02540nas a2200265 4500008004100000022001400041245014200055210006900197260008000266300001400346490000700360520155100367653002701918653001801945653002801963100001801991700001702009700001902026700001902045700002302064700002402087700001702111700001702128856012902145 2011 eng d a0944-134400aDegradation of tannic acid by cold-adapted klebsiella sp NACASA1 and phytotoxicity assessment of tannic acid and its degradation products0 aDegradation of tannic acid by coldadapted klebsiella sp NACASA1  aTIERGARTENSTRASSE 17, D-69121 HEIDELBERG, GERMANYbSPRINGER HEIDELBERGcAUG a1129-11380 v183 a

The focus of the present study is to know the potential of bacterial isolate for tannic acid degradation at low temperature. Also, we tried to evaluate the suitability of phytotoxicity testing protocol for the determination of tannic acid toxicity. Screening for tannic acid degrading bacterial strains was carried out by using microbial isolation techniques. The 16S rDNA amplicon of the isolate was used to identify the isolate. The effect of different concentrations of tannic acid and its degradation products on germination of Vigna unguiculata was evaluated. The study was carried out to determine total sugar and starch content of the used seeds and even to check the presence of alpha-amylase activity during seed germination. The isolated bacterium was identified as Klebsiella sp NACASA1 and it showed degradation of tannic acid in 40 (+/- 0.85***) h at 15A degrees C and pH 7.0. A gradual decrease in root/shoot length was observed with increasing concentration of tannic acid. There was 95.11 (+/- 0.24**)% inhibition in alpha-amylase activity at 20,000 ppm tannic acid, as compared to control. No such effects were observed on germination, root-shoot length, and alpha-amylase activity with tannic acid degradation products. The results obtained confirmed that tannic acid may act as a toxic agent in plant cells. The simple biodegradation process presented in this study was found to be effective in reducing toxicity of tannic acid. Also, it reveals the potential of soil bacterium to degrade tannic acid at low temperature.

10aCold-adapted bacterium10aPhytotoxicity10aTannic acid degradation1 aJadhav, Umesh1 aKadu, Sudhir1 aThokal, Nilesh1 aPadul, Manohar1 aDawkar, Vishal, V.1 aChougale, Ashok, D.1 aSalve, Abhay1 aPatil, Manoj uhttps://library.ncl.res.in/content/degradation-tannic-acid-cold-adapted-klebsiella-sp-nacasa1-and-phytotoxicity-assessment-001657nas 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-002403nas 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-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

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.

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-002538nas a2200193 4500008004100000022001400041245010300055210006900158260011000227300001400337490000600351520172700357100002502084700002702109700002402136700002502160700002902185856013002214 2013 eng d a1742-206X00aNovel mechanism for antiglycative action of limonene through stabilization of protein conformation0 aNovel mechanism for antiglycative action of limonene through sta aTHOMAS GRAHAM HOUSE, SCIENCE PARK, MILTON RD, CAMBRIDGE CB4 0WF, CAMBS, ENGLANDbROYAL SOC CHEMISTRYcJUN a2463-24720 v93 a

Inhibition of protein glycation is known to ameliorate secondary complications in diabetes. In the present study antiglycative properties of limonene, a natural product, were evaluated using BSA as a model protein. AMG (aminoguanidine) was used as a positive control. Measurement of total AGEs (Advanced Glycation End-products) and specific AGEs revealed that limonene could inhibit protein glycation to the extent of 56.3% and 75.1% respectively at 50 mu M concentration as against 54.4% and 82.2% by AMG at 1 mM. Congo red binding and CD (Circular Dichroism) analysis revealed inhibition of alpha-helix to beta-sheet transition wherein 18.5% beta-sheet structures were observed in glycated BSA (bovine serum albumin) as against 4.9% with limonene. Glycation of protein in the presence of urea was enhanced by 18%, while in the presence of limonene it was reduced by 23% revealing the stabilizing effect of limonene. Electrophoretic mobility was similar to the normal control and a zeta potential value of -12.1 mV as against -15.1 mV in diabetic control was observed. Inhibition of glycation in limonene treated samples was confirmed through LC-MS analysis wherein AGEs such as pentosidine, CML (N-epsilon-(carboxymethyl)lysine), CEL (N-epsilon-(carboxyethyl) lysine), MOLD (methylglyoxal-lysine dimer) and imidazolone observed in glycated samples were absent in limonene treated samples. PatchDock studies revealed that limonene could bind to the major glycation sites IB, IIA and IIB sub domains and AMG to the IIIA sub domain. Thus limonene is a potent protein glycation inhibitor that prevents protein glycation through a novel mechanism of stabilization of protein structure through hydrophobic interactions.

