Proteomic Analysis of Glycated Proteins from Streptozotocin-Induced Diabetic Rat Kidney |
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Authors: | Ashok D Chougale Shweta P Bhat Swapnil V Bhujbal Mandar R Zambare Shraddha Puntambekar Rahul S Somani Ramanamurthy Boppana Ashok P Giri Mahesh J Kulkarni |
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Institution: | (1) Chemical Proteomics Group, Biochemical Sciences Division, National Chemical Laboratory (CSIR), Pune, 411008, India;(2) Sinhgad College of Pharmacy, Vadgaon, Pune, India;(3) National Centre for Cell Science, Pune, India; |
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Abstract: | Glycation of proteins leading to formation of advanced glycation end products (AGEs) has been considered as one of the important
causes of diabetic nephropathy. Therefore, in this study, glycated proteins were detected by anti-AGE antibodies from kidney
of streptozotocin-induced diabetic rat showing nephropathic symptoms, by using two dimensional electrophoresis and western
blot analysis. These glycated proteins were identified and characterized by using combination of peptide mass finger printing
and tandem mass spectrometric approaches. Glycated proteins identified included proteins from metabolic pathways, oxidative
stress, cell signaling, and transport. Several of the proteins modified by glycation were involved in glucose metabolism.
The extent of glycation was higher in diabetes compared to control, in the glycated proteins that were common to both control
and diabetic kidney. Two dimensional electrophoresis proteins profiling of glycated proteins suggest that four of the glycated
proteins were significantly up regulated in diabetes. |
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