University Microfilms International 300 N
Total Page:16
File Type:pdf, Size:1020Kb
Load more
Recommended publications
-
An Interactomics Overview of the Human and Bovine Milk Proteome Over Lactation Lina Zhang1, Aalt D
Zhang et al. Proteome Science (2017) 15:1 DOI 10.1186/s12953-016-0110-0 RESEARCH Open Access An interactomics overview of the human and bovine milk proteome over lactation Lina Zhang1, Aalt D. J. van Dijk2,3,4 and Kasper Hettinga1* Abstract Background: Milk is the most important food for growth and development of the neonate, because of its nutrient composition and presence of many bioactive proteins. Differences between human and bovine milk in low abundant proteins have not been extensively studied. To better understand the differences between human and bovine milk, the qualitative and quantitative differences in the milk proteome as well as their changes over lactation were compared using both label-free and labelled proteomics techniques. These datasets were analysed and compared, to better understand the role of milk proteins in development of the newborn. Methods: Human and bovine milk samples were prepared by using filter-aided sample preparation (FASP) combined with dimethyl labelling and analysed by nano LC LTQ-Orbitrap XL mass spectrometry. Results: The human and bovine milk proteome show similarities with regard to the distribution over biological functions, especially the dominant presence of enzymes, transport and immune-related proteins. At a quantitative level, the human and bovine milk proteome differed not only between species but also over lactation within species. Dominant enzymes that differed between species were those assisting in nutrient digestion, with bile salt- activated lipase being abundant in human milk and pancreatic ribonuclease being abundant in bovine milk. As lactation advances, immune-related proteins decreased slower in human milk compared to bovine milk. -
Separation and Quantitation of Water Soluble Cellular Metabolites by Hydrophilic Interaction Chromatography-Tandem Mass Spectrometry Sunil U
Journal of Chromatography A, 1125 (2006) 76–88 Separation and quantitation of water soluble cellular metabolites by hydrophilic interaction chromatography-tandem mass spectrometry Sunil U. Bajad a, Wenyun Lu a, Elizabeth H. Kimball a, Jie Yuan a, Celeste Peterson b, Joshua D. Rabinowitz a,∗ a Lewis-Sigler Institute for Integrative Genomics and Department of Chemistry, Princeton University, Princeton, NJ 08544, USA b Department of Molecular Biology, Princeton University, Princeton, NJ 08544, USA Received 13 January 2006; received in revised form 8 May 2006; accepted 10 May 2006 Available online 6 June 2006 Abstract A key unmet need in metabolomics is the ability to efficiently quantify a large number of known cellular metabolites. Here we present a liquid chromatography (LC)–electrospray ionization tandem mass spectrometry (ESI-MS/MS) method for reliable measurement of 141 metabolites, including components of central carbon, amino acid, and nucleotide metabolism. The selected LC approach, hydrophilic interaction chromatography with an amino column, effectively separates highly water soluble metabolites that fail to retain using standard reversed-phase chromatography. MS/MS detection is achieved by scanning through numerous selected reaction monitoring events on a triple quadrupole instrument. When applied to extracts of Escherichia coli grown in [12C]- versus [13C]glucose, the method reveals appropriate 12C- and 13C-peaks for 79 different metabolites. © 2006 Elsevier B.V. All rights reserved. Keywords: LC–ESI-MS/MS; Escherichia coli; Metabolomics; Metabonomics; Hydrophilic interaction chromatography; Bacteria; Metabolite; metabolism; Triple quadrupole; Mass spectrometry 1. Introduction pounds, likely capture most key metabolic end products and intermediates [5–8]. Thus, a key current need is an assay that The ability to quantify numerous mRNA in parallel using can reliably and efficiently measure these known compounds DNA microarrays has revolutionized biological science, with [9]. -
