Thomas D


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References (18)

Title : Tumor microenvironment-derived monoacylglycerol lipase provokes tumor-specific immune responses and lipid profiles - Gruden_2023_Prostaglandins.Leukot.Essent.Fatty.Acids_196_102585
Author(s) : Gruden E , Kienzl M , Hasenoehrl C , Sarsembayeva A , Ristic D , Schmid ST , Maitz K , Taschler U , Hahnefeld L , Gurke R , Thomas D , Kargl J , Schicho R
Ref : Prostaglandins Leukot Essent Fatty Acids , 196 :102585 , 2023
Abstract : We recently described that monoacylglycerol lipase (MGL) is present in the tumor microenvironment (TME), increasing tumor growth. In this study we compare the implications of MGL deficiency in the TME in different tumor types. We show that subcutaneous injection of KP (Kras(LSL-G12D)/p53(fl/fl), mouse lung adenocarcinoma) or B16-F10 cells (mouse melanoma) induced tumor growth in MGL wild type (WT) and knockout (KO) mice. MGL deficiency in the TME attenuated the growth of KP cell tumors whereas tumors from B16-F10 cells increased in size. Opposite immune cell profiles were detected between the two tumor types in MGL KO mice. In line with their anti-tumorigenic function, the number of CD8(+) effector T cells and eosinophils increased in KP cell tumors of MGL KO vs. WT mice whereas their presence was reduced in B16-F10 cell tumors of MGL KO mice. Differences were seen in lipid profiles between the investigated tumor types. 2-arachidonoylglycerol (2-AG) content significantly increased in KP, but not B16-F10 cell tumors of MGL KO vs. WT mice while other endocannabinoid-related lipids remained unchanged. However, profiles of phospho- and lysophospholipids, sphingomyelins and fatty acids in KP cell tumors were clearly distinct to those measured in B16-F10 cell tumors. Our data indicate that TME-localized MGL impacts tumor growth, as well as levels of 2-AG and other lipids in a tumor specific manner.
ESTHER : Gruden_2023_Prostaglandins.Leukot.Essent.Fatty.Acids_196_102585
PubMedSearch : Gruden_2023_Prostaglandins.Leukot.Essent.Fatty.Acids_196_102585
PubMedID: 37573716

Title : Endocannabinoids as potential biomarkers: It's all about pre-analytics - Kratz_2021_J.Mass.Spectrom.Adv.Clin.Lab_22_56
Author(s) : Kratz D , Thomas D , Gurke R
Ref : J Mass Spectrom Adv Clin Lab , 22 :56 , 2021
Abstract : INTRODUCTION: Arachidonoyl ethanolamide (AEA) and 2-arachidonoyl glycerol (2-AG) are central lipid mediators of the endocannabinoid system. They are highly relevant due to their involvement in a wide variety of inflammatory, metabolic or malign diseases. Further elucidation of their modes of action and use as biomarkers in an easily accessible matrix, like blood, is restricted by their susceptibility to deviations during blood sampling and physiological co-dependences, which results in high variability of reported concentrations in low ng/mL ranges. OBJECTIVES: The objective of this review is the identification of critical parameters during the pre-analytical phase and proposal of minimum requirements for reliable determination of endocannabinoids (ECs) in blood samples. METHODS: Reported physiological processes influencing the EC concentrations were put into context with published pre-analytical research and stability data from bioanalytical method validation. RESULTS: The cause for variability in EC concentrations is versatile. In part, they are caused by inter-individual factors like sex, metabolic status and/or diurnal changes. Nevertheless, enzymatic activity in freshly drawn blood samples is the main reason for changing concentrations of AEA and 2-AG, besides additional non-enzymatic isomerization of the latter. CONCLUSION: Blood samples for EC analyses require immediate processing at low temperatures (>0 degreesC) to maintain sample integrity. Standardization of the respective blood tube or anti-coagulant, sampling time point, applied centrifugal force and complete processing time can further decrease variability caused by sample handling. Nevertheless, extensive characterization of study participants is needed to reduce distortion of clinical data caused by co-variables and facilitate research on the endocannabinoid system.
ESTHER : Kratz_2021_J.Mass.Spectrom.Adv.Clin.Lab_22_56
PubMedSearch : Kratz_2021_J.Mass.Spectrom.Adv.Clin.Lab_22_56
PubMedID: 34939056

