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-001656nas 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-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<p>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.</p>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<p>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.</p>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-002064nas a2200253   4500008004100000022001400041245013500055210006900190260009300259300001200352490000700364520103800371653004301409653003301452653001301485653003701498100002501535700002301560700002401583700002501607700002301632700002501655856013001680       2012                        eng d  a1469-066700aZoom-in - a targeted database search for identification of glycation modifications analyzed by untargeted tandem mass spectrometry0 aZoomin a targeted database search for identification of glycatio  a6 CHARLTON MILL, CHARLTON, CHICHESTER,, W SUSSEX PO18 0HY, ENGLANDbIM PUBLICATIONScJAN  a475-4810 v183 a<p>Post-translational modifications (PTMs) are very important to biological function, however their identification and characterization is technically challenging. In this study, we have identified glycation modifications by nano LC-MSE, a data independent acquisition work flow, followed by database search using the Protein Lynx Global Server (PLGS). PLGS search with a complete human protein database hardly identified glycation modifications in a glycated human serum albumin (HSA), which was detected to be glycated by western blotting with advanced glycation end products (AGE) antibody and fluorescence spectroscopy. To overcome this difficulty, ``Zoom-In'' approach, a targeted database search was used to identify glycation modifications in a glycated HSA, which were further manually validated. This approach was useful for identification of glycation modifications from untargeted tandem mass spectrometry workflow such as MSE, but may require the development of a new algorithm or an upgrade of the existing software.</p>10aadvanced glycation end products (AGEs)10adata independent acquisition10aDiabetes10apost-translational modifications1 aBhonsle, Hemangi, S.1 aKorwar, Arvind, M.1 aKesavan, Suresh, K.1 aBhosale, Santosh, D.1 aBansode, Sneha, B.1 aKulkarni, Mahesh, J.  uhttps://library.ncl.res.in/content/zoom-targeted-database-search-identification-glycation-modifications-analyzed-untargeted-002342nas a2200205   4500008004100000022001400041245005200055210005000107260011000157300001400267490000600281520163200287100002001919700002501939700002001964700002501984700002102009700002202030856008402052       2013                        eng d  a2046-206900aArsenomics of exiguobacterium sp PS (NCIM 5463)0 aArsenomics of exiguobacterium sp PS NCIM 5463  aTHOMAS GRAHAM HOUSE, SCIENCE PARK, MILTON RD, CAMBRIDGE CB4 0WF, CAMBS, ENGLANDbROYAL SOC CHEMISTRYcAPR  a9705-97130 v33 a<p>In the present study, arsenate [As(V)] tolerant organisms were isolated from a metal contaminated site, and identified by 16S rDNA sequencing as Exiguobacterium sp. Arsenomics (omics of arsenic response) in Exiguobacterium sp. PS via two-dimensional gel electrophoresis (2-DGE) coupled with identification of proteins using MALDI-TOF MS, MALDI-TOF MS/MS and LC/MSE are studied vide this paper. Out of 2460 Coomassie stained proteins, 270 were differentially expressed (p &lt; 0.05). Considering the resolution and abundance level, 45 spots (proteins) were subjected to MALDI-TOF MS/MS, MALDI-TOF/TOF and LC/MSE. Out of these, 33 were identified and categorized into several functional categories (including both known and novel/putative stress responsive proteins) viz., carbohydrate and energy metabolism, stress response, motility, amino acid, and purine and protein synthesis. The identifications of unique proteins, phosphate ABC transporter ATPase subunit and pyridine nucleotide disulfide oxidoreductase, are the significant findings of the present study which may be used as markers of As(V) stress in Exiguobacterium sp. PS. The absence of As(V) reductase activity and non-amplification of the arsC gene of the ars operon suggests that the classical mechanism of As(V) resistance may not be operating in Exiguobacterium sp. PS. Lastly, considering the fact that proteomic studies under As(V) stress were performed only in Gram negative organisms, this study is the first comprehensive endeavour to explore the mechanism of As(V) response in Gram positive organisms, Exiguobacterium sp. PS at the proteomic level.