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)

The blood-ocular barrier (BOB) shares similar neuroepithelial origin, microanatomy and functions with the blood-brain barrier. There are many natural (e. g. diabetes, hypertension) or iatrogenic (chemotherapy, retinal photocoagulation) conditions which can cause a BOB breakdown, resulting in visual acuity impairment or loss. The authors examined 42 patients affected by BOB damage in different pathological conditions. All patients previously underwent a conventional fluoroangiographic (FA) study. Nine patients with normal FA exam were evaluated also. Despite normal MRI findings immediately after Gd-DTPA injection, contrast leakage into the vitreous body or into the aqueous fluid was demonstrated in delayed scans (40-50 min after contrast administration), proving the existence of a BOB damage (sensitively 94 %). Although FA exam remains the choice modality in BOB breakdown demonstration, we propose MRI as a useful diagnostic tool when optic media opacity (cataract, haemovitreous, intraocular silicon oil) occurs, preventing direct retinal fundus imaging and/or an early screening tool.
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PMID:Blood-ocular barrier damage: use of contrast-enhanced MRI. 900 Apr 10

Nonenzymatic glycation by glucose and/or ascorbate leads to the formation of advanced glycation end products (AGEs), which are thought to be a critical element in lens protein aging and cataract formation. The relative participation of these two glycating agents was evaluated in vitro. The incubation of 100 mM [U-14C]-D-glucose and 10 mM [U-14C]-L-ascorbate with lens proteins resulted in an increasing incorporation over 3 weeks, reaching a maximum of 100 nMol mg-1 protein and 160 nMol mg-1 protein with ascorbate. Glycation was proportional to carbohydrate concentration with both reagents, however ascorbate was 18-fold more reactive with lens proteins than glucose. Protein crosslinking was not obvious with 250 mM glucose as measured by SDS-PAGE, however, ascorbate caused extensive crosslinking even at 3.0 mM. The sugar-dependent incorporation of N alpha-formyl-[U-14C]-L-lysine ([U-14C]Nfl) into proteins, gave values of 1.5 nMol mg-1 protein after 3 weeks with 100 mM glucose compared to 11 nMol mg-1 protein with 10 mM ascorbate. On a molar basis, ascorbate was 70-fold more active than glucose and 100-fold more active than fructose in the crosslinking assay. N alpha-formyl-N epsilon-fructosyllysine (1.0 mM) dissociated to cause the incorporation of 1.2 nMol of [U-14C]NfL, but 1.0 mM 3-deoxyglucosone, the putative active dissociation product of fructosyl-lysine, produced only 1.5 nMol mg-1 protein of crosslinks. The chelator, DTPA, had little or no effect on crosslinking in our assay except at the highest carbohydrate level. These data argue that glucose crosslinking can be shown in vitro with lens proteins, however, it does not proceed significantly via 3-deoxyglucosone, and does not require transition metal ion-mediated oxidation to occur. Quantitatively, however, it is almost two orders of magnitude less than the crosslinking by ascorbate oxidation products in vitro.
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PMID:The relative ability of glucose and ascorbate to glycate and crosslink lens proteins in vitro. off. 970 82