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  1. Article ; Online: Description and evaluation of a peracetic acid air sampling and analysis method.

    Nordling, John / Kinsky, Owen R / Osorio, Magdalena / Pechacek, Nathan

    Toxicology and industrial health

    2017  Volume 33, Issue 12, Page(s) 922–929

    Abstract: Peracetic acid (PAA) is a corrosive chemical with a pungent odor, which is extensively used in occupational settings and causes various health hazards in exposed workers. Currently, there is no US government agency recommended method that could be ... ...

    Abstract Peracetic acid (PAA) is a corrosive chemical with a pungent odor, which is extensively used in occupational settings and causes various health hazards in exposed workers. Currently, there is no US government agency recommended method that could be applied universally for the sampling and analysis of PAA. Legacy methods for determining airborne PAA vapor levels frequently suffered from cross-reactivity with other chemicals, particularly hydrogen peroxide (H
    MeSH term(s) Air Pollutants, Occupational/analysis ; Chromatography, High Pressure Liquid ; Environmental Monitoring/methods ; Limit of Detection ; Peracetic Acid/analysis
    Chemical Substances Air Pollutants, Occupational ; Peracetic Acid (I6KPI2E1HD)
    Language English
    Publishing date 2017-11-14
    Publishing country England
    Document type Journal Article
    ZDB-ID 56831-4
    ISSN 1477-0393 ; 0748-2337
    ISSN (online) 1477-0393
    ISSN 0748-2337
    DOI 10.1177/0748233717739165
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 2268: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
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  2. Article ; Online: Metformin Scavenges Methylglyoxal To Form a Novel Imidazolinone Metabolite in Humans.

    Kinsky, Owen R / Hargraves, Tiffanie L / Anumol, Tarun / Jacobsen, Neil E / Dai, Jixun / Snyder, Shane A / Monks, Terrence J / Lau, Serrine S

    Chemical research in toxicology

    2016  Volume 29, Issue 2, Page(s) 227–234

    Abstract: Methylglyoxal (MG) is a highly reactive dicarbonyl compound involved in the formation of advanced glycation endproducts (AGE). Levels of MG are elevated in patients with type-2 diabetes mellitus (T2DM), and AGE have been implicated in the progression of ... ...

    Abstract Methylglyoxal (MG) is a highly reactive dicarbonyl compound involved in the formation of advanced glycation endproducts (AGE). Levels of MG are elevated in patients with type-2 diabetes mellitus (T2DM), and AGE have been implicated in the progression of diabetic complications. The antihyperglycemic drug metformin (MF) has been suggested to be a scavenger of MG. The present work examined and characterized unequivocally the resulting scavenged product from the metformin-MG reaction. The primary product was characterized by (1)H, (13)C, 2D-HSQC, and HMBC NMR and tandem mass spectrometry. X-ray diffraction analysis determined the structure of the metformin and MG-derived imidazolinone compound as (E)-1,1-dimethyl-2-(5-methyl-4-oxo-4,5-dihydro-1H-imidazol-2-yl)guanidine (IMZ). A LC-MS/MS multiple reaction monitoring method was developed to detect and quantify the presence of IMZ in metformin-treated T2DM patients. Urine from >90 MF-treated T2DM patients was analyzed, with increased levels of MF directly correlating with elevations in IMZ. Urinary MF was detected in the range of 0.17 μM to 23.0 mM, and simultaneous measurement of IMZ concentrations were in the range of 18.8 nM to 4.3 μM. Since plasma concentrations of MG range from 40 nM to 4.5 μM, the level of IMZ production may be of therapeutic significance. Thus, in addition to lowering hepatic gluconeogenesis, metformin also scavenges the highly reactive MG in vivo, thereby reducing potentially detrimental MG protein adducts, with subsequent reductions in diabetic complications.
    MeSH term(s) Adult ; Aged ; Aged, 80 and over ; Chromatography, High Pressure Liquid ; Crystallography, X-Ray ; Diabetes Mellitus, Type 2/drug therapy ; Diabetes Mellitus, Type 2/pathology ; Female ; Humans ; Hypoglycemic Agents/chemistry ; Hypoglycemic Agents/metabolism ; Hypoglycemic Agents/therapeutic use ; Imidazolines/urine ; Male ; Metformin/chemistry ; Metformin/metabolism ; Metformin/therapeutic use ; Middle Aged ; Molecular Conformation ; Pyruvaldehyde/blood ; Pyruvaldehyde/chemistry ; Tandem Mass Spectrometry ; Young Adult
    Chemical Substances Hypoglycemic Agents ; Imidazolines ; Pyruvaldehyde (722KLD7415) ; Metformin (9100L32L2N)
    Language English
    Publishing date 2016-02-15
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 639353-6
    ISSN 1520-5010 ; 0893-228X
    ISSN (online) 1520-5010
    ISSN 0893-228X
    DOI 10.1021/acs.chemrestox.5b00497
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: Site specific modification of the human plasma proteome by methylglyoxal.