</p>1 aSacheti, Poonam1 aBhonsle, Hemangi, S.1 aPatil, Rajendra1 aKulkarni, Mahesh, J.1 aSrikanth, Rapole1 aGade, Wasudeo, N.  uhttps://library.ncl.res.in/content/arsenomics-exiguobacterium-sp-ps-ncim-5463-001301nas a2200241   4500008004100000022001400041245005300055210005200108260007500160300001200235490000600247520057000253653001000823653001300833653001400846653000900860100002500869700002300894700001600917700002500933700002000958856008100978       2013                        eng d  a1862-834600aGlycated proteome: from reaction to intervention0 aGlycated proteome from reaction to intervention  aPOSTFACH 101161, 69451 WEINHEIM, GERMANYbWILEY-V C H VERLAG GMBHcJAN  a155-1700 v73 a<p>Glycation, a nonenzymatic reaction between reducing sugars and proteins, is a proteome wide phenomenon, predominantly observed in diabetes due to hyperglycemia. Glycated proteome of plasma, kidney, lens, and brain are implicated in the pathogenesis of various diseases, including diabetic complications, neurodegenerative diseases, cancer, and aging. This review discusses the strategies to characterize protein glycation, its functional implications in different diseases, and intervention strategies to protect the deleterious effects of protein glycation.</p>10aaging10aDiabetes10aGlycation10aRAGE1 aKulkarni, Mahesh, J.1 aKorwar, Arvind, M.1 aMary, Sheon1 aBhonsle, Hemangi, S.1 aGiri, Ashok, P.  uhttps://library.ncl.res.in/content/glycated-proteome-reaction-intervention-002352nas a2200205   4500008004100000022001400041245015300055210006900208260008800277300001000365490000700375520148400382100002301866700002501889700002201914700002201936700003301958700002501991856013002016       2013                        eng d  a1536-231000aProteomic profiling and interactome analysis of ER-positive/HER2/neu negative invasive ductal carcinoma of the breast: towards proteomics biomarkers0 aProteomic profiling and interactome analysis of ERpositiveHER2ne  a140 HUGUENOT STREET, 3RD FL, NEW ROCHELLE, NY 10801 USAbMARY ANN LIEBERT, INCcJAN  a27-400 v173 a<p>Breast cancer, especially ER positive/HER2/neu negative IDC, is the predominant subtype of invasive ductal carcinoma. Although proteomic approaches have been used towards biomarker discovery in clinical breast cancer, ER positive/HER2/neu negative IDC is the least studied subtype. To discover biomarkers, as well as to understand the molecular events associated with disease progression of estrogen receptor positive/HER2/neu negative subtype of invasive ductal carcinoma, differential protein expression profiling was performed by using LC-MSE (MS at elevated energy). A total of 118 proteins were identified, of which 26 were differentially expressed. These identified proteins were functionally classified and their interactions and coexpression were analyzed by using bioinformatic tools PANTHER (Protein Analysis THrough Evolutionary Relationships) and STRING (Search Tool for the Retrieval of Interacting Genes). These proteins were found to be upregulated and were involved in cytoskeletal organization, calcium binding, and stress response. Interactions of annexin A5, actin, S100 A10, glyceraldehyde 3 phosphate dehydrogenase, superoxide dismutase 1, apolipoprotein, fibrinogen, and heat shock proteins were prominent. Differential expression of these proteins was validated by two-dimensional gel electrophoresis and Western blot analysis. The cluster of these proteins may serve as a signature profile for estrogen receptor positive/ HER2/neu negative subtype.</p>1 aKorwar, Arvind, M.1 aBhonsle, Hemangi, S.1 aGhole, Vikram, S.1 aGawai, Kachru, R.1 aKoppikar, Chaitanyananda, B.1 aKulkarni, Mahesh, J.  uhttps://library.ncl.res.in/content/proteomic-profiling-and-interactome-analysis-er-positiveher2neu-negative-invasive-ductal-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<p>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; &gt;8%) and non-diabetic control (ND;&lt;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.