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    Celiac Disease: New Hope for a Pill Treatment?


    WebMD News from HealthDay

    By Barbara Bronson Gray

    HealthDay Reporter

    FRIDAY, Feb. 8 (HealthDay News) -- For people with celiac disease, everyday foods such as bread, pizza crust and muffins are potential enemies. But scientists anticipate that some day a simple pill could help prevent the digestive upsets caused by ingesting the gluten in wheat, rye or barley products.

    The only current treatment for celiac disease is a gluten-free diet. A new study, however, offers some potential for hope. Researchers have re-engineered a naturally occurring enzyme, kumamolisin-As, to break down gluten in the stomach into much smaller protein pieces, called peptides. They say these are less likely to trigger the autoimmune response that can create a wide range of painful and irritating symptoms.

    The re-engineered enzyme, named KumaMax, appears to be highly effective, at least in a test tube. It dismantled more than 95 percent of a gluten peptide that is thought to cause celiac disease, according to the study, which was published recently in the Journal of the American Chemical Society.

    Ideally, the team could develop the enzyme into a food additive such as the gas remedies Beano or Gas-X and offer it without a prescription, said lead study author Justin Siegel, assistant professor of chemistry and biochemistry at the University of California, Davis. But this could take a few years to develop. If the researchers opt to make a prescription drug, the process of clinical trials and obtaining U.S. Food and Drug Administration approval could take a decade or more, he said.

    An enzyme is a protein that performs a chemical reaction. Proteins are the workhorses in every cell of every living thing, and their function is defined by their shape and structure.

    In this case, the researchers re-engineered the natural enzyme to recognize the peptide that triggers celiac disease and modified the protein in the laboratory so it would survive the acidic stomach environment. "We did the engineering to change the genes and sent that into standard microorganisms to create the protein," Siegel said.

    The next step is to show that the enzyme is not toxic and functions as designed in animals. "It shouldn't be toxic; it's just a protein you're eating," Siegel said.

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