1 aJoglekar, Madhav, M.1 aPanaskar, Shrimant, N.1 aChougale, Ashok, D.1 aKulkarni, Mahesh, J.1 aArvindekar, Akalpita, U. uhttps://library.ncl.res.in/content/novel-mechanism-antiglycative-action-limonene-through-stabilization-protein-conformation-002124nas a2200217 4500008004100000022001400041245008100055210006900136260010300205300001200308490000700320520130500327100002301632700002401655700002201679700002001701700002701721700002501748700002501773856010801798 2013 eng d a1535-947600aProteomic analysis of protease resistant proteins in the diabetic rat kidney0 aProteomic analysis of protease resistant proteins in the diabeti a9650 ROCKVILLE PIKE, BETHESDA, MD 20814-3996 USAbAMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INCcJAN a228-2360 v123 a

Glycation induced protein aggregation has been implicated in the development of diabetic complications and neurodegenerative diseases. These aggregates are known to be resistant to proteolytic digestion. Here we report the identification of protease resistant proteins from the streptozotocin induced diabetic rat kidney, which included enzymes in glucose metabolism and stress response proteins. These protease resistant proteins were characterized to be advanced glycation end products modified and ubiquitinated by immunological and mass spectrometry analysis. Further, diabetic rat kidney exhibited significantly impaired proteasomal activity. The functional analysis of identified physiologically important enzymes showed that their activity was reduced in diabetic condition. Loss of functional activity of these proteins was compensated by enhanced gene expression. Aggregation prone regions were predicted by in silico analysis and compared with advanced glycation end products modification sites. These findings suggested that the accumulation of protein aggregates is an inevitable consequence of impaired proteasomal activity and protease resistance due to advanced glycation end products modification. Molecular & Cellular Proteomics 12: 10.1074/mcp.M112.020651, 228-236, 2013.

1 aBansode, Sneha, B.1 aChougale, Ashok, D.1 aJoshi, Rakesh, S.1 aGiri, Ashok, P.1 aBodhankar, Subhash, L.1 aHarsulkar, Abhay, M.1 aKulkarni, Mahesh, J. uhttps://library.ncl.res.in/content/proteomic-analysis-protease-resistant-proteins-diabetic-rat-kidney-001879nas a2200253 4500008004100000022001400041245011900055210006900174260006300243300001200306490000600318520096300324653001401287653001001301653001501311100002501326700002301351700002401374700002101398700002201419700002701441700002501468856013201493 2013 eng d a1791-299700aProteomic study reveals downregulation of apolipoprotein A1 in plasma of poorly controlled diabetes: a pilot study0 aProteomic study reveals downregulation of apolipoprotein A1 in p aPOB 18179, ATHENS, 116 10, GREECEbSPANDIDOS PUBL LTDcFEB a495-4980 v73 a

Proteomic approaches aid in gaining a better understanding of the pathophysiology of diabetic complications. In view of this, differential protein expression in diabetic plasma samples was studied by a combination of proteomic and western blot analyses. Diabetic plasma samples were categorized based on glycated haemoglobin levels as controlled diabetes (CD; 7-8%), poorly controlled diabetes (PCD; >8%) and non-diabetic control (ND;<6.4%). Two-dimensional electrophoresis and liquid chromatography-mass spectrometry revealed differential expression of proteins including upregulation of fibrinogen and haptoglobin and downregulation of vitamin D binding protein, alpha-1-antitrypsin, transthyretin and apolipoprotein A1 (Apo A1) in diabetic compared with non-diabetic plasma samples. Amongst these proteins, Apo A1 downregulation was prominent in PCD. Downregulation of Apo A1 may serve as an early predictive marker of diabetic complications.

10abiomarker10aHbA1c10aproteomics1 aBhonsle, Hemangi, S.1 aKorwar, Arvind, M.1 aChougale, Ashok, D.1 aKote, Sachin, S.1 aDhande, Nitin, L.1 aShelgikar, Kishore, M.1 aKulkarni, Mahesh, J. uhttps://library.ncl.res.in/content/proteomic-study-reveals-downregulation-apolipoprotein-a1-plasma-poorly-controlled-diabetes-002204nas a2200253 4500008004100000022001400041245009100055210006900146260011000215300001600325490000600341520123900347100002901586700003901615700001801654700002401672700001701696700002301713700002401736700002601760700002101786700002501807856011801832 2016 eng d a2046-206900aMolecules with O-acetyl group protect protein glycation by acetylating lysine residues0 aMolecules with Oacetyl group protect protein glycation by acetyl aTHOMAS GRAHAM HOUSE, SCIENCE PARK, MILTON RD, CAMBRIDGE CB4 0WF, CAMBS, ENGLANDbROYAL SOC CHEMISTRYcJUL a65572-655780 v63 a