</p>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-002477nas a2200325   4500008004100000022001400041245009500055210006900150260005700219300001400276490000700290520142400297653001201721653002001733653001501753653001101768653002001779100002001799700002001819700001701839700002501856700002101881700002001902700002201922700001901944700002501963700002101988700002202009856012002031       2014                        eng d  a0175-759800aProteomics of arsenic stress in the gram-positive organism Exiguobacterium sp PS NCIM 54630 aProteomics of arsenic stress in the grampositive organism Exiguo  a233 SPRING ST, NEW YORK, NY 10013 USAbSPRINGERcAUG  a6761-67730 v983 a<p>The general responses of microorganisms to environmental onslaughts are modulated by altering the gene expression pattern to reduce damage in the cell and produce compensating stress responses. The present study attempts to unravel the response of the Gram-positive Exiguobacterium sp. PS NCIM 5463 in the presence of [As(III)] and arsenate [As(V)] using comparative proteomics via two-dimension gel electrophoresis (2-DE) coupled with identification of proteins using matrix-assisted laser desorption/ionisation (MALDI-TOF/MALDI-TOF/TOF). Out of 926 Coomassie-stained proteins, 45 were differentially expressed (p &lt; 0.05). Considering the resolution and abundance level, 24 spots (peptides) were subjected to MALDI analysis, identified and categorised into several functional categories, viz., nitrogen metabolism, energy and stress regulators, carbohydrate metabolism, protein synthesis components and others. A functional role of each protein is discussed in Exiguobacterium sp. PS 5463 under arsenic stress and validated at their transcript level using a quantitative real-time polymerase chain reaction. Unlike previous reports that unravel the responses toward arsenic stress in Gram-negative organisms, the present study identified new proteins under arsenic stress in a Gram-positive organism, Exiguobacterium sp. PS NCIM 5463, which could elucidate the physiology of organisms under arsenic stress.</p>
10aArsenic10aExiguobacterium10aproteomics10aStress10aTranscriptomics1 aSacheti, Poonam1 aPatil, Rajendra1 aDube, Ankita1 aBhonsle, Hemangi, S.1 aThombre, Dipalee1 aMarathe, Sayali1 aVidhate, Ravindra1 aWagh, Priyanka1 aKulkarni, Mahesh, J.1 aRapole, Srikanth1 aGade, Wasudeo, N.  uhttps://library.ncl.res.in/content/proteomics-arsenic-stress-gram-positive-organism-exiguobacterium-sp-ps-ncim-546301776nas a2200205   4500008004100000245012700041210006900168260000800237300001400245490000700259520101100266100002301277700002501300700002401325700002001349700002101369700002501390700002401415856013101439       2017                        eng d00aMass spectrometry based identification of galectin-3 interacting proteins potentially involved in lung melanoma metastasis0 aMass spectrometry based identification of galectin3 interacting   cNOV  a2303-23090 v133 aAdhesive interactions between molecules on tumor cells and those on target organs play a key role in organ specific metastasis. Poly-N-acetyl-lactosamine (polyLacNAc) substituted N-oligosaccharides on melanoma cell surface glycoproteins promote lung specific metastasis via galectin-3 by facilitating their arrest and extravasation. This study reports the identification and characterization of galectin-3 interacting proteins using a combination of galectin-3 sepharose affinity and leucoagglutinating phytohemagglutinin (L-PHA) columns. A total of 83 proteins were identified as galectin-3 interacting glycoproteins, of which 35 were constituents of the L-PHA bound fraction, suggesting that these proteins carry polyLacNAc substituted beta 1,6 branched N-glycans. The identities of some of these proteins, like LAMP-1, LAMP-3, basigin, embigin, and alpha 5 and beta 1 Integrin, have been confirmed by western blotting, and functional relevance with respect to metastatic properties has been established.1 aDange, Manohar, C.1 aBhonsle, Hemangi, S.1 aGodbole, Rashmi, K.1 aMore, Shyam, K.1 aBane, Sanjay, M.1 aKulkarni, Mahesh, J.1 aKalraiya, Rajiv, D.  uhttps://library.ncl.res.in/content/mass-spectrometry-based-identification-galectin-3-interacting-proteins-potentially-involved