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Found 6 results

  1. Celiac.com 03/21/2014 - According to the National Foundation for Celiac Awareness, the burden of celiac disease can cost an extra $1,000 to $2,500 per year. However, many people who eat gluten-free diets as treatment for celiac disease or other medical conditions are eligible for tax breaks. Those who do eat gluten-free due to medical conditions will be happy to learn that both the Internal Revenue Service and the Canada Revenue Agency list gluten-free food as an eligible medical expense. That means that filers may be eligible for tax relief for gluten-free-related food expenses. For example, according to the Canada Revenue Agency website, celiac disease suffers are "entitled to claim the incremental costs associated with the purchase of gluten-free products as a medical expense." That means Canadians with celiac disease can claim the difference between the cost of their gluten-free food and the cost of comparable regular food. However, there are a few hoops to jump through. To claim the credit, Canadian taxpayers need a doctor's letter confirming celiac disease; a receipt for every item claimed; and a summary for each item calculating the cost differential for gluten-free products. U.S. residents can deduct the extra cost for gluten-free foods and goods purchased to meet celiac dietary needs. Shipping and delivery costs for those gluten-free products can also be deducted. Also, for any special trip to purchase gluten-free foods, the cost of transportation to and from the store is deductible, including mileage, tolls and parking fees. The vehicle deduction for trips during 2013 is 24 cents per mile. To claim these deductions, taxpayers first need an official, written celiac diagnosis from a doctor. A copy of this diagnosis must be submitted with other completed tax forms. Taxpayers will then complete form 1040 schedule A for medical deductions. For reference taxpayers may cite: IRS Publication 502; Revenue Rulings: 55-261, 76-80, 2002-19 and 67 TC 481; Cohen 38 TC 387; Flemming TC MEMO 1980 583; and Van Kalb TC MEMO 1978 366 This must be supported with copies of receipts for all gluten-free purchases, along with lists of prices for gluten-free food and regular counterparts being claimed. The difference between those prices is tax-deductible. For example, if a pound of wheat flour costs $0.60 and a pound of rice flour costs $3.40, then you may deduct $2.80 for each pound of rice flour you are claiming for that tax year. Remember, some specialty products like xanthan gum and sorghum flour are fully tax-deductible as they have no "regular" counterpart but are purchased to meet your dietary needs. Of course, for specific advice, contact an accountant. Sources: CAFinance.com CeliacCentral.org Celiac.com.
  2. 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.
  3. 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
  4. I know gluten is a problem for me, but I tested negative for celiac with 2 blood tests. I'm awaiting the results of an intestinal biopsy. One symptom I have that I attribute to the effects of gluten is bad teeth (eroding enamel and teeth that break easily- 2 in the past 11 months). Did anyone experience an improvement in dental health after going gluten free, or has the damage already een done?
  5. By Jessica Mahood , M.S. Bacteriology Celiac.com 09/28/2004 - A very good question: what is gliadin and why does it survive a bath in hot oil? I am a little hesitant to answer because I am not a protein chemist who specializes in such things. However, I was a bacteriologist with many years of exposure to biochemical concepts, so Im probably better equipped than most to give this a go. First of all, a protein primer: As someone mentioned, proteins are made up of building blocks. We generally call these amino acids. Sometimes amino acids are represented in the scientific literature as a single letter--you will see something like PQQLL (pay attention to this because it will come up again later). Each of those letters stands for an amino acid that is linked to the next. So, imagine the amino acids to be beads in a necklace. This configuration--the beads of amino acids connected in the necklace--is called the primary structure. Now, imagine this necklace to be twisted around itself in some fashion. This is generally known as the secondary structure of the protein and often looks like a helix. Next, take that twisted necklace and bend it around into a 3-D blob. This is known as the tertiary structure. If you were to take several different necklaces compressed into this tertiary structure and combine them, you would have a quaternary structure. So, there are four basic levels of protein structure, primary through quaternary. Of course, the actual chemistry is a bit more complicated, because many amino acids have a chemical charge to them that can influence how they respond to their neighbors, or to the outside environment. Think of a magnet--like repels like, attracts opposite. If they are attracted or repelled, its going to effect the ultimate structure of that protein. Amino acids, as molecules, are also different sizes. One amino acid may be like a small bead that fits easily between the others, while the next amino acid could be huge and practically hanging off of the necklace. Imagine this as a lump in our necklace that prohibits it from fitting neatly against another necklace in our blob. There is also the fact that not all proteins have all four of the levels of structure. Some proteins simply exist as a secondary structure or tertiary structure. So, there are many different types of protein structures in nature. Often times, these depend on the job of