Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0017160 (gastroenteritis)
 11,398 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Alocasia macrorrhiza (L) Schott and Endl is called Hai Yu, Tien Ho, Shan Yu, Kuan Yin Lien, Tu Chiao lien, Lao Hu Yu and Lang Du in Chinese. Its common English name is Giant Elephant's Ear. The toxic effects of A macrorrhiza arise from sapotoxin and include gastroenteritis and paralysis of the nerve centers. From 1985 to 1993 all individuals who called the Poison Control Center asking for information regarding macrorrhiza were included in this retrospective study. A questionnaire filled out by the Poison Control Center staff collected the demographic data of the victim, the reason for consumption, the prescribed part, clinical symptoms and signs of the victim, and medical outcome of poisonings. Among 27 cases of A macrorrhiza poisoning, the age was 1.5 to 68 y with 12 females and 15 males. One had skin contact and 1 had eye contact. In the 25 cases that consumed the plant leaf or tuber either raw or cooked, the primary symptom was in injected sore throat and the secondary symptom was numbness of the oral cavity. Some patients had salivation, dysphonia, abdominal pain, ulcers of the oral cavity, difficulty in swallowing, thoracodynia, chest tightness and swollen lips. We believe the presence of sapotoxin alone is not sufficient to explain the injected swollen and ulcerative lesions. Calcium oxalate is reported distributed in the entire plant and results in inflammation of the oral cavity and mucous membranes just as our patients had.
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PMID:Calcium oxalate is the main toxic component in clinical presentations of alocasis macrorrhiza (L) Schott and Endl poisonings. 955 63

Campylobacter jejuni, the leading cause of human gastroenteritis, expresses a ferric binding protein (cFbpA) that in many pathogenic bacteria functions to acquire iron as part of their virulence repertoire. Recombinant cFbpA is isolated with ferric iron bound from Escherichia coli. The crystal structure of cFbpA reveals unprecedented iron coordination by only five protein ligands. The histidine and one tyrosine are derived from the N-terminal domain, whereas the three remaining tyrosine ligands are from the C-terminal domain. Surprisingly, a synergistic anion present in all other characterized ferric transport proteins is not observed in the cFbpA iron-binding site, suggesting a novel role for this protein in iron uptake. Furthermore, cFbpA is shown to bind iron with high affinity similar to Neisserial FbpA and exhibits an unusual preference for ferrous iron (oxidized subsequently to the ferric form) or ferric iron chelated by oxalate. Sequence and structure analyses reveal that cFbpA is a member of a new class of ferric binding proteins that includes homologs from invasive and intracellular bacteria as well as cyanobacteria. Overall, six classes are defined based on clustering within the tree and by their putative iron coordination. The absence of a synergistic anion in the iron coordination sphere of cFbpA also suggests an alternative model of evolution for FbpA homologs involving an early iron-binding ancestor instead of a requirement for a preexisting anion-binding ancestor.
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PMID:Anion-independent iron coordination by the Campylobacter jejuni ferric binding protein. 1561 74