@article { ISI:000302437100008,
	title = {Analysis of AGE modified proteins and RAGE expression in HER2/neu negative invasive ductal carcinoma},
	journal = {Biochemical and Biophysical Research Communications},
	volume = {419},
	number = {3},
	year = {2012},
	month = {MAR},
	pages = {490-494},
	publisher = {ACADEMIC PRESS INC ELSEVIER SCIENCE},
	address = {525 B ST, STE 1900, SAN DIEGO, CA 92101-4495 USA},
	abstract = {<p>Cancer is associated with increased glycolysis and carbonyl stress. In view of this, AGE modified proteins were identified from clinical breast cancer tissue using 2DE-immunoblot and mass-spectrometry. These proteins were identified to be serotransferrin, fibrinogen gamma chain, glycerol-3-phosphate dehydrogenase, lactate dehydrogenase, annexin II, prohibitin and peroxiredoxin 6, which have established role in cancer. Further, RAGE expression and its downstream signaling proteins NADPH oxidase and NF-kB were studied. Role of these AGE modified proteins and RAGE signaling in breast cancer is discussed. (C) 2012 Elsevier Inc. All rights reserved.</p>},
	keywords = {advanced glycation end products, Breast cancer, RAGE},
	issn = {0006-291X},
	doi = {10.1016/j.bbrc.2012.02.039},
	author = {Korwar, Arvind M. and Bhonsle, Hemangi S. and Chougale, Ashok D. and Kote, Sachin S. and Gawai, Kachru R. and Ghole, Vikram S. and Koppikar, Chaitanyananda B. and Kulkarni, Mahesh J.}
}
@article { ISI:000353689400017,
	title = {Rifampicin reduces advanced glycation end products and activates DAF-16 to increase lifespan in Caenorhabditis elegans},
	journal = {Aging Cell},
	volume = {14},
	number = {3},
	year = {2015},
	month = {JUN},
	pages = {463-473},
	publisher = {WILEY-BLACKWELL},
	address = {111 RIVER ST, HOBOKEN 07030-5774, NJ USA},
	abstract = {<p>Advanced glycation end products (AGEs) are formed when glucose reacts nonenzymatically with proteins; these modifications are implicated in aging and pathogenesis of many age-related diseases including type II diabetes, atherosclerosis, and neurodegenerative disorders. Thus, pharmaceutical interventions that can reduce AGEs may delay age-onset diseases and extend lifespan. Using LC-MSE, we show that rifampicin (RIF) reduces glycation of important cellular proteins in vivo and consequently increases lifespan in Caenorhabditis elegans by up to 60\%. RIF analog rifamycin SV (RSV) possesses similar properties, while rifaximin (RMN) lacks antiglycation activity and therefore fails to affect lifespan positively. The efficacy of RIF and RSV as potent antiglycating agents may be attributed to the presence of a p-dihydroxyl moiety that can potentially undergo spontaneous oxidation to yield highly reactive p-quinone structures, a feature absent in RMN. We also show that supplementing rifampicin late in adulthood is sufficient to increase lifespan. For its effect on longevity, rifampicin requires DAF-18 (nematode PTEN) as well as JNK-1 and activates DAF-16, the FOXO homolog. Interestingly, the drug treatment modulates transcription of a different subset of DAF-16 target genes, those not controlled by the conserved Insulin-IGF-1-like signaling pathway. RIF failed to increase the lifespan of daf-16 null mutant despite reducing glycation, showing thereby that DAF-16 may not directly affect AGE formation. Together, our data suggest that the dual ability to reduce glycation in vivo and activate prolongevity processes through DAF-16 makes RIF and RSV effective lifespan-extending interventions.</p>},
	keywords = {advanced glycation end products, aging, Caenorhabditis elegans, DAF-16, Glycation, lifespan, rifampicin},
	issn = {1474-9718},
	doi = {10.1111/acel.12327},
	author = {Golegaonkar, Sandeep and Tabrez, Syed S. and Pandit, Awadhesh and Sethurathinam, Shalini and Jagadeeshaprasad, Mashanipalya G. and Bansode, Sneha B. and Sampathkumar, Srinivasa-Gopalan and Kulkarni, Mahesh J. and Mukhopadhyay, Arnab}
}
