@article { ISI:000313903700015, title = {Glycated proteome: from reaction to intervention}, journal = {Proteomics Clinical Applications}, volume = {7}, number = {1-2, SI}, year = {2013}, month = {JAN}, pages = {155-170}, publisher = {WILEY-V C H VERLAG GMBH}, address = {POSTFACH 101161, 69451 WEINHEIM, GERMANY}, abstract = {

Glycation, a nonenzymatic reaction between reducing sugars and proteins, is a proteome wide phenomenon, predominantly observed in diabetes due to hyperglycemia. Glycated proteome of plasma, kidney, lens, and brain are implicated in the pathogenesis of various diseases, including diabetic complications, neurodegenerative diseases, cancer, and aging. This review discusses the strategies to characterize protein glycation, its functional implications in different diseases, and intervention strategies to protect the deleterious effects of protein glycation.

}, keywords = {aging, Diabetes, Glycation, RAGE}, issn = {1862-8346}, doi = {10.1002/prca.201200101}, author = {Kulkarni, Mahesh J. and Korwar, Arvind M. and Mary, Sheon and Bhonsle, Hemangi S. and Giri, Ashok P.} } @article {42688, title = {Glycation induces conformational changes in Amyloid-? peptide and enhances its aggregation propensity: molecular insights}, journal = {Physical Chemistry Chemical Physics}, volume = {18}, year = {2016}, month = {OCT}, pages = {31446-31458}, doi = {10.1039/C6CP05041G}, author = {Jana, Asis K. and Batkulwar, Kedar B. and Kulkarni, Mahesh J. and Sengupta, Neelanjana} } @article {43543, title = {Glycation inhibitors extend yeast chronological lifespan by reducing advanced glycation end products and by back regulation of proteins involved in mitochondrial respiration}, journal = {Journal of Proteomics}, volume = {156}, year = {2017}, month = {MAR}, pages = {104-112}, abstract = {Advanced Glycation End products (AGEs) are implicated in aging process. Thus, reducing AGEs by using glycation inhibitors may help in attenuating the aging process. In this study using Saccharomyces cerevisiae yeast system, we show that Aminoguanidine (AMG), a well-known glycation inhibitor, decreases the AGE modification of proteins in non-calorie restriction (NR) (2\% glucose) and extends chronological lifespan (CLS) similar to that of calorie restriction (CR) condition (0.5\% glucose). Proteomic analysis revealed that AMG back regulates the expression of differentially expressed proteins especially those involved in mitochondrial respiration in NR condition, suggesting that it switches metabolism from fermentation to respiration, mimicking CR. AMG induced back regulation of differentially expressed proteins could be possibly due to its chemical effect or indirectly by glycation inhibition. To delineate this, Metformin (MET), a structural analog of AMG and a mild glycation inhibitor and Hydralazine (HYD), another potent glycation inhibitor but not structural analog of AMG were used. HYD was more effective than MET in mimicking AMG suggesting that glycation inhibition was responsible for restoration of differentially expressed proteins. Thus glycation inhibitors particularly AMG, HYD and MET extend yeast CLS by reducing AGEs, modulating the expression of proteins involved in mitochondrial respiration and possibly by scavenging glucose. Significance: This study reports the role of glycation in aging process. In the non-caloric restriction condition, carbohydrates such as glucose promote protein glycation and reduce CLS. While, the inhibitors of glycation such as AMC, HYD, MET mimic the caloric restriction condition by back regulating deregulated proteins involved in mitochondria( respiration which could facilitate shift of metabolism from fermentation to respiration and extend yeast CLS. These findings suggest that glycation inhibitors can be potential molecules that can be used in management of aging. (C) 2017 Elsevier B.V. All rights reserved.}, doi = {10.1016/j.jprot.2017.01.015}, author = {Kazi, Rubina S. and Banarjee, Reema M. and Deshmukh, Arati B. and Patil, Gouri V. and Jagadeeshaprasad, Mashanipalya G. and Kulkarni, Mahesh J.} } @article {46229, title = {Glycation of glucose sensitive lysine residues K36, K438 and K549 of albumin is associated with prediabetes}, journal = {Journal of Proteomics}, year = {2019}, month = {AUG}, type = {Article}, abstract = {

Prediabetes is a risk factor for the development of diabetes. Early diagnosis of prediabetes may prevent the onset and progression of diabetes and its associated complications. Therefore, this study aimed at the identification of novel markers for efficient prediction of prediabetes. In this pursuit, we have evaluated the ability of glycated peptides of albumin in predicting prediabetes. Glycated peptides of in vitro glycated albumin were characterized by data dependent acquisition and parallel reaction monitoring using LC-HRMS. Amongst 14 glycated peptides characterized in vitro, four peptides, particularly, FK(CML)DLGEENFK, K(AML)VPQVSTPTLVEVSR, K(CML)VPQVSTPTLVEVSR, and K(AML)QTALVELVK, corresponding to 3 glucose sensitive lysine residues K36, K438, and K549, respectively showed significantly higher abundance in prediabetes than control. Additionally, the abundance of three of these peptides, namely K(AML)QTALVELVK, K(CML)VPQVSTPTLVEVSR and FK(CML)DLGEENFK was \>1.8-fold in prediabetes, which was significantly higher than the differences observed for FBG, PPG, and HbA1c. Further, the four glycated peptides showed a significant correlation with FBG, PPG, HbA1c, triglycerides, VLDL, and HDL. This study supports that glycated peptides of glucose sensitive lysine residues K36, K438 and K549 of albumin could be potentially useful markers for prediction of prediabetes. SIGNIFICANCE: Undiagnosed prediabetes may lead to diabetes and associated complications. This study reports targeted quantification of four glycated peptides particulary FK(CML)DLGEENFK, K(AML)VPQVSTPTLVEVSR, K(CML)VPQVSTPTLVEVSR, and K(AML)QTALVELVK, corresponding to 3 glucose sensitive lysine residues K36, K438 and K549 respectively by parallel reaction monitoring in healthy and prediabetic subjects. These peptides showed significantly higher abundance in prediabetes than healthy subjects, and showed significant correlation with various clinical parameters including FBG, PPG, HbA1c, and altered lipid profile. Therefore, together these four peptides constitute a panel of markers that can be useful for prediction of prediabetes.

}, doi = {10.1016/j.jprot.2019.103481}, author = {Rathore, R. and Sonwane, B. P. and Jagadeeshaprasad, M. G. and Kahar, S. and Santhakumari, B. and Unnikrishnan, A. G. and Kulkarni, Mahesh J.} }