease quality (CDQ) was relatively high throughout the study, indicating that AN-PEP was well tolerated. In the efficacy phase, the team saw no significant deterioration in the CDQ scores of patients consuming gluten with placebo or gluten with AN-PEP, nor did they observe any other differences between the groups. During the efficacy phase, neither the placebo nor the AN-PEP group showed significant antibody titers. IgA-EM concentrations remained negative in both groups. The team excluded two patients from entering the efficacy phase because their mucosa showed an increase of two Marsh steps after the safety phase, yet with undetectable serum antibodies. A total of 14 patients were considered histologically stable on gluten with AN-PEP. Also, after the efficacy phase, the team saw no significant deterioration in immunohistological and flow cytometric evaluation in the group consuming placebo compared to the group receiving AN-PEP. Furthermore, in four out of seven patients on placebo, IgA-tTG deposit staining increased after two weeks of gluten intake compared to baseline. In the seven patients receiving AN-PEP, one patient showed increased and one showed decreased IgA-tTG deposits. AN–PEP appears to be well tolerated. However, the primary endpoint was not met due to lack of clinical deterioration upon placebo, impeding an effect of AN–PEP. The research team included Greetje J Tack, Jolanda MW van de Water, Chris J Mulder of the Department of Gastroenterology and Hepatology, VU University Medical Centre in Amsterdam, The Netherlands; Engelina MC Kooy-Winkelaar, Jeroen van Bergen, and Frits Koning of the Department of Immunohematology and Blood Transfusion, Leiden University Medical Centre in Leiden, The Netherlands; Petra Bonnet, B Mary E von Blomberg, and Marco WJ Schreurs from the Department of Pathology, VU University Medical Centre, in Amsterdam, The Netherlands; Anita CE Vreugdenhil, with Department of Paediatrics, University Hospital Maastricht in Maastricht, The Netherlands; and Ilma Korponay-Szabo, with the Department of Paediatrics, University of Debrecen in Hungary, and the Paediatric Research Centre, University of Tampere, in Tampere, Finland. Source: World Journal of Gastroenterology, 10/03/2013
  10. Celiac.com 11/02/2011 - With the rise in celiac disease diagnoses, increasing awareness of gluten-free issues, and an explosion of gluten-free related products, it is no surprise that supplements claiming to break down gluten would find their way onto the market. In fact, a number of supplements currently on the market claim to do just that: to break down gluten after it has been consumed. Are these claims accurate? Are these products in any way helpful for people following a gluten-free diet? Finally, do these supplements offer a safe alternative to a gluten-free diet for people who suffer from celiac disease and/or gluten-sensitivity? For example, GlutenEase, made by Enzymedica Inc., contains a blend of enzymes, including amylase, glucoamylase and dipeptidyl peptidase-4 (DDP-IV) — that are intended to "digest both gluten and casein, a protein found in milk," according to the company. The website for GlutenEase says that the supplement can "support" people who have trouble digesting gluten. However, and most importantly, the site says that GlutenEase is "not formulated" for people with celiac disease. Gluten Defense, made by Enzymatic Therapy Inc., contains a similar blend of enzymes that includes DDP-IV, lactase and amylase. The site for Gluten Defense says the product is "specifically formulated to defend against hidden gluten" that can cause gas, bloating and indigestion. But what does that mean? Does that mean that taking the supplement might offer people with celiac disease some extra protection against accidental gluten contamination? That seems doubtful, and unproven from a scientific standpoint. Unlike GlutenEase, Gluten Defense offers no specific disclaimer for people with celiac disease. There is also no claim that the product is safe, or in any way formulated for people with celiac disease. Dave Barton, whose title is "Director of Education" for Enzymedica, claims that many people who say they have celiac disease see improvement when taking product, and that some even manage to begin eating wheat again. However, Barton is quick to warn consumers that there's "no way to guarantee that it would break down 100% of gluten proteins." But that's the problem isn't it? It would need to break down nearly all of the gluten proteins in order for those proteins to not cause damage to the person with celiac disease. The fact is that these enzyme supplements may break down a few molecules of gluten protein, but no supplement exists that will make it safe for