[Analysis of cytoskeletal proteins in rat selenium cataract using two-dimensional electrophoresis]
H Matsushima1, K Mukai, Y Obara
1Department of Ophthalmology, Dokkyo University School of Medicine, Tochigi, Japan.
Background And Purpose:
Previous studies used sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) to characterize the modifications to lens proteins during opacification in the selenite model for cataract. To analyze the protein modifications in more detail, two dimensional electrophoresis (2 DE), which is more sensitive than 1 D electrophoresis, was used.
Results:
The results of 2 DE demonstrated rapid changes in cytoskeletal proteins including spectrin and vimentin at the earliest stages of opacification.
Conclusion:
The results suggested that the mechanism of opacification might involve changes in cytoskeletal proteins during the earliest stages of cataract formation.
More Related Videos
09:29Isolation of Intermediate Filament Proteins from Multiple Mouse Tissues to Study Aging-associated Post-translational Modifications
Published on: May 18, 2017
12:34Two-dimensional Gel Electrophoresis Coupled with Mass Spectrometry Methods for an Analysis of Human Pituitary Adenoma Tissue Proteome
Published on: April 2, 2018
Related Concept Videos
01:27SDS-PAGE
A variation of gel electrophoresis, termed polyacrylamide gel electrophoresis (PAGE), is commonly used for separating proteins according to their molecular size by passing them through a polyacrylamide gel. Because of the varying charges associated with amino acid side chains, PAGE can be used to separate intact proteins...
01:22Two-dimensional Gel Electrophoresis
The first dimension separation uses the isoelectric focusing or IEF technique performed on immobilized pH gradient (IPG) strips that separate proteins according to their isoelectric points.
Biological samples, such as cells...