    Kimzey, Michael J / Kinsky, Owen R / Yassine, Hussein N / Tsaprailis, George / Stump, Craig S / Monks, Terrence J / Lau, Serrine S

    Toxicology and applied pharmacology

    2015  Volume 289, Issue 2, Page(s) 155–162

    Abstract: ... modification, dihydroxyimidazolidine (R+72) and hydroimidazolone (R+54) adducts. One of the sites identified ...

    Abstract Increasing evidence identifies dicarbonyl stress from reactive glucose metabolites, such as methylglyoxal (MG), as a major pathogenic link between hyperglycemia and complications of diabetes. MG covalently modifies arginine residues, yet the site specificity of this modification has not been thoroughly investigated. Sites of MG adduction in the plasma proteome were identified using LC-MS/MS analysis in vitro following incubation of plasma proteins with MG. Treatment of plasma proteins with MG yielded 14 putative MG hotspots from five plasma proteins (albumin [nine hotspots], serotransferrin, haptoglobin [2 hotspots], hemopexin, and Ig lambda-2 chain C regions). The search results revealed two versions of MG-arginine modification, dihydroxyimidazolidine (R+72) and hydroimidazolone (R+54) adducts. One of the sites identified was R257 in human serum albumin, which is a critical residue located in drug binding site I. This site was validated as a target for MG modification by a fluorescent probe displacement assay, which revealed significant drug dissociation at 300 μM MG from a prodan-HSA complex (75 μM). Moreover, twelve human plasma samples (six male, six female, with two type 2 diabetic subjects from both genders) were analyzed using multiple reaction monitoring (MRM) tandem mass spectrometry and revealed the presence of the MG-modified albumin R257 peptide. These data provide insights into the nature of the site-specificity of MG modification of arginine, which may be useful for therapeutic treatments that aim to prevent MG-mediated adverse responses in patients.
    MeSH term(s) Arginine ; Binding Sites ; Biomarkers/blood ; Blood Proteins/metabolism ; Chromatography, High Pressure Liquid ; Diabetes Mellitus, Type 2/blood ; Diabetes Mellitus, Type 2/diagnosis ; Female ; High-Throughput Screening Assays ; Humans ; Male ; Peptide Mapping ; Protein Binding ; Protein Carbonylation ; Protein Processing, Post-Translational ; Proteomics/methods ; Pyruvaldehyde/blood ; Serum Albumin/metabolism ; Serum Albumin, Human ; Spectrometry, Mass, Electrospray Ionization ; Tandem Mass Spectrometry
    Chemical Substances ALB protein, human ; Biomarkers ; Blood Proteins ; Serum Albumin ; Pyruvaldehyde (722KLD7415) ; Arginine (94ZLA3W45F) ; Serum Albumin, Human (ZIF514RVZR)
    Language English
    Publishing date 2015-12-01
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 204477-8
    ISSN 1096-0333 ; 0041-008X
    ISSN (online) 1096-0333
    ISSN 0041-008X
    DOI 10.1016/j.taap.2015.09.029
    Database MEDical Literature Analysis and Retrieval System OnLINE

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