Title : Impact of cholinesterase inhibitors or memantine on survival in adults with Down syndrome and dementia: clinical cohort study - Eady_2018_Br.J.Psychiatry_212_155
Author(s) : Eady N , Sheehan R , Rantell K , Sinai A , Bernal J , Bohnen I , Bonell S , Courtenay K , Dodd K , Gazizova D , Hassiotis A , Hillier R , McBrien J , Mukherji K , Naeem A , Perez-Achiaga N , Sharma V , Thomas D , Walker Z , McCarthy J , Strydom A
Ref : British Journal of Psychiatry , 212 :155 , 2018
Abstract : BACKGROUND: There is little evidence to guide pharmacological treatment in adults with Down syndrome and Alzheimer's disease. Aims To investigate the effect of cholinesterase inhibitors or memantine on survival and function in adults with Down syndrome and Alzheimer's disease. METHOD: This was a naturalistic longitudinal follow-up of a clinical cohort of 310 people with Down syndrome diagnosed with Alzheimer's disease collected from specialist community services in England. RESULTS: Median survival time (5.59 years, 95% CI 4.67-6.67) for those on medication (n = 145, mainly cholinesterase inhibitors) was significantly greater than for those not prescribed medication (n = 165) (3.45 years, 95% CI 2.91-4.13, log-rank test P<0.001). Sequential assessments demonstrated an early effect in maintaining cognitive function. CONCLUSIONS: Cholinesterase inhibitors appear to offer benefit for people with Down syndrome and Alzheimer's disease that is comparable with sporadic Alzheimer's disease; a trial to test the effect of earlier treatment (prodromal Alzheimer's disease) in Down syndrome may be indicated. Declaration of interest A.S. has undertaken consulting for Ono Pharmaceuticals, outside the submitted work. Z.W. has received a consultancy fee and grant from GE Healthcare, outside the submitted work.
ESTHER : Eady_2018_Br.J.Psychiatry_212_155
PubMedSearch : Eady_2018_Br.J.Psychiatry_212_155
PubMedID: 29486820

Title : The oxidized linoleic acid metabolite 12,13-DiHOME mediates thermal hyperalgesia during inflammatory pain - Zimmer_2018_Biochim.Biophys.Acta_1863_669
Author(s) : Zimmer B , Angioni C , Osthues T , Toewe A , Thomas D , Pierre SC , Geisslinger G , Scholich K , Sisignano M
Ref : Biochimica & Biophysica Acta , 1863 :669 , 2018
Abstract : Eicosanoids play a crucial role in inflammatory pain. However, there is very little knowledge about the contribution of oxidized linoleic acid metabolites in inflammatory pain and peripheral sensitization. Here, we identify 12,13-dihydroxy-9Z-octadecenoic acid (12,13-DiHOME), a cytochrome P450-derived linoleic acid metabolite, as crucial mediator of thermal hyperalgesia during inflammatory pain. We found 12,13-DiHOME in increased concentrations in peripheral nervous tissue during acute zymosan- and complete Freund's Adjuvant-induced inflammatory pain. 12,13-DiHOME causes calcium transients in sensory neurons and sensitizes the transient receptor potential vanilloid 1 (TRPV1)-mediated intracellular calcium increases via protein kinase C, subsequently leading to enhanced TRPV1-dependent CGRP-release from sensory neurons. Peripheral injection of 12,13-DiHOME in vivo causes TRPV1-dependent thermal pain hypersensitivity. Finally, application of the soluble epoxide hydrolase (sEH)-inhibitor TPPU reduces 12,13-DiHOME concentrations in nervous tissue and reduces zymosan- and CFA-induced thermal hyperalgesia in vivo. In conclusion, we identify a novel role for the lipid mediator 12,13-DiHOME in mediating thermal hyperalgesia during inflammatory pain and propose a novel mechanism that may explain the antihyperalgesic effects of sEH inhibitors in vivo.
ESTHER : Zimmer_2018_Biochim.Biophys.Acta_1863_669
PubMedSearch : Zimmer_2018_Biochim.Biophys.Acta_1863_669
PubMedID: 29625231
Gene_locus related to this paper: human-EPHX2