S-Adenosylmethionine Deficiency and Brain Accumulation of S-Adenosylhomocysteine in Thioacetamide-Induced Acute Liver Failure
nutrients Article S-Adenosylmethionine Deficiency and Brain Accumulation of S-Adenosylhomocysteine in Thioacetamide-Induced Acute Liver Failure Anna Maria Czarnecka , Wojciech Hilgier and Magdalena Zieli ´nska* Department of Neurotoxicology, Mossakowski Medical Research Centre, Polish Academy of Sciences, 5 Pawi´nskiego Street, 02-106 Warsaw, Poland; [email protected] (A.M.C.); [email protected] (W.H.) * Correspondence: [email protected]; Tel.: +48-22-6086470; Fax: +48-22-6086442 Received: 11 June 2020; Accepted: 15 July 2020; Published: 17 July 2020 Abstract: Background: Acute liver failure (ALF) impairs cerebral function and induces hepatic encephalopathy (HE) due to the accumulation of neurotoxic and neuroactive substances in the brain. Cerebral oxidative stress (OS), under control of the glutathione-based defense system, contributes to the HE pathogenesis. Glutathione synthesis is regulated by cysteine synthesized from homocysteine via the transsulfuration pathway present in the brain. The transsulfuration-transmethylation interdependence is controlled by a methyl group donor, S-adenosylmethionine (AdoMet) conversion to S-adenosylhomocysteine (AdoHcy), whose removal by subsequent hydrolysis to homocysteine counteract AdoHcy accumulation-induced OS and excitotoxicity. Methods: Rats received three consecutive intraperitoneal injections of thioacetamide (TAA) at 24 h intervals. We measured AdoMet and AdoHcy concentrations by HPLC-FD, glutathione (GSH/GSSG) ratio (Quantification kit). Results: AdoMet/AdoHcy ratio was reduced in the brain but not in the liver. The total glutathione level and GSH/GSSG ratio, decreased in TAA rats, were restored by AdoMet treatment. Conclusion: Data indicate that disturbance of redox homeostasis caused by AdoHcy in the TAA rat brain may represent a deleterious mechanism of brain damage in HE. -
Integrating Comprehensive Two-Dimensional Gas Chromatography Mass Spectrometry and Parallel Two-Dimensional Liquid Chromatograph
Electronic Supplementary Material (ESI) for Analyst. This journal is © The Royal Society of Chemistry 2019 Integrating Comprehensive Two-dimensional Gas Chromatography Mass Spectrometry and Parallel Two-dimensional Liquid Chromatography Mass Spectrometry for Untargeted Metabolomics Md Aminul Islam Prodhan1,2,3,4, Biyun Shi1,4, Ming Song2,3,6, Liqing He1,2,3,4, Fang Yuan1,2,3,4, Xinmin Yin1,4, Patrick Bohman8 , Craig McClain2,3,5,6,7, Xiang Zhang1,2,3,4,5 1Department of Chemistry, 2University of Louisville Alcohol Research Center, 3University of Louisville Hepatobiology & Toxicology Program, 4Center for Regulatory and Environmental Analytical Metabolomics, 5 Department of Pharmacology & Toxicology, 6 Department of Medicine, University of Louisville, Louisville, KY 40208, USA,7Robley Rex Louisville VAMC, Louisville, Kentucky 40292, USA, 8Thermo Fisher Scientific International Inc., 3000 Lakeside Dr., Bannockburn, IL, 60015, USA *CORRESPONDING AUTHOR Prof. Xiang Zhang, Department of Chemistry, University of Louisville, 2210 South Brook Street, Louisville, KY 40208, USA. Phone: +01 502 852 8878. Fax: +01 502 852 8149. E-mail: [email protected]. 1 Figure S1. Two compounds co-eluted from the first dimension GC but separated by the second dimension GC. (A) is a three-dimensional view, and (B) is a contour plot. 2 Table S1. Data processing parameters used in LECO ChromaTOF software Data processing parameters used in LECO ChromaTOF. Baseline Offset 1 Number of Data Points Averaged for Baseline Auto Smoothing Peak Width for Peak Finding -
