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Today marks International Celiac Day, a time to raise awareness about celiac disease, a chronic autoimmune condition affecting approximately one percent of the global population. Celiac disease is triggered by the consumption of gluten, a protein found in wheat, barley, rye, and some oats, leading to severe intestinal damage if left untreated. For individuals with this condition, a strict gluten-free diet is essential to avoid health complications.
A recent study conducted by Dr. Veronica Dodero and her team at Bielefeld University has shed new light on how specific gluten-derived molecules can trigger leaky gut syndrome in people with celiac disease. The study, now published in the journal Angewandte Chemie, identifies the 33-mer deamidated gliadin peptide (DGP) as a key player in this process.
Key Findings on 33-mer Deamidated Gliadin Peptide
The research reveals that in active celiac disease, the 33-mer DGP forms nanosized structures known as oligomers. These oligomers accumulate in the gut epithelial cells, disrupting the integrity of the gut lining. This disruption leads to increased intestinal permeability, commonly referred to as leaky gut syndrome.
“Using high-resolution microscopy and biophysical techniques, our interdisciplinary team characterized the formation of 33-mer DGP oligomers,” explained Dr. Maria Georgina Herrera, the study’s first author and a researcher at the University of Buenos Aires. “We observed that the accumulation of these oligomers increases gut permeability in our cell model.”
Mechanisms Behind Leaky Gut Syndrome
Leaky gut syndrome occurs when the intestinal barrier becomes permeable, allowing harmful substances to enter the bloodstream. This permeability can lead to inflammatory responses and various diseases. In celiac disease, there is ongoing debate about the origins of this increased permeability. While the mainstream theory suggests that chronic inflammation in celiac disease causes a leaky gut, another theory posits that gluten’s direct effects on gut lining cells are the primary cause.
The study supports the latter theory, suggesting that the accumulation of 33-mer DGP oligomers directly damages the epithelial cells of the gut lining, leading to increased permeability. This damage allows gluten peptides, bacteria, and other toxins to enter the bloodstream, triggering inflammation and, in susceptible individuals, autoimmune responses associated with celiac disease.
“Our findings reinforce the medical hypothesis that impairment of the epithelial barrier promoted by gluten peptides is a cause and not a result of the immune response in celiac patients,” stated Dr. Veronica Dodero from the Faculty of Chemistry at Bielefeld University.
The Role of Human Leukocyte Antigens in Celiac Disease
Human leukocyte antigens (HLAs) are proteins on the surface of cells that play a crucial role in the immune system by distinguishing between self and non-self substances. In celiac disease, the HLA proteins HLA-DQ2 and HLA-DQ8 are strongly associated with the condition. The 33-mer DGP fits perfectly with HLA-DQ2 or HLA-DQ8, triggering an immune response that leads to inflammation and damage to the small intestine.
This interaction between the 33-mer DGP and HLA proteins transforms the peptide into a superantigen, driving the immune response that characterizes celiac disease. For those affected, adhering to a gluten-free diet remains the only effective long-term treatment.
As we observe International Celiac Day, these new insights highlight the importance of continued research in understanding and managing celiac disease, ultimately improving the quality of life for those affected by this condition.
