01416nas a2200253   4500008004100000022001400041245007100055210006900126260011100195300001200306490000700318520052500325653001300850653001200863653001200875653001700887653002600904100002500930700002500955700002600980700002601006700002501032856010501057       2008                        eng d  a0929-866500aAlbumin competitively inhibits glycation of less abundant proteins0 aAlbumin competitively inhibits glycation of less abundant protei  aEXECUTIVE STE Y26, PO BOX 7917, SAIF ZONE, 1200 BR SHARJAH, U ARAB EMIRATESbBENTHAM SCIENCE PUBL LTDcJUL  a663-6670 v153 a<p>Glycation, a non-enzymatic reaction between glucose and protein is the primary cause of diabetic complications. Albumin, the most abundant plasma protein undergoes glycation both in vivo and in vitro. The influence of albumin on glycation of less abundant proteins has not been addressed. For the first time, we show that albumin competitively inhibits the glycation of less abundant proteins. This study suggests that at least in the initial stages of diabetes, albumin may protect other proteins from glycation.</p>10aDiabetes10aglucose10ainsulin10aMALDI-TOF-MS10avascular complication1 aBhonsle, Hemangi, S.1 aSingh, Sameer, Kumar1 aSrivastava, Ghanshyam1 aBoppana, Ramanamurthy1 aKulkarni, Mahesh, J.  uhttps://library.ncl.res.in/content/albumin-competitively-inhibits-glycation-less-abundant-proteins-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