Title : The antiidiotypic approach to obtaining a proteolytic antibody -
Author(s) : Smirnov IV , Vorobiev II , Friboulet A , Avalle B , Thomas D , Knorre VD , Gabibov AG , Ponomarenko NA
Ref : Dokl Biochem Biophys , 420 :105 , 2008
PubMedID: 18680902

Title : [A structure-activity study of a catalytic antiidiotypic antibody to the human erythrocyte acetylcholinesterase] - Aleksandrova_2002_Bioorg.Khim_28_118
Author(s) : Aleksandrova ES , Koralevski F , Titov MI , Demin AV , Kozyr AV , Kolesnikov AV , Tramontano A , Paul S , Thomas D , Gabibov AG , Gnuchev NV , Friboulet A
Ref : Bioorganicheskaia Khimiia , 28 :118 , 2002
Abstract : The catalytic monoclonal antibody 9A8 (MA 9A8), antiidiotypic to the antibody AE-2 (MA AE2) produced to the active site of acetyl cholinesterase from human erythrocytes, was subjected to a structure-function study. The specific binding of MA 9A8 to MA AE2 (K 2.26 x 10(9) M-1) was shown by the method of surface plasmon resonance, and the functional activity of MA 9A8 was demonstrated. Unlike acetyl cholinesterase, this antibody specifically reacted with the irreversible phosphonate inhibitors of esterases. A peptide map of MA 9A8 was analyzed by MALDI mass spectrometry. The Ser99 residue of its heavy chain was shown to be within the active site of the catalytic antibody. A computer modeling of the MA 9A8 active site suggested the existence of a catalytic dyad formed by Ser99 and His35. A comparison of the tertiary structures of the MA 9A8 and the 17E8 monoclonal antibody, which also exhibited an esterase activity and was produced to the stable analogue of the reaction transition state, indicated a practically complete coincidence of the structures of their presumed active sites.
ESTHER : Aleksandrova_2002_Bioorg.Khim_28_118
PubMedSearch : Aleksandrova_2002_Bioorg.Khim_28_118
PubMedID: 11962233

Title : Antibody proteases: induction of catalytic response - Gabibov_2002_Biochemistry.(Mosc)_67_1168
Author(s) : Gabibov AG , Friboulet A , Thomas D , Demin AV , Ponomarenko NA , Vorobiev, II , Pillet D , Paon M , Alexandrova ES , Telegin GB , Reshetnyak AV , Grigorieva OV , Gnuchev NV , Malishkin KA , Genkin DD
Ref : Biochemistry (Mosc) , 67 :1168 , 2002
Abstract : Most of the data accumulated throughout the years on investigation of catalytic antibodies indicate that their production increases on the background of autoimmune abnormalities. The different approaches to induction of catalytic response toward recombinant gp120 HIV-1 surface protein in mice with various autoimmune pathologies are described. The peptidylphosphonate conjugate containing structural part of gp120 molecule is used for reactive immunization of NZB/NZW F1, MRL, and SJL mice. The specific modification of heavy and light chains of mouse autoantibodies with Val-Ala-Glu-Glu-Glu-Val-PO(OPh)2 reactive peptide was demonstrated. Increased proteolytic activity of polyclonal antibodies in SJL mice encouraged us to investigate the production of antigen-specific catalytic antibodies on the background of induced experimental autoimmune encephalomyelitis (EAE). The immunization of autoimmune-prone mice with the engineered fusions containing the fragments of gp120 and encephalitogenic epitope of myelin basic protein (MBP(89-104)) was made. The proteolytic activity of polyclonal antibodies isolated from the sera of autoimmune mice immunized by the described antigen was shown. Specific immune response of SJL mice to these antigens was characterized. Polyclonal antibodies purified from sera of the immunized animals revealed proteolytic activity. The antiidiotypic approach to raise the specific proteolytic antibody as an "internal image" of protease is described. The "second order" monoclonal antibodies toward subtilisin Carlsberg revealed pronounced proteolytic activity.
ESTHER : Gabibov_2002_Biochemistry.(Mosc)_67_1168
PubMedSearch : Gabibov_2002_Biochemistry.(Mosc)_67_1168
PubMedID: 12460115

