01656nas a2200253   4500008004100000022001400041245015600055210006900211260009300280300001200373490000700385520069100392653000801083653001901091653001501110653002601125653002301151653001101174100002901185700002501214700002601239700002501265856011201290       2010                        eng d  a1469-066700aDiscovery of rifampicin as a new anti-glycating compound by matrix-assisted laser desorption/ionization mass spectrometry-based insulin glycation assay0 aDiscovery of rifampicin as a new antiglycating compound by matri  a6 CHARLTON MILL, CHARLTON, CHICHESTER,, W SUSSEX PO18 0HY, ENGLANDbIM PUBLICATIONScFEB  a221-2260 v163 a<p>An in vitro insulin glycation assay was developed for screening glycation inhibitors. The assay involves the use of matrix-assisted laser desorption/ionization time-of-flight mass spectrometry for monitoring the formation of glycated insulin. The assay is simple, rapid and amenable for high throughput screening. Using this assay we have discovered a strong anti-glycation activity for the anti-tuberculosis drug rifampicin. These results were compared with bovine serum albumin glucose fluorescence assay. In addition, the IC(50) of rifampicin was lower than that of aminoguanidine, a known anti-glycating agent, suggesting that rifampicin is a more potent glycation inhibitor.</p>10aAGE10aaminoguanidine10aantibiotic10adiabetic complication10adrug repositioning10aIC(50)1 aGolegaonkar, Sandeep, B.1 aBhonsle, Hemangi, S.1 aBoppana, Ramanamurthy1 aKulkarni, Mahesh, J.  uhttps://library.ncl.res.in/content/discovery-rifampicin-new-anti-glycating-compound-matrix-assisted-laser-002107nas a2200301   4500008004100000022001400041245009200055210006900147260007900216300001000295490000700305520106700312653000801379653001301387653002101400653001601421653003401437100002401471700002101495700002501516700002401541700002601565700002201591700002601613700002001639700002501659856012101684       2012                        eng d  a1073-608500aProteomic analysis of glycated proteins from streptozotocin-induced diabetic rat kidney0 aProteomic analysis of glycated proteins from streptozotocininduc  a999 RIVERVIEW DRIVE SUITE 208, TOTOWA, NJ 07512 USAbHUMANA PRESS INCcJAN  a28-380 v503 a<p>Glycation of proteins leading to formation of advanced glycation end products (AGEs) has been considered as one of the important causes of diabetic nephropathy. Therefore, in this study, glycated proteins were detected by anti-AGE antibodies from kidney of streptozotocin-induced diabetic rat showing nephropathic symptoms, by using two dimensional electrophoresis and western blot analysis. These glycated proteins were identified and characterized by using combination of peptide mass finger printing and tandem mass spectrometric approaches. Glycated proteins identified included proteins from metabolic pathways, oxidative stress, cell signaling, and transport. Several of the proteins modified by glycation were involved in glucose metabolism. The extent of glycation was higher in diabetes compared to control, in the glycated proteins that were common to both control and diabetic kidney. Two dimensional electrophoresis proteins profiling of glycated proteins suggest that four of the glycated proteins were significantly up regulated in diabetes.</p>10aAGE10aDiabetes10aGlucose toxicity10aNephropathy10aPost-translation modification1 aChougale, Ashok, D.1 aBhat, Shweta, P.1 aBhujbal, Swapnil, V.1 aZambare, Mandar, R.1 aPuntambekar, Shraddha1 aSomani, Rahul, S.1 aBoppana, Ramanamurthy1 aGiri, Ashok, P.1 aKulkarni, Mahesh, J.  uhttps://library.ncl.res.in/content/proteomic-analysis-glycated-proteins-streptozotocin-induced-diabetic-rat-kidney-0