Milk Allergen by the Numbers
Milk allergen component testing Bos d4 Milk Bos allergen d5 Bos by the d8 numbers Detect sensitizations to the complete milk protein to create personalized management plans for your patients. High levels of milk IgE may predict the likelihood of sensitivity, but may not be solely predictive of TC 2851 reactions to baked milk or α-lactalbumin allergy duration.1 • Susceptible to heat denaturation2 • HIGHER RISK of reaction to fresh milk1,3 • LOWER RISK of reaction Milk allergen to baked milk1,3,a • Patient likely to “outgrow” component testing milk allergy4 Measurement of specific IgE by blood test that provides objective assessment of sensitization to milk is the first step in discovering your patient’s allergy. Milk allergen component tests can help α-lactalbumin β-lactoglobulin Casein Test interpretations and next steps you determine the likelihood of reaction to baked goods, such as cookies or cheese pizza, as well as • Avoid fresh milk the likelihood of allergy persistence. + + - • Likely to tolerate baked milk products • Baked milk oral food challenge (OFC), Knowing which protein your patient is with a specialist may be appropriate sensitized to can help you develop a + - - • Likely to outgrow allergy management plan.3,5-9 - + - • Avoid all forms of milk +/- +/- + • Unlikely to become tolerant of milk over time • Avoid milk and baked milk products (yogurt, cookies, cakes), as well as products processed with milk (chocolate, sausage, potato chips) % of children with milk allergy 75 do not react to baked milk.3 Bos d4 Bos Bos d5 d8 TC 2852 TC 2853 β-lactoglobulin Casein Determine • Susceptible to heat • Resistant to heat which proteins denaturation2 denaturation3 your patient is • HIGHER RISK of reaction • HIGHER RISK of reaction to fresh milk1,3 to all forms of milk1,3,5 sensitized to. -
Protease-Activated Alpha-2-Macroglobulin Can Inhibit Amyloid Formation Via Two Distinct Mechanisms
University of Wollongong Research Online Faculty of Science, Medicine and Health - Papers: part A Faculty of Science, Medicine and Health 1-1-2013 Protease-activated alpha-2-macroglobulin can inhibit amyloid formation via two distinct mechanisms Amy R. Wyatt University of Wollongong, [email protected] Patrick Constantinescu University of Wollongong, [email protected] Heath Ecroyd University of Wollongong, [email protected] Christopher M. Dobson University of Cambridge Mark R. Wilson University of Wollongong, [email protected] See next page for additional authors Follow this and additional works at: https://ro.uow.edu.au/smhpapers Part of the Medicine and Health Sciences Commons, and the Social and Behavioral Sciences Commons Recommended Citation Wyatt, Amy R.; Constantinescu, Patrick; Ecroyd, Heath; Dobson, Christopher M.; Wilson, Mark R.; Kumita, Janet R.; and Yerbury, Justin J., "Protease-activated alpha-2-macroglobulin can inhibit amyloid formation via two distinct mechanisms" (2013). Faculty of Science, Medicine and Health - Papers: part A. 745. https://ro.uow.edu.au/smhpapers/745 Research Online is the open access institutional repository for the University of Wollongong. For further information contact the UOW Library: [email protected] Protease-activated alpha-2-macroglobulin can inhibit amyloid formation via two distinct mechanisms Abstract α2-Macroglobulin (α2M) is an extracellular chaperone that inhibits amorphous and fibrillar protein aggregation. The reaction of α2M with proteases results in an ‘activated’ conformation, where the proteases become covalently-linked within the interior of a cage-like structure formed by α2M. This study investigates, the effect of activation on the ability of α2M to inhibit amyloid formation by Aβ1–42 and I59T human lysozyme and shows that protease-activated α2M can act via two distinct mechanisms: (i) by trapping proteases that remain able to degrade polypeptide chains and (ii) by a chaperone action that prevents misfolded clients from continuing along the amyloid forming pathway. -
