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  1. Article ; Online: A method for the efficient evaluation of substrate-based cholinesterase imaging probes for Alzheimer's disease.

    Darvesh, Sultan / Banfield, Scott / Dufour, Maeve / Forrestall, Katrina L / Maillet, Hillary / Reid, G Andrew / Sands, Dane / Pottie, Ian R

    Journal of enzyme inhibition and medicinal chemistry

    2023  Volume 38, Issue 1, Page(s) 2225797

    Abstract: Cholinesterase (ChE) enzymes have been identified as diagnostic markers for Alzheimer disease (AD). Substrate-based probes have been synthesised to detect ChEs but they have not detected changes in ChE distribution associated with AD pathology. Probes ... ...

    Abstract Cholinesterase (ChE) enzymes have been identified as diagnostic markers for Alzheimer disease (AD). Substrate-based probes have been synthesised to detect ChEs but they have not detected changes in ChE distribution associated with AD pathology. Probes are typically screened using spectrophotometric methods with pure enzyme for specificity and kinetics. However, the biochemical properties of ChEs associated with AD pathology are altered. The present work was undertaken to determine whether the Karnovsky-Roots (KR) histochemical method could be used to evaluate probes at the site of pathology. Thirty thioesters and esters were synthesised and evaluated using enzyme kinetic and KR methods. Spectrophotometric methods demonstrated all thioesters were ChE substrates, yet only a few provided staining in the brain with the KR method. Esters were ChE substrates with interactions with brain ChEs. These results suggest that the KR method may provide an efficient means to screen compounds as probes for imaging AD-associated ChEs.
    MeSH term(s) Humans ; Cholinesterases/metabolism ; Alzheimer Disease/diagnostic imaging ; Cholinesterase Inhibitors/chemistry ; Brain ; Acetylcholinesterase/metabolism
    Chemical Substances Cholinesterases (EC 3.1.1.8) ; Cholinesterase Inhibitors ; 2-(N-cyclohexylamino)ethanesulfonic acid (103-47-9) ; Acetylcholinesterase (EC 3.1.1.7)
    Language English
    Publishing date 2023-06-26
    Publishing country England
    Document type Journal Article
    ZDB-ID 2082578-X
    ISSN 1475-6374 ; 1475-6366
    ISSN (online) 1475-6374
    ISSN 1475-6366
    DOI 10.1080/14756366.2023.2225797
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: Butyrylcholinesterase-knockout reduces brain deposition of fibrillar β-amyloid in an Alzheimer mouse model.

    Reid, G Andrew / Darvesh, Sultan

    Neuroscience

    2015  Volume 298, Page(s) 424–435

    Abstract: In Alzheimer's disease (AD), numerous β-amyloid (Aβ) plaques are associated with butyrylcholinesterase (BChE) activity, the significance of which is unclear. A mouse model, containing five human familial AD genes (5XFAD), also develops Aβ plaques with ... ...

    Abstract In Alzheimer's disease (AD), numerous β-amyloid (Aβ) plaques are associated with butyrylcholinesterase (BChE) activity, the significance of which is unclear. A mouse model, containing five human familial AD genes (5XFAD), also develops Aβ plaques with BChE activity. Knock-out of BChE in this model showed diminished fibrillar Aβ plaque deposition, more so in males than females. This suggests that lack of BChE reduces deposition of fibrillar Aβ in AD and this effect may be influenced by sex.
    MeSH term(s) Age Factors ; Alzheimer Disease/genetics ; Alzheimer Disease/pathology ; Amyloid/metabolism ; Amyloid beta-Peptides/metabolism ; Amyloid beta-Protein Precursor/genetics ; Animals ; Brain/metabolism ; Brain/pathology ; Butyrylcholinesterase/genetics ; Butyrylcholinesterase/metabolism ; Female ; Gene Expression Regulation/genetics ; Humans ; Male ; Mice ; Mice, Inbred C57BL ; Mice, Transgenic ; Presenilin-1/genetics
    Chemical Substances Amyloid ; Amyloid beta-Peptides ; Amyloid beta-Protein Precursor ; Presenilin-1 ; Butyrylcholinesterase (EC 3.1.1.8)
    Language English
    Publishing date 2015-07-09
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 196739-3
    ISSN 1873-7544 ; 0306-4522
    ISSN (online) 1873-7544
    ISSN 0306-4522
    DOI 10.1016/j.neuroscience.2015.04.039
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: Synthesis and Preliminary Evaluation of Phenyl 4-123I-Iodophenylcarbamate for Visualization of Cholinesterases Associated with Alzheimer Disease Pathology.

    Macdonald, Ian R / Reid, G Andrew / Pottie, Ian R / Martin, Earl / Darvesh, Sultan

    Journal of nuclear medicine : official publication, Society of Nuclear Medicine

    2016  Volume 57, Issue 2, Page(s) 297–302

    Abstract: Unlabelled: Acetylcholinesterase and butyrylcholinesterase accumulate with brain β-amyloid (Aβ) plaques in Alzheimer disease (AD). The overall activity of acetylcholinesterase is found to decline in AD, whereas butyrylcholinesterase has been found to ... ...

