@article { ISI:000298860100004,
	title = {Proteomic analysis of glycated proteins from streptozotocin-induced diabetic rat kidney},
	journal = {Molecular Biotechnology},
	volume = {50},
	number = {1},
	year = {2012},
	month = {JAN},
	pages = {28-38},
	publisher = {HUMANA PRESS INC},
	address = {999 RIVERVIEW DRIVE SUITE 208, TOTOWA, NJ 07512 USA},
	abstract = {<p>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.</p>},
	keywords = {AGE, Diabetes, Glucose toxicity, Nephropathy, Post-translation modification},
	issn = {1073-6085},
	doi = {10.1007/s12033-011-9409-3},
	author = {Chougale, Ashok D. and Bhat, Shweta P. and Bhujbal, Swapnil V. and Zambare, Mandar R. and Puntambekar, Shraddha and Somani, Rahul S. and Boppana, Ramanamurthy and Giri, Ashok P. and Kulkarni, Mahesh J.}
}
