Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0086543 (cataract)
29,165 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

As the UV-B cataract and early stages of diabetic cataract in rats only touches the epithelium and anterior superficial cortex, a whole lens analysis is not meaningful, but a regional analysis with the freeze-sectioning device has to be performed. Scheimpflug photography with microdensitometric image analysis enables the scientist to discern in vivo single layers along the optical axis of the lens. UV-B cataracts (0.2 J/cm2, every 2nd day) and diabetic cataracts (Streptozotocin (STZ), 70 mg/kg BW) were induced in Brown-Norway rats. The stages of lens opacification were documented by Scheimpflug photography. 8 weeks after start of UV-B treatment and at several dates before onset of visible diabetic cataractous changes, the animals were sacrificed. The lenses were divided reproducibly into 4 or 7 parts such as an equatorial ring and several layers of the central cylinder from anterior to posterior part. The enzyme activity spectrum shows highly region related pattern that would not have been found in a whole lens analysis. Aldose reductase was activated before appearance of visible cataractous changes due to diabetes compared to normal lenses. In contrast Fructose-1,6-biphosphate-aldolase activity was lower before onset of visible changes than in normal lenses, but only within the 1st section where later visible cataractous changes of UV-B cataract could be detected.
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PMID:Regional enzymatic analysis of UV-B and streptozotocin induced diabetic cataract lens. 196 39

Cataract is the major cause of blindness worldwide. Non-enzymic modification of lens proteins leading to a disruption of their short range order is an important route to cataract formation. A reaction between lens proteins and a compound found in the lens indicates a potential role for that compound in cataract formation. The reactions of glucose and fructose with lens protein in vitro were investigated. Fructose bound to lens protein at pH 6.9 in a time-dependent fashion over a period of 20 days. The reactions of both glucose and fructose with lens proteins and bovine serum albumin led to the formation of coloured and fluorescent compounds. The formation of such compounds was greater with fructose than with glucose. The kinetics of the reactions of lens proteins and bovine serum albumin with fructose as measured by the formation of the above compounds were not identical. This point must be appreciated when attempting to extrapolate from results obtained with bovine serum albumin as to the reactions of lens proteins. The incubation of lens proteins with fructose led to an enhancement of protein aggregation. The implications of the reactions between lens proteins and fructose for the formation of cataract in diabetics are discussed. Ibuprofen intake is associated with protection against cataract. At relatively high concentrations (10-20 mM) ibuprofen decreased the binding of fructose to lens protein: this decrease was statistically significant at selected times (Student's t-test, P less than 0.05). The formation of fluorescent compounds in the presence of fructose was also decreased by ibuprofen.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Non-enzymic modification of lens proteins by glucose and fructose: effects of ibuprofen. 201 2

Assay of the activities of hexokinase, phosphofructokinase, and pyruvate kinase showed that the first two declined in aging human lens cortex and all three enzymes retained constant activities in the epithelium throughout life. Moreover, both clear and cataractous aging lenses contained the same enzyme activities. ATP contents in cataracts, however, were lower than in clear lenses; in fact, after incubation at 37.5 degrees C in isotonic (290 to 300 mOsm), glucose-containing media, ATP was rapidly lost from cataracts (but not from clear lenses), suggesting excessive ATP expenditure in cataracts for osmotic balance. Cataracts incubated in media containing either glucose-6-phosphate or fructose-1, 6-diphosphate produced significantly higher ATP than with glucose in the media, indicating that glucose metabolism in human senile cataracts could be supplemented with hexose phosphates. Fructose-1, 6-diphosphate appeared to be more efficient than glucose-6-phosphate in preventing lens swelling during incubation.
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PMID:Supplementing glucose metabolism in human senile cataracts. 645 78