<?xml version="1.0" encoding="UTF-8"?><xml><records><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Adeshara, Krishna A.</style></author><author><style face="normal" font="default" size="100%">Agrawal, Sanskruthi B.</style></author><author><style face="normal" font="default" size="100%">Gaikwad, Sushama M.</style></author><author><style face="normal" font="default" size="100%">Tupe, Rashmi S.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Pioglitazone inhibits advanced glycation induced protein modifications and down-regulates expression of RAGE and NF-kappa B in renal cells</style></title><secondary-title><style face="normal" font="default" size="100%">International Journal of Biological Macromolecules</style></secondary-title></titles><dates><year><style  face="normal" font="default" size="100%">2018</style></year><pub-dates><date><style  face="normal" font="default" size="100%">NOV</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">119</style></volume><pages><style face="normal" font="default" size="100%">1154-1163</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">The present work aims to determine the effect of pioglitazone on in-vitro albumin glycation and AGE-RAGE induced oxidative stress and inflammation. Bovine serum albumin was glycated by methylglyoxal in absence or presence of pioglitazone. Glycation markers (fructosamine, carbonyl groups, (l-amyloid aggregation, thiol groups, bilirubin binding capacity and AOPP); protein conformational changes (native-PAGE and HPLC analysis) were determined. Cellular study was done by estimating antioxidants, ROS levels, expression profile of membrane RAGE, NF-kappa B and levels of inflammatory cytokines (IL-6, TNF-alpha) using HEK-293 cell line. We observed that levels of glycation markers were reduced at higher concentration of pioglitazone as compared to glycated albumin. Structural analysis of glycated albumin showed inhibition of protein migration and structural changes when treated with pioglitazone. Pioglitazone has potentially restored cellular antioxidants and reduced levels of IL-6 and TNF-alpha by declining expression of membrane RAGE and NF-kappa B. In conclusion, pioglitazone preferentially binds to protein and alleviates protein structural changes by maintaining its integrity. Additionally, it suppresses RAGE and NF-kappa B levels hence alleviate cellular oxidative stress and inflammation. (C) 2018 Elsevier B.V. All rights reserved.</style></abstract><work-type><style face="normal" font="default" size="100%">Article</style></work-type><custom3><style face="normal" font="default" size="100%">Foreign</style></custom3><custom4><style face="normal" font="default" size="100%">3.909</style></custom4></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Nisar, Akib</style></author><author><style face="normal" font="default" size="100%">Ajabia, Devangi K.</style></author><author><style face="normal" font="default" size="100%">Agrawal, Sanskruthi B.</style></author><author><style face="normal" font="default" size="100%">Varma, Sanjana</style></author><author><style face="normal" font="default" size="100%">Chaudhari, Bhushan P.</style></author><author><style face="normal" font="default" size="100%">Tupe, Rashmi S.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Mechanistic insight into differential interactions of iron oxide nanoparticles with native, glycated albumin and their effect on erythrocytes parameters</style></title><secondary-title><style face="normal" font="default" size="100%">International Journal of Biological Macromolecules</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Albumin</style></keyword><keyword><style  face="normal" font="default" size="100%">Glycation</style></keyword><keyword><style  face="normal" font="default" size="100%">iron oxide nanoparticles</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2022</style></year><pub-dates><date><style  face="normal" font="default" size="100%">JUL </style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">212</style></volume><pages><style face="normal" font="default" size="100%">232-247</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;
	Nanoparticles and protein bioconjugates have been studied for multiple biomedical applications. We sought to investigate the interaction and structural modifications of bovine serum albumin (BSA) with iron oxide nanoparticles (IONPs). The IONPs were green synthesized using E. crassipes aqueous leaf extract following characterization using transmission electron microscopy, energy dispersive X-ray analysis and X-ray diffraction. Two different concentrations of native/glycated albumin (0.5 and 1.5 mg/ml) with IONPs were allowed to interact for 1 h at 37 degrees C. Glycation markers, protein modification markers, cellular antioxidant, and hemolysis studies showed structural modifications and conformational changes in albumin due to the presence of IONPs. UV-visible absorbance resulted in hyperchromic and bathochromic effects of IONPs-BSA conjugates. Fluorescence measurements of tyrosine, tryptophan, advanced glycated end products, and ANS binding assay were promising and quenching effects proved IONPs-BSA conjugate formation. In FTIR of BSA-IONPs, transmittance was increased in amide A and B bands while decreased in amide I and II bands. In summary, native PAGE, HPLC, and FTIR analysis displayed a differential behaviour of IONPs with native and glycated BSA. These results provided an understanding of the interaction and structural modifications of glycated and native BSA which may provide fundamental repercussions in future studies.&lt;/p&gt;
</style></abstract><work-type><style face="normal" font="default" size="100%">Article</style></work-type><custom3><style face="normal" font="default" size="100%">&lt;p&gt;
	Foreign&lt;/p&gt;
</style></custom3><custom4><style face="normal" font="default" size="100%">&lt;p&gt;
	8.025&lt;/p&gt;
</style></custom4></record></records></xml>