people with celiac disease to eat gluten again. According to Dr. Stefano Guandalini, professor of pediatrics and director of the University of Chicago Celiac Disease Center, "[t]he amount of gluten that these would be able to digest is ridiculously low. For people with celiac disease, these are something to completely avoid." Dr. Peter Green, director of the Columbia University's Celiac Disease Center, agrees that current enzyme supplements would digest only a small percentage of gluten molecules. However, Green adds, the basic concept is sound. Pharmaceutical companies are spending hundreds of millions of dollars to create an enzyme-based drug that would permit people with celiac disease to consume gluten. However, Green points out, the companies wouldn't be spending that money if a successful over-the-counter alternative already existed. Bottom line: Enzymes currently claiming to help break down gluten protein will not permit people with celiac disease to safely consume products made with wheat, rye or barley. Any benefit these enzymes may provide for people with celiac disease is strictly theoretical, and likely minimal at best. A completely gluten-free diet is currently the only proven treatment for celiac disease. Talk with your doctor before making any changes to your gluten-free diet for celiac disease treatment. Source: http://www.latimes.com/health/la-he-skeptic-gluten-supplements-20110926,0,2998711.story
  11. Celiac.com 09/12/2011 - Exogenous enzymes are enzymes that are created outside of the body. Doctors use exogenous enzymes, usually orally, to treat several diseases, such as pancreatic insufficiency and lactose intolerance. Because these enzymes are protein-based, they can be inactivated and/or digested in the gastrointestinal (GI) tract. A research team recently established a convenient fluorescence-based test to measure the activity of therapeutic enzymes live and in real time in the GI tract. The research team included Gregor Fuhrmann and Jean-Christophe Leroux. They are affiliated with the Department of Chemistry and Applied Biosciences, Institute of Pharmaceutical Sciences in Zurich, Switzerland. To establish proof of their principle, the team applied their assay to proline-specific endopeptidases (PEPs), a group of enzymes recently proposed as adjuvant therapy for celiac disease, which is a very common immunogenetic enteropathy. To do so, they took a short PEP-specific peptide sequence from larger immunotoxic sequences of gluten. They then labeled each sequence with a fluorescent dye and a corresponding quencher. Once the enzyme sequence split, they dequenched the fluorescence emission and then used an live imaging system to detect the result. The team then evaluated PEPs originating from Flavobacterium meningosepticum (FM) and Myxococcus xanthus (MX) after oral administration in rats. While MX PEP could not split the peptide in the stomach, FM PEP showed significant gastric activity reaching 40–60% of the maximal live signal intensity. However, both enzymes produced similar fluorescence signals in the small intestine. Using an antacid significantly enhanced MX PEP’s gastric activity due to increased pH and/or inhibition of stomach proteases. By using this simple method, the team was able to observe differences in the live performance of PEPs, which could not be identified under laboratory conditions. This imaging method could be used for live study other oral enzymes and may prove useful in improving current treatments. Source: PNAS 108:9032-9037. DOI:10.1073/pnas.1100285108
  12. Celiac.com 06/30/2010 - Presently, the only proven treatment for celiac disease is a lifelong gluten-free diet. As part of a gluten-free diet, people with celiac disease are encouraged to avoid consuming foods containing rye, along with avoiding wheat and barley. However, there is surprisingly little evidence to document the adverse effects of rye in cases of celiac disease. To address this deficiency, a team of clinicians set out to determine conclusively whether rye should be excluded from the celiac diet. The team included S. M. Stenman, K. Lindfors, J. I. Venäläinen, A. Hautala, P. T. Männistö, J. A. Garcia-Horsman, A. Kaukovirta-Norja, S. Auriola, T. Mauriala, M. Mäki, and K. Kaukinen They are affiliated variously with the Department of Pediatrics, and the Pediatric Research Center of the Medical School University of Tampere, the Department of Gastroenterology and Alimentary Tract Surgery at Tampere University Hospital, the Department of Pharmacology and Toxicology, the Department of Pharmaceutical Chemistry at the University of Kuopio, the Division of Pharmacology and Toxicology, the Division of Pharmaceutical Chemistry at the University of Helsinki, and Technical