Title : Catalysis of esterolytic reactions by the anti-idiotypic antibody against human erythrocyte acetylcholinesterase -
Author(s) : Alexandrova ES , Koralewski F , Titov MI , Demin AV , Ignatova AN , Kozyr AV , Kolesnikov AV , Tramontano A , Paul S , Thomas D , Gabibov AG , Friboulet A
Ref : Dokl Biochem Biophys , 377 :75 , 2001
PubMedID: 11712155

Title : Enzyme mimicry by the antiidiotypic antibody approach - Kolesnikov_2000_Proc.Natl.Acad.Sci.U.S.A_97_13526
Author(s) : Kolesnikov AV , Kozyr AV , Alexandrova ES , Koralewski F , Demin AV , Titov MI , Avalle B , Tramontano A , Paul S , Thomas D , Gabibov AG , Friboulet A
Ref : Proc Natl Acad Sci U S A , 97 :13526 , 2000
Abstract : The concept of "internal image" of antiidiotypic antibodies has provided the basis for eliciting catalytic antibodies. A monoclonal IgM 9A8 that was obtained as an antiidiotype to AE-2 mAb, a known inhibitor of acetylcholinesterase, displayed esterolytic activity. Study of recombinant Fab fragments and separate light and heavy chains of 9A8 confirmed that the antibody variable domain encodes the catalytic function, whereas neither part of the primary sequence of the Fab exhibited homology with the enzyme. The specific modification of the 9A8 variable domain by an active site-directed covalent inhibitor revealed the presence of an active site Ser residue. A three-dimensional modeling suggests the existence of a functional catalytic dyad Ser-His. Comparison of active sites of 9A8 and 17E8 esterolytic abzyme raised against transition-state analog revealed structural similarity although both antibodies were elicited by two different approaches.
ESTHER : Kolesnikov_2000_Proc.Natl.Acad.Sci.U.S.A_97_13526
PubMedSearch : Kolesnikov_2000_Proc.Natl.Acad.Sci.U.S.A_97_13526
PubMedID: 11095704

Title : Antiidiotypic antibodies as functional internal images of enzyme-active sites -
Author(s) : Friboulet A , Izadyar L , Avalle B , Roseto A , Thomas D
Ref : Annals of the New York Academy of Sciences , 750 :265 , 1995
PubMedID: 7785852

Title : Monoclonal anti-idiotypic antibodies as functional internal images of enzyme active sites: production of a catalytic antibody with a cholinesterase activity - Izadyar_1993_Proc.Natl.Acad.Sci.U.S.A_90_8876
Author(s) : Izadyar L , Friboulet A , Remy MH , Roseto A , Thomas D
Ref : Proceedings of the National Academy of Sciences of the United States of America , 90 :8876 , 1993
Abstract : Monoclonal antibody 9A8 was selected by immunizing mice with AE-2, a monoclonal antibody directed against the active site of acetylcholinesterase. In accordance with the idiotypic network theory, monoclonal anti-idiotypic antibody 9A8 displayed internal-image properties of the original immunogen, the acetylcholinesterase active site. Hydrolysis of acetylthiocholine and related esters of thiocholine by 9A8 follows saturation kinetics and kinetic parameters were determined. The hydrolytic activity is characterized by a lowered kcat value (81 s-1) and an increased Km value (0.6 mM) when compared with the original enzyme. However, the rate acceleration (kcat/kuncat = 4.15 x 10(8) remains higher than for the esterase activities usually described for catalytic antibodies directed against transition-state analogs. The 9A8 activity exhibits a relaxation of specificity toward both substrates and inhibitors. This specificity does not correspond to a known enzymatic activity. The anti-idiotypic approach should be valuable for producing different structural and functional copies of the same enzyme active site. This should allow further insights into structure-activity relationships. Furthermore, use of chemically modified enzymes as immunogens may result in anti-idiotypic antibodies with catalytic activities not found in the native enzymes.
ESTHER : Izadyar_1993_Proc.Natl.Acad.Sci.U.S.A_90_8876
PubMedSearch : Izadyar_1993_Proc.Natl.Acad.Sci.U.S.A_90_8876
PubMedID: 8415624