Cysteine, Glutathione, and Thiol Redox Balance in Astrocytes
antioxidants Review Cysteine, Glutathione, and Thiol Redox Balance in Astrocytes Gethin J. McBean School of Biomolecular and Biomedical Science, Conway Institute, University College Dublin, Dublin, Ireland; [email protected]; Tel.: +353-1-716-6770 Received: 13 July 2017; Accepted: 1 August 2017; Published: 3 August 2017 Abstract: This review discusses the current understanding of cysteine and glutathione redox balance in astrocytes. Particular emphasis is placed on the impact of oxidative stress and astrocyte activation on pathways that provide cysteine as a precursor for glutathione. The effect of the disruption of thiol-containing amino acid metabolism on the antioxidant capacity of astrocytes is also discussed. − Keywords: cysteine; cystine; cysteamine; cystathionine; glutathione; xc cystine-glutamate exchanger; transsulfuration 1. Introduction Thiol groups, whether contained within small molecules, peptides, or proteins, are highly reactive and prone to spontaneous oxidation. Free cysteine readily oxidises to its corresponding disulfide, cystine, that together form the cysteine/cystine redox couple. Similarly, the tripeptide glutathione (γ-glutamyl-cysteinyl-glycine) exists in both reduced (GSH) and oxidised (glutathione disulfide; GSSG) forms, depending on the oxidation state of the sulfur atom on the cysteine residue. In the case of proteins, the free sulfhydryl group on cysteines can adopt a number of oxidation states, ranging from disulfides (–S–S–) and sulfenic acids (–SOOH), which are reversible, to the more oxidised sulfinic (–SOO2H) and sulfonic acids (–SOO3H), which are not. These latter species may arise as a result of chronic and/or severe oxidative stress, and generally indicate a loss of function of irreversibly oxidised proteins. Methionine residues oxidise to the corresponding sulfoxide, which can be rescued enzymatically by methionine sulfoxide reductase [1]. -
The Biosynthesis of Cystathionine in Patients with Homocystinuria
Pediat. Res. 2: 149-160 (1968) Cystathionase homoserine cystathionine pyridoxine cystine serine homocystinuria The Biosynthesis of Cystathionine in Patients with Homocystinuria P.W.K.WONG[30], V.SCHWARZ and G.M.KOMROWER Department of Medical Biochemistry, University of Manchester, and the Mental Retardation Unit, Royal Manchester Children's Hospital, Manchester, England Extract The synthesis in rat and normal human liver homogenates of cystathionine from homoserine +cysteine was studied. When cystathionine was used as substrate, cyst(e)ine was formed and incubation of liver homogenate with homoserine-(-cysteine resulted in the formation of cystathionine. Incubation of homogenate prepared from homocystinuric hVer with L-homoserine+DL-cysteine- 3-14G or DL-cysteine-35S resulted in the formation of labelled cystathionine. The identity of cystathio- nine was established in three chromatographic separations. Oral loading with homoserine and cysteine or cystine in two patients with homocystinuria resulted in urinary excretion of cystathionine in amounts similar to that reported in normal human subjects without amino acid loading. Speculation The observation that human and monkey brains contain much larger quantities of cystathionine than those of other species [26] suggests a special relation of this amino acid to the normal development and function of the primate brain. Cystathionine is either absent from or markedly deficient in the brain of untreated homocystinuric patients [2, 9]. Since we have shown that synthesis of cystathionine from homoserine and cysteine does take place in the patient's liver in vitro, supplementation of the diet with homoserine and cysteine may prove effective in raising intracellular cystathionine concentration to- ward the normal, and may possibly improve the prognosis in this disease. -
View a Sample of the Test Results (List of Allergens Tested)
SAMPLE INFORMATION PATIENT INFORMATION Sample ID: Patient ID: Sampling date: 02.02.2021 Name: Approval status: Approved Birth date: Age: 32 Print date: 02.02.2021 ID/MR#: Gender: F Calibration curve: ORDERING PHYSICIAN INFORMATION Ordering physician: Address: London Allergy & Immunology Centre Ltd 1. Summary of positive IgE results Mainly species-specific aeroallergen components Grass pollen Bermuda grass Cyn d 1 Grass group 1 3,9 ISU-E Timothy grass Phl p 1 Grass group 1 13 ISU-E Phl p 4 Berberine bridge enzyme 2,5 ISU-E Phl p 5 Grass group 5 2,6 ISU-E Phl p 6 Grass group 6 0,6 ISU-E Tree pollen Birch Bet v 1 PR-10 protein 11 ISU-E Olive pollen Ole e 1 Common olive group 1 1,3 ISU-E Ole e 9 Beta-1,3-glucanase 0,8 ISU-E Animal Dog Can f 1 Lipocalin 13 ISU-E Can f 2 Lipocalin 6,5 ISU-E Can f 5 Arginine Esterase 26 ISU-E Can f 6 Lipocalin 1,7 ISU-E Horse Equ c 1 Lipocalin 3,6 ISU-E Cat Fel d 1 Uteroglobin 7,8 ISU-E Fel d 4 Lipocalin 0,6 ISU-E Mite D. farinae (HDM) Der f 2 NPC2 family 3,8 ISU-E D. pteronyssinus (HDM) Der p 2 NPC2 family 2,1 ISU-E SAMPLE ID: PATIENT ID: PATIENT NAME: 02.02.2021 Page 1 / 9 Cross-reactive components PR-10 protein Birch Bet v 1 PR-10 protein 11 ISU-E Alder Aln g 1 PR-10 protein 1,3 ISU-E Hazelnut Cor a 1.0401 PR-10 protein 1,9 ISU-E Apple Mal d 1 PR-10 protein 2,5 ISU-E Kiwi Act d 8 PR-10 protein 2,2 ISU-E ISAC Standardized Units (ISU-E) Level < 0.3 Undetectable 0.3 - 0.9 Low 1 - 14.9 Moderate / High Very High SAMPLE ID: PATIENT ID: PATIENT NAME: 02.02.2021 Page 2 / 9 SAMPLE INFORMATION PATIENT INFORMATION Sample ID: Patient ID: Sampling date: 02.02.2021 Name: Approval status: Approved Birth date: Age: 32 Print date: 02.02.2021 ID/MR#: Gender: F Calibration curve: ORDERING PHYSICIAN INFORMATION Ordering physician: Address: London Allergy & Immunology Centre Ltd 2. -
List of 116 Targeted Metabolites
[E-140169] Ver.1.5.0 Table II Target metabolites for CARCINOSCOPE No Annotation KEGG ID No Annotation KEGG ID 1 2,3-Diphosphoglyceric acid C01159 59 Guanosine C00387 2 2-Hydroxyglutaric acid C01087,C02630,C03196 60 Guanosine 5-diphosphate C00035 3 2-Oxoglutaric acid C00026 61 Guanosine 5-monophosphate C00144 4 2-Oxoisovaleric acid C00141 62 Guanosine 5-triphosphate C00044 5 2-Phosphoglyceric acid C00631 63 Histidine C00135,C00768,C06419 6 3-Phosphoglyceric acid C00197 64 Homocysteine C00155 7 6-Phosphogluconic acid C00345 65 Homoserine C00263 8 Acetoacetyl coenzyme A C00332 66 Hydroxymethylglutaroyl coenzyme A C00356 9 Acetyl coenzyme A C00024 67 Hydroxyproline C01015,C01157 10 Adenine C00147 68 Hypoxanthine C00262 11 Adenosine C00212 69 Inosine C00294 12 Adenosine 5-diphosphate C00008 70 Inosine 5-monophosphate C00130 13 Adenosine 5-monophosphate C00020 71 Isocitric acid C00311 14 Adenosine 5-triphosphate C00002 72 Isoleucine C00407,C06418,C16434 15 Adenylosuccinic acid C03794 73 Lactic acid C00186,C00256,C01432 16 ADP-ribose C00301 74 Leucine C00123,C01570,C16439 17 Alanine C00041,C00133,C01401 75 Lysine C00047,C00739,C16440 18 Arginine C00062,C00792 76 Malic acid C00149,C00497,C00711 19 Argininosuccinic acid C03406 77 Malonyl coenzyme A C00083 20 Asparagine C00152,C01905,C16438 78 Methionine C00073,C00855,C01733 21 Asparaginic acid C00049,C00402,C16433 79 Mevalonic acid C00418 22 Betaine C00719 80 N,N -Dimethylglycine C01026 23 Betaine aldehyde C00576 81 N-Acetylglutamic acid C00624 24 Carbamoyl aspartic acid C00438 82 Nicotineamide -
