A research collaboration between scientists in France, the US and Switzerland has discovered that a molecule called ‘elafin’, which is present in the intestine of non-coeliac individuals, is significantly decreased in patients with coeliac disease. The research was published in the April edition of The American Journal of Gastroenterology.
People with coeliac disease are known to lack the digestive enzymes needed to digest gluten properly. All peptides that are not effectively digested induce inflammation and this inflammation is further amplified by an enzyme called tissue transglutaminase 2.
Researchers found that the elafin molecule interacts with the transglutaminase 2 enzyme, decreasing the enzymatic reaction that would otherwise increase the toxicity of gluten-derived peptides. The same team developed a probiotic using a lactic bacterium strain (Lactococcus lactis) which allows delivery of elafin into the digestive system. In studies using gluten intolerant mice, the researchers found this probiotic protected the intestinal lining of the upper gut that was usually damaged by consumption of gluten.
The study authors maintain their results raise the possibility of using elafin as a new therapy to protect patients from unintentional gluten consumed within a gluten-free diet. This would add flexibility to a restrictive lifelong diet, increase patients’ quality of life and potentially accelerate the healing of coeliac lesions.
The next step of the research program will seek to define the mechanisms underlying the positive effects of elafin in coeliac disease and identification of bacteria that naturally produce proteins with anti-inflammatory properties similar to elafin.
Reference: Galipeau et al. 2014. The American Journal of Gastroenterology Vol. 109 Pp. 748-756. Doi:10.1038/ajg.2014.48