Title : Reaction-diffusion coupling in a structured system: application to the quantitative simulation of endplate currents - Friboulet_1993_J.Theor.Biol_160_441
Author(s) : Friboulet A , Thomas D
Ref : Journal of Theoretical Biology , 160 :441 , 1993
Abstract : An approach derived from reaction-diffusion problems is introduced to describe the synaptic endplate current (EPC) at the neuromuscular junction. The model constructed borrows heavily from earlier models, but it takes into account the anisotropic distribution of the different elements participating to the generation of EPC. The transmitter acetylcholine (ACh) is released at the presynaptic membrane, diffuses through the cleft where acetylcholinesterase is homogeneously distributed and then reaches the postsynaptic surface where the receptor is located. The system is defined by a series of partial differential equations which are solved by an explicit difference method. The model predicts amplitudes and time constants in agreement with those observed experimentally, in all the conditions of inhibition of the enzyme or the receptor tested.
ESTHER : Friboulet_1993_J.Theor.Biol_160_441
PubMedSearch : Friboulet_1993_J.Theor.Biol_160_441
PubMedID: 8501917

Title : Antiidiotypic antibodies exhibiting an acetylcholinesterase abzyme activity -
Author(s) : Joron L , Izadyar L , Friboulet A , Remy MH , Pancino G , Roseto A , Thomas D
Ref : Annals of the New York Academy of Sciences , 672 :216 , 1992
PubMedID: 1476371

Title : Modulation of lipase hydrolysis and synthesis reactions using carbohydrates - Sanchez-Montero_1991_Biochim.Biophys.Acta_1078_345
Author(s) : Sanchez-Montero JM , Hamon V , Thomas D , Legoy MD
Ref : Biochimica & Biophysica Acta , 1078 :345 , 1991
Abstract : A novel method for modulation of lipase hydrolysis and synthesis lipase was investigated by using carbohydrates in the microenvironment of the Candida rugosa enzyme. The influence of the addition of different sugars to the previously dialysed enzyme was tested on the two reactions. Rates of hydrolysis were lowered by using dialysed enzyme but were increased after sugar addition, regardless of the identity of the added sugar. In contrast, synthesis reaction rates depended on the nature of the carbohydrate. Rates were increased by adding lactose, which is not a water activity depressor, but were lowered by adding fructose, glucose, sucrose or sorbitol, which are all water activity depressors.
ESTHER : Sanchez-Montero_1991_Biochim.Biophys.Acta_1078_345
PubMedSearch : Sanchez-Montero_1991_Biochim.Biophys.Acta_1078_345
PubMedID: 1859825

Title : Poster: Anti-idiotypic antibodies exhibiting an acetylcholinesterase abzyme activity -
Author(s) : Joron L , Friboulet A , Remy MH , Pancino G , Roseto A , Thomas D
Ref : In: Cholinesterases: Structure, Function, Mechanism, Genetics, and Cell Biology , (Massoulie J, Barnard EA, Chatonnet A, Bacou F, Doctor BP, Quinn DM) American Chemical Society, Washington, DC :55 , 1991

