Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0017536 (giardiasis)
 1,714 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Among 10 children with giardiasis, eight had iron deficiency; iron deficiency anemia was the main complaint in three. Evaluation of iron absorption by the oral iron load test demonstrated a subnormal response (i.e., increase in serum iron levels of less than 100 micrograms/dl) in all eight patients with iron deficiency. In contrast, in two iron-sufficient patients with giardiasis the response to an oral iron load was normal. Xylose absorption was abnormal in five of the 10 patients. After metronidazole dosing, iron absorption became normal in seven patients but remained abnormal in one patient, who also had IgA deficiency. Xylose absorption became normal in all five patients who underwent a second test, but remained abnormal in the patient with IgA deficiency. Concomitant morphologic-studies of jejunal biopsy material from these patients revealed moderate changes in the intestinal mucosa of two patients. We conclude that malabsorption of iron is a complication of giardiasis.
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PMID:Iron malabsorption in giardiasis. 400 42

Giardia lambia is a flagellated protozoan parasite that lives in the small intestine and is the causal agent of giardiasis. It has been reported that G. lamblia exhibits glucose-6-phosphate dehydrogenase (G6PD), the first enzyme in the pentose phosphate pathway (PPP). Our group work demonstrated that the g6pd and 6pgl genes are present in the open frame that gives rise to the fused G6PD::6PGL protein; where the G6PD region is similar to the 3D structure of G6PD in Homo sapiens. The objective of the present work was to show the presence of the structural NADP+ binding site on the fused G6PD::6PGL protein and evaluate the effect of the NADP+ molecule on protein stability using biochemical and computational analysis. A protective effect was observed on the thermal inactivation, thermal stability, and trypsin digestions assays when the protein was incubated with NADP+. By molecular docking, we determined the possible structural-NADP+ binding site, which is located between the Rossmann fold of G6PD and 6PGL. Finally, molecular dynamic (MD) simulation was used to test the stability of this complex; it was determined that the presence of both NADP+ structural and cofactor increased the stability of the enzyme, which is in agreement with our experimental results.
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PMID:Identification of the NADP+ Structural Binding Site and Coenzyme Effect on the Fused G6PD::6PGL Protein from Giardia lamblia. 3189 24