01657nas a2200265 4500008004100000022001400041245010500055210006900160260009500229300001200324490000800336520066400344653003601008653001801044653000901062100002301071700002501094700002401119700002101143700002201164700002201186700003301208700002501241856012501266 2012 eng d a0006-291X00aAnalysis of AGE modified proteins and RAGE expression in HER2/neu negative invasive ductal carcinoma0 aAnalysis of AGE modified proteins and RAGE expression in HER2neu a525 B ST, STE 1900, SAN DIEGO, CA 92101-4495 USAbACADEMIC PRESS INC ELSEVIER SCIENCEcMAR a490-4940 v4193 a

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.

10aadvanced glycation end products10aBreast cancer10aRAGE1 aKorwar, Arvind, M.1 aBhonsle, Hemangi, S.1 aChougale, Ashok, D.1 aKote, Sachin, S.1 aGawai, Kachru, R.1 aGhole, Vikram, S.1 aKoppikar, Chaitanyananda, B.1 aKulkarni, Mahesh, J. uhttps://library.ncl.res.in/content/analysis-age-modified-proteins-and-rage-expression-her2neu-negative-invasive-ductal-002873nas a2200325 4500008004100000022001400041245012300055210006900178260006700247300001200314490000700326520171600333653003602049653001002085653002702095653001102122653001402133653001302147653001502160100002502175700002102200700002102221700002702242700003902269700002302308700003602331700002502367700002402392856013102416 2015 eng d a1474-971800aRifampicin reduces advanced glycation end products and activates DAF-16 to increase lifespan in Caenorhabditis elegans0 aRifampicin reduces advanced glycation end products and activates a111 RIVER ST, HOBOKEN 07030-5774, NJ USAbWILEY-BLACKWELLcJUN a463-4730 v143 a

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.

10aadvanced glycation end products10aaging10aCaenorhabditis elegans10aDAF-1610aGlycation10alifespan10arifampicin1 aGolegaonkar, Sandeep1 aTabrez, Syed, S.1 aPandit, Awadhesh1 aSethurathinam, Shalini1 aJagadeeshaprasad, Mashanipalya, G.1 aBansode, Sneha, B.1 aSampathkumar, Srinivasa-Gopalan1 aKulkarni, Mahesh, J.1 aMukhopadhyay, Arnab uhttps://library.ncl.res.in/content/rifampicin-reduces-advanced-glycation-end-products-and-activates-daf-16-increase-lifespan-002201nas a2200205 4500008004100000022001400041245006800055210006500123260000800188300001000196490000700206520153200213653003601745653002401781653001201805653001801817100002901835700003601864856009501900 2020 eng d a1387-287700aP301 L, an FTDP-17 mutant, exhibits enhanced glycation in vitro0 aP301 L an FTDP17 mutant exhibits enhanced glycation in vitro cJAN a61-710 v753 a

Background: Frontotemporal dementia and parkinsonism-linked to chromosome-17 are a group of diseases with tau mutations leading to primary tauopathies which include progressive supranuclear palsy, corticobas al syndrome, and frontotemporal lobar degeneration. Alzheimer's disease is a non-primary tauopathy, which displays tau neuropathology of excess tangle formation and accumulation. FTDP-17 mutations are responsible for early onset of AD, which can be attributed to compromised physiological functions due to the mutations. Tau is a microtubule-binding protein that secures the integrity of polymerized microtubules in neuronal cells. It malfunctions owing to various insults and stress conditions-like mutations and post-translational modifications. Objective: In this study, we modified the wild type and tau mutants by methyl glyoxal and thus studied whether glycation can enhance the aggregation of predisposed mutant tau. Methods: Tau glycation was studied by fluorescence assays, SDS-PAGE analysis, conformational evaluation, and transmission electron microscopy. Results: Our study suggests that FTDP-17 mutant P301 L leads to enhanced glycation-induced aggregation as well as advanced glycation end products formation. Glycation forms amorphous aggregates of tau and its mutants without altering its native conformation. Conclusion: The metabolic anomalies and genetic predisposition have found to accelerate tau-mediated neurodegeneration and prove detrimental for the early-onset of Alzheimer's disease.

10aadvanced glycation end products10aAlzheimer's disease10aFTDP-1710atau glycation1 aSonawane, Shweta, Kishor1 aChinnathambi, Subashchandrabose uhttps://library.ncl.res.in/content/p301-l-ftdp-17-mutant-exhibits-enhanced-glycation-vitro