I told him I thought I was sick from emotional distress from the divorce (which he said does trigger the symptoms) Anyway they found H Pylori virus and I took heavy antibiotics. Those lead to the IBS getting super bad. (killed the good as well as the bad bacteria)

I have learned so much more all on my own than any doctor has taught me! For me it is ALL tied together. My stomach, the gluten, the migraines, the reflux........all tied together and working against each other.

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Here's an interesting article from the American Journal of Epidemiology in 2013: RE: Decreased Risk of Celiac Disease in Patients with Helicobacter Pylori Colonization. Interesting end of the Medscape article and study: "Additional studies may be warranted for confirmation and to examine whether H. pylori could modulate gluten immunogenicity among genetically susceptible hosts."

The article is quite technical because it is for health professionals (I have a physio background) - you could bring it to your doc's attn. http://www.medscape.com/viewarticle/817671_4

"Acknowledgments:

B.L. was supported by the National Center for Advancing Translational Sciences, National Institutes of Health (grant KL2 TR000081). M.J.B. was supported by the National Institutes of Health (grant R01 GM63270) and the Diane Belfer Program in Human Microbial Ecology. J.F.L. was supported by Örebro University Hospital, Karolinska Institutet, the Swedish Society of Medicine, the Swedish Research Council–Medicine (grant 522-2A09-195), and the Swedish Celiac Society.

Selected findings from this study were presented at the Digestive Disease Week conference in Orlando, Florida, on May 18, 2013. "

It i also possible to have a biopsy come back inconclusive/negative even though you may still have coeliac. My daughter ended up having genetic testing - apparently it is the 'new thing' in coeliac testing. There are markers in your genes which indicate the likelihood of you having the disease. My daughters biopsies both came back inconclusive, as did her genetic testing (she only had one of the predisposition genes, not both) so she is eating gluten and waiting until she gets older/ more poorly before they do another biopsy.

Ask your doc for the genetic test if you still think you may be coeliac but have negative blood tests.

"Celiac disease is caused by an interaction between the celiac disease genes and environment. Strong evidence shows that in order to develop celiac disease, a person must have one or both of two genes known as HLA-DQ2 and HLA-DQ8. The major environmental factor, of course, is gluten ingestion. Gluten proteins interact with the celiac disease genes to trigger an abnormal immune response that damages the lining of the small intestine.

More than 97% of patients with celiac disease have at least one of the two genes. Most patients (more than 90%) carry the DQ2 gene. Fewer than 10% carry the DQ8 gene. In the near future, researchers will likely discover additional genes that predispose an individual to celiac disease. "
Good luck.

New study (on Medscape - health professionals' continuing ed website)
'Novel Role of the Serine Protease Inhibitor Elafin in Gluten-related Disorders'
Am J Gastroenterol. 2014;109(5):748-756.

Discussion

CD is one of the most common gastrointestinal diseases, affecting about 1% of the Caucasian population, and its incidence has substantially risen in the past two decades.[34,35] The only treatment is a life-long adherence to a GFD, which is costly and difficult to follow, leading to high nonadherence rates.[6] In CD, gluten-derived peptides are recognized by HLA-DQ2 or HLA-DQ8 heterodimers on antigen-presenting cells, which trigger a proinflammatory gluten-specific T-cell response.[36] Through the process of deamidation, TG-2 activity has an important role by introducing negatively charged residues on gluten peptides. This enhances recognition of these gluten peptides by the HLA-DQ2 or −DQ8 molecules, which are efficiently recognized by T cells.[36,37] However, the factors that drive TG-2 activation in patients with CD are not completely understood.[37,38]

Elafin is a potent endogenous human serine protease inhibitor, and its levels have been found to be reduced in the colon of patients with inflammatory bowel disease (IBD).[15,17] In this study, we show that patients with active CD also have reduced elafin expression within the small intestinal epithelium compared with patients in whom CD was excluded. After 1 year of GFD, elafin expression was somewhat higher than in active CD patients, but was not statistically different from nonceliac controls. The reduced elafin expression in patients with active CD may reflect the presence of enteropathy, and its loss may contribute to enhanced inflammation in CD. In fact, expression of other enzymes in the small intestine, such as cytochrome P450, CYP3A, was found to correlate with the degree of enteropathy, raising the possibility of using these markers as an indication of villous health.[39,40] Reduced expression of elafin in patients with active CD may reflect activity of inflammation or mucosal damage in the small intestine, similar to what has been described in the colon of patients with IBD.[15,16,17]