the protein. Hopefully I havent thoroughly confused you by now. Suffice it to say that there are many factors involved in determining the properties of a certain protein. So much so that there are actually a set series of tests that scientists use to classify proteins. It is a very complex discipline. Now, back to your original question. Proteins cannot be killed, per se, as they are not alive. HOWEVER, they can be damaged or destroyed. This is a process that is called denaturation. Denaturation can be irreversible, such as when you burn something to a crisp. Its as if you melted the strand of that necklace and all of the shapes that it made were lost. Denaturation can also be somewhat temporary. You denature your hair, to some extent, when you use a curling iron. You are slightly unraveling a higher structure of the hair protein, but it can be righted over time (unless the curling iron is too hot!). The ease with which a protein denatures depends on many things. Think back to our necklace. If we have, say, five necklaces clustered together to form a single protein, it would probably take a lot of chemical disruption to fully destroy that protein. However, if we had one tiny necklace twisted up slightly, it would be a lot less work to break it apart. There are many other factors involved in this--the size and charge of the beads, for example. Gliadin is a fragment of the protein gluten. Gliadin is NOT a single amino acid. Gliadin is simply a subset of a larger protein. Think of it as one necklace within a jumble of many. According to a Stanford research website (http://www.friedli.com/research/PhD/Predict/discuss.html), gluten has the basic structure of: MKTFLILALLAIVATTATTAVRVPVPQLQPQNPSQQQPQ EQVPLVQQQQFLGQQQPFPPQQPYPQPQPFPSQQPYLQLQ PFLQPQLPYSQPQPFRPQQPYPQPQPQYSQPQQPISQQQQ QQQQQQQQQQQQQQQIIQQILQQQLIPCMDVVLQQHNIV HGKSQVLQQSTYQLLQELCCQHLWQIPEQSQCQAIHNVVH AIILHQQQKQQQQPSSQVSFQQPLQQYPLGQGSFRPSQQ NPQAQGSVQPQQLPQFEEIRNLARK What do these letters mean? Again, they are amino acids. Each one of those letters stands for an amino acid. Its like a code. If the same letter is used, the same amino acid is in those two parts. Within that larger sequence, you see: RPQQPYPQPQPQ This smaller list of letters is the amino acid code for gliadin. So just for a start, in denaturing our gliadin, we have to destroy all of the rest of the gluten protein that is around it. The next issue is that this sequence contains the letter Q several times. This letter Q represents the amino acid glutamine. This is probably what the person meant when they said that gliadin was an amino acid. They were most likely thinking of glutamine. In any case, as far as amino acids go, glutamine is fairly large and pretty hearty. At this point in time, go to the following website: http://www.chemie.fu-berlin.de/chemistry/bio/aminoacid/glutamin_en.html Look at the picture of glutamine next to the name at the top--it looks like a couple of groups of letters connected by black lines. If you look to the far left, you see the letters H2N. A certain chemical process in the body changes that H2N into a different chemical group. This is called deamidation, and you hear about it a lot in reference to the Celiac response. It is the deamidated protein within the gliadin fragment of the gluten protein that is believed to be the big trigger for the antibody response that causes damage. What a mouthful, eh? Back to gliadin and hot oil, the original question. Okay, so now we know that proteins are pretty complicated. They can have big structures and lots of chemical interactions. Gluten is such a protein. The gliadin fragment of the gluten protein is tough to get to. You must also destroy the properties of the amino acids in the gliadin fragment to truly nullify the immune-irritating properties of gliadin to Celiacs. So, for various chemical reasons, gliadin is not easy to denature. According to that Stanford website (http://www.friedli.com/research/PhD/chapter8.html), gliadin is tough stuff. Many changes made to the protein are reversible. Researchers are still exploring the properties of gliadin and trying to find a way to use the molecules interactions to stop the Celiac response. It gives me a hope. For now, we have to resign ourselves to being suspicious of those soupy vats of oil in the back of bars and restaurants.
  6. Celiac.com 09/30/2010 - New York arena football kicker, Craig Pinto, will attempt to set a world record for most field goals kicked within a twelve hour period, and to raise money and awareness for celiac disease. Pinto's effort will get underway on October 10, 2010, when he begins kicking field goals for 12 straight hours. In addition to raising money and awareness for celiac disease, a condition in which people who consume proteins found in wheat, rye, or barley suffer damage to their digestive tracts, Pinto, who has lived with celiac disease for more than a decade hopes to show that people with celiac disease can remain physically active, and even excel in their chosen activities. “With something that has affected me, and is so close to my heart, it only makes sense to utilize things I love – kicking and football – to raise money and awareness for my other passion,” says Craig. “And that is spreading the word and educating people about Celiac Disease.” Each field goal must be kicked from at least forty yards away from the goal post, and will be judged by official referees to make sure each kick meets specific record breaking criteria. All proceeds will benefit the Celiac Disease Center at Columbia University. For more information or to make a donation visit www.kicking4celiac.com. Bethpage High School 10 Cherry Avenue Bethpage, New York 11714 October 10th, 2010 7:30 a.m.-7:30 p.m.