Research Centre of Finland. The goal of the team was to determine whether rye secalin triggers toxic reactions in vitro in intestinal epithelial cell models to the same degree as wheat gliadin. Moreover, they examined whether the harmful effects of secalin can be reduced by germinating cereal enzymes from oat, wheat and barley to hydrolyze secalin into short fragments as a pretreatment. The data showed that secalin did trigger toxic reactions in intestinal Caco-2 epithelial cells in a similar manner to gliadin. Secalin triggered epithelial cell layer permeability, tight junctional protein occludin and ZO-1 distortion, and actin reorganization. High-performance liquid chromatography and mass spectroscopy (HPLC-MS), showed that germinating barley enzymes best degraded the secalin and gliadin peptides. Further in vitro analysis showed that germinating barley enzyme pretreatment ameliorated all toxic secalin-triggered reactions. From these results, the team concludes that germinating enzymes from barley offer efficient degradation of rye secalin. In future, these enzymes might be utilized as a novel medical treatment for celiac disease or in food processing in order to develop high-quality celiac-safe food products. Such enzyme treatments might pave the way for either new treatments for celiac disease, or, new methods of processing rye for production of new, celiac-safe foods. SOURCE: Clinical & Experimental Immunology DOI:10.1111/j.1365-2249.2010.04119.x
  13. Celiac.com 06/18/2010 - One of the conditions associated with celiac disease is called exocrine pancreatic insufficiency. A previous study showed that exocrine pancreatic insufficiency is the trigger for about one in three (20/66) cases of current or persistent diarrhea in adults with celiac disease. Of these 20 patients, 19 showed initial improvement with pancreatic supplementation. However, at this point, there are no longitudinal studies on exocrine pancreatic insufficiency in the medical literature. A research team set out to rectify that by conducting their own longitudinal study. The team included Kate E. Evans, John S. Leeds, Stephen Morley, and David S. Sanders. Over the next four years, the team conducted prospective follow-up checks on the 20 patients who received therapy for exocrine pancreatic insufficiency. The team assessed gastrointestinal symptoms, dietary adherence, celiac antibody status, and dose of enzyme supplementation. They repeated titters for fecal elastase-1 (Fel-1) to reassess exocrine pancreatic function. The team was able to review 19 of the 20 patients; one patient had died. The group averaged 59.7 years of age. Seven subjects were male. On average, patients suffered from celiac disease for 13.2 years. Eleven out of nineteen patients continued on enzyme supplementation, with average doses of 45,000 units of lipase per day. Only one of the eleven patients reported no reduction in symptoms, while eight of the 19 patients had discontinued the supplements after their diarrhea abated. The entire group showed a substantial increase in Fel-1 levels over time, with median values of 90 lg/g at zero months, 212 lg/g at six months, and 365 lg/g at follow-up of 45–66 months (p/0.0001). Fecal elastase-1 is helpful in spotting exocrine pancreatic insufficiency in adult celiac patients with diarrhea. Results of the team's longitudinal survey indicate that that patients with celiac disease can end pancreatic enzyme supplementation as symptoms improve. Source: Dig Dis Sci. DOI 10.1007/s10620-010-1261-y
  14. J Pharmacol Exp Ther. 2004 May 13 Piper JL, Gray GM, Khosla C. Stanford University. Celiac.com 11/28/2004 - A study by researchers at Stanford University looked at the ability of Prolyl endopeptidase (PEP)--a specific type of enzyme--to break down gliadin peptides in a living organism--rats. In an effort to determine whether a resistance to the break down of proteins by proteases enzymes is the cause of toxicity of the Pro- and Gln-rich peptides, the scientists analyzed the digestive resistance of a panel of alpha and gamma-gliadin peptides that are believed to induce gluten toxicity--all of which happen to be very resistant to gastric and pancreatic protease digestion--but can be broken down by intestinal brush border peptidases. The researchers determined that supplementation of PEP substantially reduced the concentrations of these peptides, and they determined a pharmacologically useful PEP dosage. According to the researchers: "This data verifies and extends our earlier proposal that gliadin peptides, while resistant to proteolysis, can be processed efficiently by PEP supplementation. Indeed, PEP may be able to treat Celiac Sprue by reducing or eliminating such peptides from the intestine."
