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Proteomic analysis of glycated proteins from streptozotocin-induced diabetic rat kidney

Chougale, Ashok D; Bhat, Shweta P.; Bhujbal, Swapnil V.; Zambare, Mandar R.; Puntambekar, Shraddha; Somani, Rahul S; Boppana, Ramanamurthy; Giri, Ashok P.; Kulkarni, Mahesh J.
Journal article, Peer reviewed
Published version
View/Open
10.1007%252Fs12033-011-9409-3.pdf (Locked)
URI
http://hdl.handle.net/11250/2491371
Date
2011
Metadata
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  • Institutt for bioteknologi og matvitenskap [898]
  • Publikasjoner fra CRIStin - NTNU [20734]
Original version
10.1007/s12033-011-9409-3
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.
Publisher
Springer Verlag
Journal
Molecular Biotechnology

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