Pharmaceutical intervention for reduction of advanced glycation end products (AGEs) is considered as a therapeutic strategy to attenuate the pathogenesis of diabetes. Many molecules have been reported to possess antiglycation activity, one such example is acetylsalicylic acid (aspirin). It protects proteins from glycation by acetylating the lysine residues. Therefore, in this study we have synthesized and screened molecules containing free N-acetyl, O-acetyl and acetophenone groups. All the selected molecules in this study showed glycation inhibition but interestingly, only molecules with O-acetyl but not N-acetyl and acetophenone groups were capable of acetylating lysine residue. Furthermore, we have demonstrated that pre-acetylation or aspirin treatment prior to the induction of diabetes helps in reducing HbA1c and AGE formation in the streptozotocin induced diabetic mice. Hence pre-acetylation may have an additional therapeutic efficacy of reducing AGE levels in vivo. Incorporation of O-acetyl group into anti-diabetic molecules could be a useful strategy, as it may have an additive effect in reducing AGEs. Identification of such novel acetylating agents represents a new area in the drug discovery process.

1 aVannuruswamy, Garikapati1 aJagadeeshaprasad, Mashanipalya, G.1 aKashinath, K.1 aKesavan, Suresh, K.1 aBhat, Shweta1 aKorwar, Arvind, M.1 aChougale, Ashok, D.1 aBoppana, Ramanamurthy1 aReddy, Srinivasa1 aKulkarni, Mahesh, J. uhttps://library.ncl.res.in/content/molecules-o-acetyl-group-protect-protein-glycation-acetylating-lysine-residues03089nas a2200265 4500008004100000022001400041245013700055210006900192260000800261300001400269490000700283520219600290653001602486653001102502653001502513653001502528653002202543653001502565100002302580700002302603700002302626700002102649700002402670856012902694 2018 eng d a0022-114700aNutritional quality and antioxidant activity of wheatgrass (Triticum aestivum) unwrap by proteome profiling and DPPH and FRAP assays0 aNutritional quality and antioxidant activity of wheatgrass Triti cAUG a2127-21390 v833 a

Precious contribution of plants in the field of medicine is very well known. Wheat (Triticum aestivum) seeds and seedlings are an important source of food and feed due to the presence of various health-promoting compounds. Proteomic analysis of three seed developmental stages (0, 8, and 16 days after germination [DAG]) of wheat was carried out using liquid chromatography-mass spectrometry. A total of 297 proteins were identified and their functional annotation revealed that a majority of them were involved in preventing many diseases, oxidative stress, primary metabolism, storage, and energy related mechanisms. Particularly to mention, peroxidases, superoxide dismutases, and cytochromes are abundantly present in wheatgrass. In the ferric-reducing antioxidant power assay, antioxidant activity was increased by 1.55 times after 16 DAG as compared to 0 DAG, however it was decreased after 8 DAG. The antioxidant activity of the plant extracts by DPPH had an increasing trend after all the three time points. The percent radical scavenging activity of extract by DPPH was 15, 22, and 30 after 0, 8, and 16 DAG, respectively. Observations obtained revealed that antioxidant power of the plants is directly proportional to the age of seedlings. Data attained on wheatgrass showing that it can be a strong antioxidant agent due to its free radical scavenging activity and could be used in stress and nourishing human health. Practical ApplicationWheatgrass contains minerals, phytochemicals, active enzymes, and vitamins that can be easily absorbed. The consumption of wheatgrass juice can give better health benefits. Information about beneficial properties of wheat grass juice is clearly mentioned in this work.Proteins found in wheatgrass are known to be involved in preventing many diseases, oxidative stress, primary metabolism, storage, and energy-related mechanisms. Results of this work revealed that Triticum aestivum seedlings can act as an antioxidant agent due to their free radical scavenging activity and can be constructive to control or treat many health complications. From all these results we believed that wheatgrass can be used for the nourishment of humans.

10aAntioxidant10aLC-MSE10aperoxidase10aproteomics10aTriticum aestivum10awheatgrass1 aParit, Santosh, B.1 aDawkar, Vishal, V.1 aTanpure, Rahul, S.1 aPai, Sandeep, R.1 aChougale, Ashok, D. uhttps://library.ncl.res.in/content/nutritional-quality-and-antioxidant-activity-wheatgrass-triticum-aestivum-unwrap-proteome