  15. Celiac.com 04/10/2009 - According to the latest findings by a Norwegian research team, the inner workings of a particular enzymatic reaction is helping scientists figure out how celiac disease develops. In the latest issue of the Journal of Proteome Research, doctors Siri Dørum, Burkhard Fleckenstein, and associates at Norway’s University of Oslo and Rikshospitalet University Hospital describe how they used a quantitative MS method to chart a significant association between the amount of deamidation and the rate at which various epitopes are recognized by T cells of people with celiac disease. The team set out to determine whether the rate of TG2 deamidation correlates with T cell recognition of gluten peptide epitopes. Celiac disease is a common digestive disorder, in which people suffer from an adverse reaction to gliadin proteins in the gluten of wheat, barley, and rye. When people with celiac disease eat gluten, an adverse immune reaction occurs, in which the intestinal villi, the finger-like projections that line the small intestine and serve to absorb nutrients, suffer damage and eventually flatten and disappear. Currently, the only treatment is the adoption of a gluten-free diet that eliminates exposure to the proteins that trigger the immune response. In most cases, the gluten-free diet heals the intestinal damage. So, how does gluten exposure cause this adverse immune system reaction? Much of this process remains a mystery, but there appears to be a strong genetic component. It is known that most people with celiac disease display the human leukocyte antigen (HLA) molecules DQ2 or DQ8, which function as receptors on antigen-presenting cells. The standard method of measuring deamidation is to tie the transglutaminase activity to a secondary enzymatic reaction, which gives off ammonium. But this method is not direct, and if there are multiple peptides in a mixture, which may be highly complex, one can only assess the total production of ammonium. By contrast, the MS method allows the detection of changes on each peptide, and allows the locations of those modifications to be pinpointed within each peptide. The team achieved their results by measuring the centroid masses of the peptides’ isotopic envelopes before TG2 treatment, and comparing the results to the values obtained after TG2 treatment. Depending on the sequence context, the glutamine residues were shown to influence the extent of residual deamidation by TG2. Additionally, they team revealed that peptide length also plays a key role in the process—the longer the given gliadin peptide, the more likely it is to have deamidated glutamines. The team examined an array of gluten peptides with known epitopes, both individually and in mixture, to assess the degree of deamidation. A 33-mer, shorter α-gliadin peptides, and one peptide from γ-gliadin all showed rapid deamidation. The rest of the peptides showed only partial deamidation, even after a long period of incubation. They observed that the frequency of the T cell response in celiac disease patients seems to be tied to the rate of peptide deamidation. T cells from nearly every patient recognized the 33-mer and the α-gliadin peptide, which also served as good TG2 substrates. In comparison, the glutamines of most γ-gliadin peptides were deamidated less often and were recognized less frequently by patient T cells. However, one γ-gliadin peptide showed itself to be an exception. The γ-II epitope functions as an excellent substrate for TG2, but is poorly recognized by T cells. Another factor may be proteolytic stability, as it is understood that the γ-II epitope is part of a gluten fragment that is less stable than the 33-mer. By analyzing gluten peptides using MS, researchers were able to figure out whether the rate of glutamine deamidation by TG2 impacts the recognition of these peptides by the immune systems of those with celiac disease. J. Proteome Res., 2009, 8 (4), pp 1748–1755
