02403nas a2200313 4500008004100000022001400041245010700055210006900162260007100231300001400302490000700316520127100323653004301594653001201637653001201649653003601661100002501697700002301722700002101745700002901766700002401795700002301819700002201842700002001864700002701884700002601911700002501937856012701962 2012 eng d a1535-389300aLow plasma albumin levels are associated with increased plasma protein glycation and HbA1c in diabetes0 aLow plasma albumin levels are associated with increased plasma p a1155 16TH ST, NW, WASHINGTON, DC 20036 USAbAMER CHEMICAL SOCcFEB a1391-13960 v113 a

Albumin is one of the most abundant plasma proteins and is heavily glycated in diabetes. In this study, we have addressed whether variation in the albumin levels influence glycation of plasma proteins and HbA1c. The study was performed in three systems: (1) streptozotocin (STZ)-induced diabetic mice plasma, (2) diabetic clinical plasma, and (3) in vitro glycated plasma. Diabetic mice and clinical plasma samples were categorized as diabetic high albumin plasma (DHAP) and diabetic low albumin plasma (DLAP) on the basis of their albumin levels. For the in vitro experiment, two albumin levels, high albumin plasma (HAP) and low albumin plasma (LAP), were created by differential depletion of plasma albumin. Protein glycation was studied by using a combination of two-dimensional electrophoresis (2DE), Western blotting, and LC-MSE. In both mice and clinical experiments, an increased plasma protein glycation was observed in DLAP than in DHAP. Additionally, plasma albumin levels were negatively correlated with HbA1c. The in vitro experiment with differential depletion of albumin mechanistically showed that the low albumin levels are associated with increased plasma protein glycation and that albumin competes for glycation with other plasma proteins.

10aadvanced glycation end products (AGEs)10aAlbumin10aglucose10apost translational modification1 aBhonsle, Hemangi, S.1 aKorwar, Arvind, M.1 aKote, Sachin, S.1 aGolegaonkar, Sandeep, B.1 aChougale, Ashok, D.1 aShaik, Mahemud, L.1 aDhande, Nitin, L.1 aGiri, Ashok, P.1 aShelgikar, Kishore, M.1 aBoppana, Ramanamurthy1 aKulkarni, Mahesh, J. uhttps://library.ncl.res.in/content/low-plasma-albumin-levels-are-associated-increased-plasma-protein-glycation-and-hba1c-002227nas a2200265 4500008004100000022001400041245014100055210006900196260007300265300001200338490000700350520126500357653001201622653001701634653001401651100001701665700002101682700002201703700001801725700001901743700001701762700002701779700002501806856013001831 2015 eng d a0141-813000aZinc inhibits glycation induced structural, functional modifications in albumin and protects erythrocytes from glycated albumin toxicity0 aZinc inhibits glycation induced structural functional modificati aPO BOX 211, 1000 AE AMSTERDAM, NETHERLANDSbELSEVIER SCIENCE BVcAUG a601-6100 v793 a

The present work aims to investigate the concentration and time dependant effect of zinc on the in vitro non enzymatic modifications of albumin by diabetic levels of glucose. Further, preventive and curative effect of zinc was studied by adding zinc before and after initiation of glycation respectively. Glycation of albumin was done at different concentrations of zinc (125, 250 and 500 mu M) at different time intervals (21,28 and 35 days) with appropriate controls. The antiglycation potential of zinc was assessed by estimating different markers of albumin glycation (fructosamines, carbonyls, bound sugar, AGEs), structural modifications (free amino, thiol group, beta amyloid, native PAGE, ANS binding, fluorescence lifetime decay and CD analysis) and functional properties (antioxidant activity, hemolysis). Zinc at highest concentration (500 mu M) significantly reduced modifications of albumin which was comparable to aminoguanidine and also protected secondary and tertiary structure of albumin after 28 days of incubation. Zinc exhibited significant protective effect on erythrocytes by inhibiting hemolysis. Thus the present study indicate preventive mode of albumin glycation inhibition by zinc. (C) 2015 Elsevier B.V. All rights reserved.

10aAlbumin10aErythrocytes10aGlycation1 aTupe, Rashmi1 aKulkarni, Amruta1 aAdeshara, Krishna1 aSankhe, Neena1 aShaikh, Shamim1 aDalai, Sayli1 aBhosale, Siddharth, H.1 aGaikwad, Sushama, M. uhttps://library.ncl.res.in/content/zinc-inhibits-glycation-induced-structural-functional-modifications-albumin-and-protects-002337nas a2200241 4500008004100000022001400041245015700055210006900212260000900281300001200290490000800302520146900310653001201779653001401791653002901805100001601834700002401850700002801874700001901902700002701921700002101948856012601969 2022 eng d a0141-813000aMechanistic insight into differential interactions of iron oxide nanoparticles with native, glycated albumin and their effect on erythrocytes parameters0 aMechanistic insight into differential interactions of iron oxide cJUL  a232-2470 v2123 a

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.

10aAlbumin10aGlycation10airon oxide nanoparticles1 aNisar, Akib1 aAjabia, Devangi, K.1 aAgrawal, Sanskruthi, B.1 aVarma, Sanjana1 aChaudhari, Bhushan, P.1 aTupe, Rashmi, S. uhttps://library.ncl.res.in/content/mechanistic-insight-differential-interactions-iron-oxide-nanoparticles-native-glycated