@article { ISI:000259509600003,
	title = {Albumin competitively inhibits glycation of less abundant proteins},
	journal = {Protein and Peptide Letters},
	volume = {15},
	number = {7},
	year = {2008},
	month = {JUL},
	pages = {663-667},
	publisher = {BENTHAM SCIENCE PUBL LTD},
	type = {Article},
	address = {EXECUTIVE STE Y26, PO BOX 7917, SAIF ZONE, 1200 BR SHARJAH, U ARAB EMIRATES},
	abstract = {<p>Glycation, a non-enzymatic reaction between glucose and protein is the primary cause of diabetic complications. Albumin, the most abundant plasma protein undergoes glycation both in vivo and in vitro. The influence of albumin on glycation of less abundant proteins has not been addressed. For the first time, we show that albumin competitively inhibits the glycation of less abundant proteins. This study suggests that at least in the initial stages of diabetes, albumin may protect other proteins from glycation.</p>},
	keywords = {Diabetes, glucose, insulin, MALDI-TOF-MS, vascular complication},
	issn = {0929-8665},
	doi = {10.2174/092986608785133690},
	author = {Bhonsle, Hemangi S. and Singh, Sameer Kumar and Srivastava, Ghanshyam and Boppana, Ramanamurthy and Kulkarni, Mahesh J.}
}
@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.}
}