  16. Enzyme Quickly Breaks Down Wheat Protein Celiac.com 05/23/2007 - The results of a study recently published in the journal Gut suggest that the enzyme prolyl endoprotease from Aspergillus niger (AN-PEP) taken along with meals might allow patients with celiac disease to safely consume gluten on occasion. The negative effects of celiac disease are due in large part to an immune response to gluten. Because proline-rich gluten proteins resist the digestive enzymes of the gastro-intestinal tract, they are very likely suspects in the generation of this immune response. A team of doctors in the Netherlands set out to assess the abilities of a post-proline cutting enzyme, prolyl endoprotease from Aspergillus niger (AN-PEP) in breaking down gluten. The research team was made up of doctors Cristina Mitea (1), Robert Havenaar (2), Jan Wouter Drijfhout (1), Luppo Edens (3), Liesbeth Dekking (1)* and Frits Koning (1). The study was not performed on actual celiac patients, but used a dynamic system that mimics the human gastrointestinal tract (TIM system). Using the TIM system, the team performed two experiments. The first used the TIM-system to process a slice of bread with and without the presence of AN-PEP. The second experiment used the TIM-system to process standard fast food items, again both with and without the presence of AN-PEP. Samples of the digesting food were taken from the TIM systems stomach, duodenum, jejunum and ileum compartments from zero to four hours after the beginning of the experiment. These samples were evaluated for levels of immunogenic peptides from gliadins and glutenins by monoclonal antibody based competition assays, Western blot analysis and proliferation T-cell assays. Results of both experiments showed that AN-PEP broke down gluten in the stomach so effectively that almost no gluten reached the duodenum compartment. Because these results show that AN-PEP is capable of speeding the breakdown of gluten in a gastrointestinal system that closely mimics live digestion, the team concluded that AN-PEP might offer celiac patients an opportunity to stray from their strict gluten free diets from time to time. Participating Institutions: 1 Dept of Immunohematology and Blood Transfusion, Leiden University Medical Center, Leiden, Netherlands. 2 TNO Quality of Life, Zeist, Netherlands 3 DSM Food Specialties, Delft, Netherlands Gut. Published Online First: 9 May 2007. doi:10.1136/gut.2006.111609 health writer who lives in San Francisco and is a frequent author of articles for Celiac.com.
  17. The following was taken from AUTISM 95: The following was written about a study: to determine whether children with autism and known food/chemical intolerance have a deficiency of phenol-sulphotransferase-P enzyme and/or a low capacity to oxidize sulfur compounds. On the results obtained so far, all 18 children have a low enzyme level, and some have a low capacity to oxidize sulfur compounds. This enzyme metabolizes phenols and amines. Therefore, with a reduced level, these children will be unable to fully metabolize foods and chemicals which contain phenols (and amines)... ...The majority of children in this category ... have allergy to or intolerance of many foods/chemicals, the main offenders being wheat, cows milk, and salicylates. Their family histories show asthma, eczema, migraines, hay fever, plus many other allergy-related conditions...Their siblings display learning difficulties, dyslexia, etc..... In autism and other disorders we suspect a peptidase deficiency so that proteins are not broken down into individual amino acids and these short, biologically active chains (peptides) exist in appreciable quantities. Even in the normal gut there will be some of these substances but they are not normally a problem. If the gut wall is leaky (celiac disease or lack of sulfur transferase, etc) these compounds will get into the bloodstream. Even then there should be no serious problem unless they enter the blood... ...The brain is protected by the blood brain barrier (BBB) which is partly physical and partly chemical in nature. Thus this would keep peptides out unless there are huge quantities circulating. So when the intestinal wall is not healthy and the brain is vulnerable, the brain is affected directly. Learning disabilities, behavioral problems, and even extremes such as schizophrenic behavior can result. The three things which happen are: Not Enough Enzymes To Fully Digest Particular Protein Chains A Breachable Intestinal Wall A Vulnerable Brain
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