@article { ISI:000313764300025,
	title = {Proteomic study reveals downregulation of apolipoprotein A1 in plasma of poorly controlled diabetes: a pilot study},
	journal = {Molecular Medicine Reports},
	volume = {7},
	number = {2},
	year = {2013},
	month = {FEB},
	pages = {495-498},
	publisher = {SPANDIDOS PUBL LTD},
	address = {POB 18179, ATHENS, 116 10, GREECE},
	abstract = {<p>Proteomic approaches aid in gaining a better understanding of the pathophysiology of diabetic complications. In view of this, differential protein expression in diabetic plasma samples was studied by a combination of proteomic and western blot analyses. Diabetic plasma samples were categorized based on glycated haemoglobin levels as controlled diabetes (CD; 7-8\%), poorly controlled diabetes (PCD; \&gt;8\%) and non-diabetic control (ND;\&lt;6.4\%). Two-dimensional electrophoresis and liquid chromatography-mass spectrometry revealed differential expression of proteins including upregulation of fibrinogen and haptoglobin and downregulation of vitamin D binding protein, alpha-1-antitrypsin, transthyretin and apolipoprotein A1 (Apo A1) in diabetic compared with non-diabetic plasma samples. Amongst these proteins, Apo A1 downregulation was prominent in PCD. Downregulation of Apo A1 may serve as an early predictive marker of diabetic complications.</p>},
	keywords = {biomarker, HbA1c, proteomics},
	issn = {1791-2997},
	doi = {10.3892/mmr.2012.1223},
	author = {Bhonsle, Hemangi S. and Korwar, Arvind M. and Chougale, Ashok D. and Kote, Sachin S. and Dhande, Nitin L. and Shelgikar, Kishore M. and Kulkarni, Mahesh J.}
}
@article { ISI:000339880300021,
	title = {Proteomics of arsenic stress in the gram-positive organism Exiguobacterium sp PS NCIM 5463},
	journal = {Applied Microbiology and Biotechnology},
	volume = {98},
	number = {15},
	year = {2014},
	month = {AUG},
	pages = {6761-6773},
	publisher = {SPRINGER},
	address = {233 SPRING ST, NEW YORK, NY 10013 USA},
	abstract = {<p>The general responses of microorganisms to environmental onslaughts are modulated by altering the gene expression pattern to reduce damage in the cell and produce compensating stress responses. The present study attempts to unravel the response of the Gram-positive Exiguobacterium sp. PS NCIM 5463 in the presence of [As(III)] and arsenate [As(V)] using comparative proteomics via two-dimension gel electrophoresis (2-DE) coupled with identification of proteins using matrix-assisted laser desorption/ionisation (MALDI-TOF/MALDI-TOF/TOF). Out of 926 Coomassie-stained proteins, 45 were differentially expressed (p \&lt; 0.05). Considering the resolution and abundance level, 24 spots (peptides) were subjected to MALDI analysis, identified and categorised into several functional categories, viz., nitrogen metabolism, energy and stress regulators, carbohydrate metabolism, protein synthesis components and others. A functional role of each protein is discussed in Exiguobacterium sp. PS 5463 under arsenic stress and validated at their transcript level using a quantitative real-time polymerase chain reaction. Unlike previous reports that unravel the responses toward arsenic stress in Gram-negative organisms, the present study identified new proteins under arsenic stress in a Gram-positive organism, Exiguobacterium sp. PS NCIM 5463, which could elucidate the physiology of organisms under arsenic stress.</p>
},
	keywords = {Arsenic, Exiguobacterium, proteomics, Stress, Transcriptomics},
	issn = {0175-7598},
	doi = {10.1007/s00253-014-5873-6},
	author = {Sacheti, Poonam and Patil, Rajendra and Dube, Ankita and Bhonsle, Hemangi S. and Thombre, Dipalee and Marathe, Sayali and Vidhate, Ravindra and Wagh, Priyanka and Kulkarni, Mahesh J. and Rapole, Srikanth and Gade, Wasudeo N.}
}
