Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0022568 (keratitis)
5,133 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

We used wide-field specular microscopy to examine 60 eyes with clinically evident corneal epithelial abnormalities in vivo. The progression of epithelial edema from early basal edema to later bullous changes and eventual subepithelial fibrovascular ingrowth was observed in 35 eyes. Three eyes with filamentary keratitis displayed a protruding mucoid filament or actual mucus incorporation into the epithelium with surrounding distortion of superficial cells. Abnormally shaped and interdigitated epithelial cells were present as a result of trophic ulceration caused by herpes simplex keratitis. The Fleischer ring of ferritin deposits. Surface epithelial cells in this disorder were elongated and contained increased numbers of dark cells in more severe cases. The raised granular lesion of Thygeson's superficial punctate keratitis and subepithelial deposits in cases of basement membrane dystrophy were also observed. Invading fibrovascular tissue was identified in superficial pannus.
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PMID:In vivo microscopic observations of human corneal epithelial abnormalities. 706 95

Acanthamoeba castellanii, a free-living amoeba, is an amphizoic organism that can behave as an opportunistic pathogen, causing granulomatous amoebic encephalitis in immunocompromised patients or infecting immunocompetent individuals via cutaneous lesions, sinusoidal infections, or amoebic keratitis. Therefore, this amoeba could be in contact with different iron-binding proteins, such as lactoferrin in tears and mucosa and transferrin and hemoglobin in blood. Iron is a vital and necessary element for host metabolism but also for parasite survival. Accordingly, parasites have developed iron uptake mechanisms, one of which is the utilization of proteases to degrade host iron-binding proteins. In this work, we performed a partial biochemical characterization of A. castellanii proteases at different pHs and utilizing protease inhibitors with 10% sodium dodecyl sulfate-polyacrylamide gel electrophoresis and copolymerized with different iron-binding proteins. We describe for the first time the presence of several cysteine proteases in a total A. castellanii crude extract and in conditioned culture medium precipitated with ethanol. These amoebic peptidases degraded human holo-lactoferrin, holo-transferrin, hemoglobin, and horse spleen ferritin; some of these proteases were substrate specific, and others degraded multiple substrates. These proteases could be considered virulence factors that promote iron acquisition from the host.
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PMID:Acanthamoeba castellanii Proteases are Capable of Degrading Iron-Binding Proteins as a Possible Mechanism of Pathogenicity. 2573 66