Dataset Information

The Multifocal On- and Off-Responses in the Human Diabetic Retina.

ABSTRACT: The characteristics of the on- and off-responses in the human diabetic retina by a "long-duration" multifocal electroretinogram (mfERG) paradigm were investigated. Changes in the retinal antagonistic interaction were also evaluated in the early stage of diabetes mellitus (DM). Twenty type II diabetic patients with no or mild non-proliferative diabetic retinopathy (NPDR) and twenty-one age-matched healthy controls were recruited for "long-duration" mfERG measurements. A 61-hexagon mfERG stimulus was displayed under two chromatic conditions (white/black and blue/black) at matched luminance. The amplitudes and implicit times of the on-response components (N1, P1 and N2) and off-response (P2) components were analysed. The blue stimulation generally triggered greater mfERG amplitudes in P1, N2 and P2 (p<0.05) than those from white stimulation in both control and diabetic groups. The diabetic group showed significantly greater N2 amplitude than the controls under white stimulation in mid-retinal regions (Rings 2 and 4) (p<0.05). When the stimulus was changed from white to blue, the diabetic group showed a smaller percentage change in N2 amplitude than the controls in peripheral retinal region (Ring 5) (p<0.02). When a stimulus is changed from white (broad-band spectral stimulation) to blue (narrow-band spectral stimulation), a decrease in the involvement of lateral antagonism would be expected. The larger amplitude of the on-response component (N2) in the diabetic patients suggested an imbalance of lateral antagonism, and the lesser percentage change of N2 amplitude in the diabetic group may indicate an impairment of the cross-talk at the middle retinal level in early stages of DM.

SUBMITTER: Lung JC

PROVIDER: S-EPMC4871365 | biostudies-literature | 2016

REPOSITORIES: biostudies-literature

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The Multifocal On- and Off-Responses in the Human Diabetic Retina.

Lung Jenny C Y JC Swann Peter G PG Chan Henry H L HH

PloS one 20160517 5

The characteristics of the on- and off-responses in the human diabetic retina by a "long-duration" multifocal electroretinogram (mfERG) paradigm were investigated. Changes in the retinal antagonistic interaction were also evaluated in the early stage of diabetes mellitus (DM). Twenty type II diabetic patients with no or mild non-proliferative diabetic retinopathy (NPDR) and twenty-one age-matched healthy controls were recruited for "long-duration" mfERG measurements. A 61-hexagon mfERG stimulus ...[more]

PMID: 27187490

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Project description:Diabetic retinopathy, a retinal vascular disease, is inhibited in animals treated with aminoguanidine, an inhibitor of inducible nitric-oxide synthase. This treatment also reduces retinal protein nitration, which is greater in diabetic rat retina than nondiabetic retina. As an approach to understanding the molecular mechanisms of diabetic retinopathy, we sought the identity of nitrotyrosine-containing proteins in retina from streptozotocin-induced diabetic rats and in a rat retinal Müller cell line grown in high glucose (25 mM). Anti-nitrotyrosine immunoprecipitation products from rat retina and Müller cells were analyzed by LC-MS/MS. Ten nitrated proteins in diabetic rat retina and three nitrated proteins in Müller cells grown in high glucose were identified; three additional nitrotyrosine-containing proteins were tentatively identified from diabetic retina. The identified nitrotyrosine-containing proteins participate in a variety of processes including glucose metabolism, signal transduction, and transcription/translation. Among the nitrated proteins were insulin-responsive glucose transporter type 4 (GLUT-4), which has been implicated previously in the pathogenesis of diabetes mellitus; exocyst complex component Exo70, which functions in insulin-stimulated glucose uptake of GLUT-4-containing vesicles; and fibroblast growth factor receptor 2, which influences retinal vascularization via fibroblast growth factor signaling. Nitration of tyrosine phosphorylation sites were identified in five proteins, including GLUT-4, exocyst complex component Exo70, protein-tyrosine phosphatase eta, sensory neuron synuclein, and inositol trisphosphate receptor 3. Quantitation of nitration and phosphorylation at common tyrosine modification sites in GLUT-4 and protein-tyrosine phosphatase eta from diabetic and nondiabetic animals suggests that nitration reduced tyrosine phosphorylation approximately 2X in these proteins from diabetic retina. The present results provide new insights regarding tyrosine nitration and its potential role in the molecular mechanisms of diabetic retinopathy.

Dataset Information

The Multifocal On- and Off-Responses in the Human Diabetic Retina.

Publications

The Multifocal On- and Off-Responses in the Human Diabetic Retina.

Similar Datasets

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