We then hypothesized that elafin may have a role in gluten-related disorders and tested the interaction of elafin with human TG-2, the enzyme that catalyzes the deamidation of gluten peptides enhancing T-cell recognition.[36] Indeed, elafin has recently been identified as a substrate for the cross-linking activity of tissue transglutaminase.[19,41,42] Our in vitro results demonstrate that the addition of elafin inhibited the deamidation of the digestion-resistant 33-mer gliadin peptide, which is one of the potential triggers of the adaptive immune response in CD.[43] The comparison of elafin to tridegin, a known transglutaminase inhibitor, revealed that elafin moderately inhibits TG-2. These data support that elafin interacts with TG-2, raising the possibility that in addition to correlating with mucosal damage a reduction of elafin in active CD could have a pathogenic role. TG-2 has important roles in tissue homeostasis and wound healing.[21,44] Thus, the moderate inhibition and small intestinal delivery of elafin could constitute an advantage over systemic, complete, and irreversible inhibition, particularly when combined with other potential beneficial effects of elafin. Our in vitro results point at an exciting novel role and specific mechanism of action of elafin in CD that should be further explored.

Elafin has been shown to have anti-inflammatory and barrier-modulating properties in models of respiratory, cardiovascular, and colonic inflammation.[17,32,41,45] We explored whether elafin administration affected these parameters in the small intestine using a model of gluten sensitivity. We used a validated delivery method that exploits a food-grade strain of L. lactis, to ensure administration of elafin to the gastrointestinal tract in mice.[17,32] Although the quantification of elafin delivered to the intestine was not determined, using GFP-tagged Ll-WT and Ll-E, we have previously demonstrated effective delivery of L. lactis and elafin to the gastrointestinal tract. Elafin was found to cluster around L.lactis, but was also detected at sites remote from the GFP-tagged L. lactis, suggesting that elafin is secreted in the mucosa in situ.[17] We found that Ll-E reduced intraepithelial lymphocytosis and restored barrier function in gliadin-sensitized mice. We showed that treatment with Ll-E normalized 51Cr-EDTA flux and conductance in the small intestine, suggesting that Ll-E protects the paracellular pathway in the small intestine. Furthermore, increased permeability after gliadin challenge was accompanied by a reduction in ZO-1 protein expression, and Ll-E therapy preserved ZO-1 protein distribution in sensitized mice. Overall, our results suggest that there are beneficial effects of Ll-E in this model of gluten-induced small intestinal dysfunction that involve immunomodulatory effects and regulation of barrier and tight-junction function. This is consistent with previous reports on the effect of elafin in the colon using animal models of colitis.[14,17,32] Proteolytic imbalances have been described in patients with irritable bowel syndrome, IBD, and in animal models of experimental colitis.[17,32] However, we found no differences in trypsin or elastase-like activity between gliadin-sensitized and control mice. In addition, treatment with Ll-E had no effect on small intestinal protease levels. Our findings highlight a difference in the mechanisms of action of elafin in gluten intolerance compared with colitis, which does not involve correction of elastolytic or trypsin activity imbalance in the small intestine.

Although the NOD/DQ8 mouse model does not develop severe atrophy that is characteristic of classical CD, sensitization and challenge induce moderate inflammation.[27] It will be important to test the effect of elafin, as well as other potential therapies for CD, in a variety of models of gluten sensitivity that express different pathological characteristics and underlying mechanisms, such as IL-15-driven models of CD.[46]

In conclusion, the reduced small intestinal elafin expression in patients with active CD, coupled to the finding that elafin may compete with gliadin peptides and reduce their deamidation, raise the possibility that loss of this protease inhibitor contributes to CD pathogenesis. The results in the animal model of gluten sensitivity suggest that mucosal delivery of elafin restores small intestinal barrier function and inflammation, likely through preservation of tight-junction function and anti-inflammatory effects in the small intestine. Owing to the combination of specific and nonspecific beneficial effects of elafin in our study, we propose that its replacement could have potential as adjuvant therapy in gluten-related disorders.


RE: Mucosal delivery of elafin via Lactobacillus lactis

Liana