@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:000381180000001,
	title = {Targeted quantification of N-1-(carboxymethyl) valine and N-1-(carboxyethyl) valine peptides of beta-hemoglobin for better diagnostics in diabetes},
	journal = {Clinical Proteomics},
	volume = {13},
	year = {2016},
	month = {MAR},
	pages = {Article Number: 7},
	publisher = {BIOMED CENTRAL LTD},
	address = {236 GRAYS INN RD, FLOOR 6, LONDON WC1X 8HL, ENGLAND},
	abstract = {<p>Background: N-1-(Deoxyfructosyl) valine (DFV) beta-hemoglobin (beta-Hb), commonly referred as HbA1c, is widely used diagnostic marker in diabetes, believed to provide glycemic status of preceding 90-120 days. However, the turnover of hemoglobin is about 120 days, the DFV-beta-Hb, an early and reversible glycation product eventually may undergo irreversible advanced glycation modifications such as carboxymethylation or carboxyethylation. Hence quantification of N-1-(carboxymethyl) valine (CMV) and N-1-(carboxyethyl) valine (CEV) peptides of beta-Hb would be useful in assessing actual glycemic status. Results: Fragment ion library for synthetically glycated peptides of hemoglobin was generated by using high resolution-accurate mass spectrometry (HR/AM). Using parallel reaction monitoring, deoxyfructosylated, carboxymethylated and carboxyethylated peptides of hemoglobin were quantified in clinical samples from healthy control, pre-diabetes, diabetes and poorly controlled diabetes. For the first time, we report N-1-beta-valine undergoes carboxyethylation and mass spectrometric quantification of CMV and CEV peptides of beta-hemoglobin. Carboxymethylation was found to be the most abundant modification of N-1-beta-valine. Both CMV-beta-Hb and CEV-beta-Hb peptides showed better correlation with severity of diabetes in terms of fasting glucose, postprandial glucose and microalbuminuria. Conclusions: This study reports carboxymethylation as a predominant modification of N-1-beta-valine of Hb, and quantification of CMV-beta-Hb and CEV-beta-Hb could be useful parameter for assessing the severity of diabetes.</p>},
	keywords = {Diabetes, Diagnosis, Glycation, Glycemic control, HbA1c, Mass spectrometry},
	issn = {1542-6416},
	doi = {10.1186/s12014-016-9108-y},
	author = {Jagadeeshaprasad, Mashanipalya G. and Batkulwar, Kedar B. and Meshram, Nishita N. and Tiwari, Shalbha and Korwar, Arvind M. and Unnikrishnan, Ambika G. and Kulkarni, Mahesh J.}
}
