@article { ISI:000300458300075,
	title = {Low plasma albumin levels are associated with increased plasma protein glycation and HbA1c in diabetes},
	journal = {Journal of Proteome Research},
	volume = {11},
	number = {2},
	year = {2012},
	month = {FEB},
	pages = {1391-1396},
	publisher = {AMER CHEMICAL SOC},
	address = {1155 16TH ST, NW, WASHINGTON, DC 20036 USA},
	abstract = {<p>Albumin is one of the most abundant plasma proteins and is heavily glycated in diabetes. In this study, we have addressed whether variation in the albumin levels influence glycation of plasma proteins and HbA1c. The study was performed in three systems: (1) streptozotocin (STZ)-induced diabetic mice plasma, (2) diabetic clinical plasma, and (3) in vitro glycated plasma. Diabetic mice and clinical plasma samples were categorized as diabetic high albumin plasma (DHAP) and diabetic low albumin plasma (DLAP) on the basis of their albumin levels. For the in vitro experiment, two albumin levels, high albumin plasma (HAP) and low albumin plasma (LAP), were created by differential depletion of plasma albumin. Protein glycation was studied by using a combination of two-dimensional electrophoresis (2DE), Western blotting, and LC-MSE. In both mice and clinical experiments, an increased plasma protein glycation was observed in DLAP than in DHAP. Additionally, plasma albumin levels were negatively correlated with HbA1c. The in vitro experiment with differential depletion of albumin mechanistically showed that the low albumin levels are associated with increased plasma protein glycation and that albumin competes for glycation with other plasma proteins.</p>},
	keywords = {advanced glycation end products (AGEs), Albumin, glucose, post translational modification},
	issn = {1535-3893},
	doi = {10.1021/pr201030m},
	author = {Bhonsle, Hemangi S. and Korwar, Arvind M. and Kote, Sachin S. and Golegaonkar, Sandeep B. and Chougale, Ashok D. and Shaik, Mahemud L. and Dhande, Nitin L. and Giri, Ashok P. and Shelgikar, Kishore M. and Boppana, Ramanamurthy and Kulkarni, Mahesh J.}
}
@article { ISI:000315745600001,
	title = {Zoom-in - a targeted database search for identification of glycation modifications analyzed by untargeted tandem mass spectrometry},
	journal = {European Journal of Mass Spectrometry},
	volume = {18},
	number = {6},
	year = {2012},
	month = {JAN},
	pages = {475-481},
	publisher = {IM PUBLICATIONS},
	type = {Article},
	address = {6 CHARLTON MILL, CHARLTON, CHICHESTER,, W SUSSEX PO18 0HY, ENGLAND},
	abstract = {<p>Post-translational modifications (PTMs) are very important to biological function, however their identification and characterization is technically challenging. In this study, we have identified glycation modifications by nano LC-MSE, a data independent acquisition work flow, followed by database search using the Protein Lynx Global Server (PLGS). PLGS search with a complete human protein database hardly identified glycation modifications in a glycated human serum albumin (HSA), which was detected to be glycated by western blotting with advanced glycation end products (AGE) antibody and fluorescence spectroscopy. To overcome this difficulty, {\textquoteleft}{\textquoteleft}Zoom-In{\textquoteright}{\textquoteright} approach, a targeted database search was used to identify glycation modifications in a glycated HSA, which were further manually validated. This approach was useful for identification of glycation modifications from untargeted tandem mass spectrometry workflow such as MSE, but may require the development of a new algorithm or an upgrade of the existing software.</p>},
	keywords = {advanced glycation end products (AGEs), data independent acquisition, Diabetes, post-translational modifications},
	issn = {1469-0667},
	doi = {10.1255/ejms.1203},
	author = {Bhonsle, Hemangi S. and Korwar, Arvind M. and Kesavan, Suresh K. and Bhosale, Santosh D. and Bansode, Sneha B. and Kulkarni, Mahesh J.}
}