Title: Homocystinuria Caused by Cystathionine Β-Synthase Deficiency Genereview — Terms Used to Describe Sulfur Amino Acids Au
Title: Homocystinuria Caused by Cystathionine β-Synthase Deficiency GeneReview — Terms Used to Describe Sulfur Amino Acids Authors: Sacharow SJ, Picker JD, Levy HL Updated: May 2017 Terms Used to Describe Sulfur Amino Acids Note: The terms used to describe the sulfur amino acids are confusing because homocysteine, the thiol within the methionine metabolic pathway (Homocystinuria Caused by Cystathionine Beta-Synthase Deficiency; see Figure 1) with its free sulfur, readily combines with other thiols (such as another homocysteine or cysteine) to form a disulfide; it is primarily the disulfides that are measured in the standard amino acid analysis. For clarity, Mudd et al [2000] have proposed the following terminology to describe the sulfur amino acid metabolites that are important in homocystinuria and related disorders: Homocysteine (HcyH). A thiol compound: Homocystine (Hcy-Hcy). A symmetric disulfide: Homocysteine-cysteine mixed disulfide (Hcy-Cys). An asymmetric disulfide: Total homocysteine (tHcy). All of the Hcy that is present, including that which is bound to protein, most of which is liberated from disulfide bonding by a specific analysis that requires prior reduction. Total free homocysteine (tfHcy). A measurement sometimes used in following individuals with homocystinuria, calculated by assigning two Hcy's to the amount of free homocystine (Hcy-Hcy), one Hcy to the amount of homocysteine-cysteine mixed disulfide (Hcy-Cys), and adding the amounts. Total free Hcy is distinguished from tHcy, which includes the Hcy that was formerly protein bound. References Mudd SH, Finkelstein JD, Refsum H, Ueland PM, Malinow MR, Lentz SR, Jacobsen DW, Brattstrom L, Wilcken B, Wilcken DE, Blom HJ, Stabler SP, Allen RH, Selhub J, Rosenberg IH. -
ALEX® Allergen List (Extracts and Components)
ALEX® allergen list (extracts and components) POLLEN w211 Wall pellitory rPar j 2 nsLTP 6 w10 White goosefoot TREE POLLEN w100 White goosefoot rChe a 1 Ole e 1-family 2 Code Allergen Source Component Protein Name t19 Acacia MOULD AND YEAST FUNGI t100 Alder Aln g 1 PR-10 protein 1 m229 Alternaria alternata rAlt a 1 Alt a 1-family t101 Alder Aln g 4 Polcalcin 4 t226 Arizona cypress nCup a 1 Pectate lyase 5 m230 Alternaria alternata rAlt a 6 Enolase t25 Ash m218 Aspergillus fumigatus rAsp f 1 Mitogillin Family 2 Peroxysomales t103 Ash rFra e 1 Ole e 1-family m220 Aspergillus fumigatus rAsp f 3 t300 Beech rFag s 1 PR-10 protein 1 protein t215 Birch rBet v 1 PR-10 protein 1 m221 Aspergillus fumigatus rAsp f 4 unknown Mn superoxide t216 Birch rBet v 2 Profilin m222 Aspergillus fumigatus rAsp f 6 t225 Birch rBet v 6 Isoflavon dismutase m2 Cladosporium her- reductase t222 Cypress barum t105 Date tree nPho d 2 Profilin 3 m100 Cladosporium her- rCla h 8 Short-chain dehy- t8 Elm barum drogenase y2 Malassezia sympo- rMala s 5 unknown t4 Hazel t102 Hazel rCor a 1.0103 PR-10 protein 1 dialis t303 Sugi rCry j 1 Pectate Lyase y3 Malassezia sympo- rMala s 6 Cyclophilin t6 Mountain ceder dialis t71 Mulberry y5 Malassezia sympo- rMala s 11 Mn superoxide t224 Olive nOle e 1 Ole e 1-family 2 dialis dismutase t240 Olive rOle e 9 1,3 β Glucanase m1 Penicilium chrysoge- t305 Paper mulberry num t241 Plane tree rPla a 1 Plant invertase MITES AND COCKROACHES t301 Plane tree nPla a 2 Polygalacturonase d70 Acarus siro t302 Plane tree rPla a 3 nsLTP 6 i100 Blatella