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1. Cataracts were developed by incubating rabbit lenses for 22hr. at 37 degrees in a culture medium containing tyrosine and tyrosinase (EC 1.10.3.1). 2. A 45% diminution in the content of GSH and significant inhibition of glucose 6-phosphate dehydrogenase (EC 1.1.1.49) activity were observed in the
OBJECTIVE
The Emory mouse is a well-characterized model for age-onset cataract. The purpose of the present study was to identify differentially expressed genes between pre- and postcataract Emory mouse lenses.
METHODS
Eyes were extracted from Emory mice at 3 weeks (precataract) and 7.5 months
OBJECTIVE
Protein tyrosine phosphorylation is an important event in the cell signal transduction process. Phosphatidylinositol-3 kinase (PI-3K) is an intracellular signal mediator and plays a key role in many cellular functions. In this study we have examined the changes in lens protein tyrosine
Congenital cataracts (CCs) are clinically and genetically heterogeneous. Mutations in the same gene may lead to CCs differing in inheritance, morphology and severity. Loci for autosomal dominant posterior polar CC and total CC have both been mapped to the chromosomal 1p36 region harboring the EPHA2
Reversible "cold cataract" phenomenon of a SD-strain rat lens (29 days old) was studied by Raman spectroscopy in the temperature range of 35-17.5 degrees C. Cold cataract appeared in the lens nucleus below 26 degrees C. The Raman spectra did not show any detectable change in the 300-800 cm-1 and
Cataract is a common age-related condition that is caused by progressive clouding of the normally clear lens. Cataract can be effectively treated by surgery; however, like any surgery, there can be complications and the development of a secondary cataract, known as posterior capsule opacification
With increase in age, proteins of the eye lens undergo covalent modifications associated with interprotein cross-linking, loss of protein solubility, generation of protein-associated pigments, and racemization of some optically active residues. Precipitated protein aggregates localized in the
Raman spectra have been measured for the lenses from cac-strain mice. These mice possess a hereditary defect and provide lenses at various stages of opacification. The Raman spectra of normal mouse lenses have been obtained also for comparison purposes. The amide I and III bands appear in very
Osmotic (cortical) cataract was induced in bovine lenses during long-term organ culture by adding the cardiac glycoside, ouabain, to the incubation medium. This insult produces a much more rapid effect on protein synthesis than it does on amino acid influx, efflux or net protein loss. The kinetics
OBJECTIVE
To determine the levels of free UV filters and selected amino acids in cataract lenses compared with normal lenses.
METHODS
Indian cataract lenses (n=39) and normal lenses (n=6) were examined by HPLC to quantify levels of UV filter compounds, the UV filter precursor amino acid tryptophan
Raman spectroscopy shows that maturation of galactose cataract greatly increases the water signal (at 3417 cm-1) which is correlated with the inbibition of water in the lens. The maximum water: protein ratio (expressed as Raman intensity ratio I3417:I2936) occurs at the peripheral cortex (i.e.
BACKGROUND
Ibrutinib is a tyrosine kinase inhibitor commonly used in patients with chronic lymphocytic leukemia. Based on the published literature, it has a very sound ophthalmologic safety profile. In the following, we describe a case of anterior chamber fibrinoid syndrome in a patient on ibrutinib
Oxidation of tyrosine in the presence of bovine lens proteins leads to the formation of brown or black melanoproteins. Both tyrosinase and the oxidizing system of ferrous sulphate-ascorbic acid-EDTA are effective. The fluorescence of the lens proteins is both altered and enhanced by the
Eyes absent (EYA) proteins are defined by a conserved C-terminal EYA domain (ED) that both contributes to its function as a transcriptional coactivator by mediating protein-protein interactions and possesses intrinsic protein tyrosine phosphatase activity. Mutations in human EYA1 result in an