Title : Substrate activation and thermal denaturation kinetics of the tetrameric and the trypsin-generated monomeric forms of horse serum butyrylcholinesterase - Cauet_1987_Biochim.Biophys.Acta_912_338
Author(s) : Cauet G , Friboulet A , Thomas D
Ref : Biochimica & Biophysica Acta , 912 :338 , 1987
Abstract : Native horse serum butyrylcholinesterase (acylcholine acylhydrolase; EC is a tetrameric enzyme which can dissociate after a limited proteolysis by trypsin into three additional molecular forms, including the monomeric entity. The trypsin-generated monomer of butyrylcholinesterase, isolated by ultracentrifugation on sucrose gradient, is stable and allows the relations between the polymeric structure of butyrylcholinesterase and its kinetic characteristics to be approached, e.g., substrate activation and complex thermal denaturation curves. The trypsin-generated monomer of butyrylcholinesterase behaves with identical kinetic parameter values as the native tetrameric enzyme. On the other hand, the thermal denaturation of the native tetrameric butyrylcholinesterase does not follow first-order kinetics, but may be described by a sum of exponential terms. This behavior is not due to the polymeric nature of butyrylcholinesterase but seems to be related to a structural heterogeneity induced by the heat treatment.
ESTHER : Cauet_1987_Biochim.Biophys.Acta_912_338
PubMedSearch : Cauet_1987_Biochim.Biophys.Acta_912_338
PubMedID: 3567204

Title : Horse serum butyrylcholinesterase kinetics: a molecular mechanism based on inhibition studies with dansylaminoethyltrimethylammonium - Cauet_1987_Biochem.Cell.Biol_65_529
Author(s) : Cauet G , Friboulet A , Thomas D
Ref : Biochemistry & Cell Biology , 65 :529 , 1987
Abstract : The kinetics of the hydrolysis of butyrylthiocholine by horse serum butyrylcholinesterase (acylcholine acylhydrolase; BCHE; EC exhibit an activation phenomenon at high substrate concentrations. At least two mechanistic models can account for the enzyme kinetics: one assumes the binding of an additional substrate molecule on the acyl-enzyme intermediate, and the other hypothesizes the existence of a peripheral regulatory site for the substrate. (1-Dimethylaminonaphthalene-5-sulfonamidoethyl)-trimethylammonium perchlorate, a potent reversible inhibitor, appears to affect BCHE activity by binding to a peripheral site. The inhibition is of the mixed type at low substrate concentrations and of the competitive type at high substrate concentrations. This is consistent with a peripheral site for the binding of the substrate responsible for the activation phenomenon.
ESTHER : Cauet_1987_Biochem.Cell.Biol_65_529
PubMedSearch : Cauet_1987_Biochem.Cell.Biol_65_529
PubMedID: 3426832

Title : Use of immobilized enzyme coupled with an electrochemical sensor for the detection of organophosphates and carbamates pesticides - Durand_1984_J.Environ.Pathol.Toxicol.Oncol_5_51
Author(s) : Durand P , Thomas D
Ref : J Environ Pathol Toxicol Oncol , 5 :51 , 1984
Abstract : The feasibility of an acetylcholinesterase electrode to detect pesticides is shown. The enzyme electrode is produced by coupling an electrochemical sensor (a slightly modified pH glass electrode) and an enzymic layer. Carbaryl (I) and azinphosethyl (II) are used as examples; typical recordings of the electrode signal and calibration curves are presented. The measurements were taken directly with inhibitor in the presence of substrate (I) or after incubation of the enzymic film (II). The electrode behavior can be modulated by varying the amount of enzyme immobilized in the film and by varying the concentration of substrate used during measurement. For I, the detection level is about 1.0 ppm and I50 = 6 10(-6) M, with acetylcholine as substrate. For II, the detection level is 1 ppm and I50 is dependent on the time of incubation. This new type of pesticide sensor could be used in air and water pollution control and is intended to be complementary to existing analytical methods.
ESTHER : Durand_1984_J.Environ.Pathol.Toxicol.Oncol_5_51
PubMedSearch : Durand_1984_J.Environ.Pathol.Toxicol.Oncol_5_51
PubMedID: 6520739