    Abstract Unlabelled: Acetylcholinesterase and butyrylcholinesterase accumulate with brain β-amyloid (Aβ) plaques in Alzheimer disease (AD). The overall activity of acetylcholinesterase is found to decline in AD, whereas butyrylcholinesterase has been found to either increase or remain the same. Although some cognitively normal older adults also have Aβ plaques within the brain, cholinesterase-associated plaques are generally less abundant in such individuals. Thus, brain imaging of cholinesterase activity associated with Aβ plaques has the potential to distinguish AD from cognitively normal older adults, with or without Aβ accumulation, during life. Current Aβ imaging agents are not able to provide this distinction. To address this unmet need, synthesis and evaluation of a cholinesterase-binding ligand, phenyl 4-(123)I-iodophenylcarbamate ((123)I-PIP), is described.
    Methods: Phenyl 4-iodophenylcarbamate was synthesized and evaluated for binding potency toward acetylcholinesterase and butyrylcholinesterase using enzyme kinetic analysis. This compound was subsequently rapidly radiolabeled with (123)I and purified by high-performance liquid chromatography. Autoradiographic analyses were performed with (123)I-PIP using postmortem orbitofrontal cortex from cognitively normal and AD human brains. Comparisons were made with an Aβ imaging agent, 2-(4'-dimethylaminophenyl)-6-(123)I-iodo-imidazo[1,2-a]pyridine ((123)I-IMPY), in adjacent brain sections. Tissues were also stained for Aβ and cholinesterase activity to visualize Aβ plaque load for comparison with radioligand uptake.
    Results: Synthesized and purified PIP exhibited binding to cholinesterases. (123)I was successfully incorporated into this ligand. (123)I-PIP autoradiography with human tissue revealed accumulation of radioactivity only in AD brain tissues in which Aβ plaques had cholinesterase activity. (123)I-IMPY accumulated in brain tissues with Aβ plaques from both AD and cognitively normal individuals.
    Conclusion: Radiolabeled ligands specific for cholinesterases have potential for use in neuroimaging AD plaques during life. The compound herein described, (123)I-PIP, can detect cholinesterases associated with Aβ plaques and can distinguish AD brain tissues from those of cognitively normal older adults with Aβ plaques. Imaging cholinesterase activity associated with Aβ plaques in the living brain may contribute to the definitive diagnosis of AD during life.
    MeSH term(s) Acetylcholinesterase/metabolism ; Alzheimer Disease/diagnostic imaging ; Alzheimer Disease/enzymology ; Amyloid beta-Peptides/metabolism ; Autoradiography ; Brain/diagnostic imaging ; Butyrylcholinesterase/metabolism ; Cholinesterase Inhibitors/metabolism ; Cholinesterases/metabolism ; Humans ; Iodine Radioisotopes ; Isotope Labeling/methods ; Phenylcarbamates/chemical synthesis ; Phenylcarbamates/pharmacokinetics ; Plaque, Amyloid/diagnostic imaging ; Plaque, Amyloid/enzymology ; Radionuclide Imaging ; Radiopharmaceuticals/chemical synthesis ; Radiopharmaceuticals/pharmacokinetics
    Chemical Substances Amyloid beta-Peptides ; Cholinesterase Inhibitors ; Iodine Radioisotopes ; Phenylcarbamates ; Radiopharmaceuticals ; phenyl 4-iodophenylcarbamate ; Acetylcholinesterase (EC 3.1.1.7) ; Butyrylcholinesterase (EC 3.1.1.8) ; Cholinesterases (EC 3.1.1.8)
    Language English
    Publishing date 2016-02
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 80272-4
    ISSN 1535-5667 ; 0097-9058 ; 0161-5505 ; 0022-3123
    ISSN (online) 1535-5667
    ISSN 0097-9058 ; 0161-5505 ; 0022-3123
    DOI 10.2967/jnumed.115.162032
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Zs.A 114: Show issues Location:
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  4. Article ; Online: Thioesters for the in vitro evaluation of agents to image brain cholinesterases.

    Macdonald, Ian R / Jollymore, Courtney T / Reid, G Andrew / Pottie, Ian R / Martin, Earl / Darvesh, Sultan

    Journal of enzyme inhibition and medicinal chemistry

    2013  Volume 28, Issue 3, Page(s) 447–455

    Abstract: Cholinesterases are associated with pathology characteristic of conditions such as Alzheimer's disease and are therefore, considered targets for neuroimaging. Ester derivatives of N-methylpiperidinol are promising potential imaging agents; however, ... ...

    Abstract Cholinesterases are associated with pathology characteristic of conditions such as Alzheimer's disease and are therefore, considered targets for neuroimaging. Ester derivatives of N-methylpiperidinol are promising potential imaging agents; however, methodology is lacking for evaluating these compounds in vitro. Here, we report the synthesis and evaluation of a series of N-methylpiperidinyl thioesters, possessing comparable properties to their corresponding esters, which can be directly evaluated for cholinesterase kinetics and histochemical distribution in human brain tissue. N-methylpiperidinyl esters and thioesters were synthesized and they demonstrated comparable cholinesterase kinetics. Furthermore, thioesters were capable, using histochemical method, to visualize cholinesterase activity in human brain tissue. N-methylpiperidinyl thioesters can be rapidly evaluated for cholinesterase kinetics and visualization of enzyme distribution in brain tissue which may facilitate development of cholinesterase imaging agents for application to conditions such as Alzheimer's disease.
    MeSH term(s) Aged, 80 and over ; Brain/enzymology ; Chemistry Techniques, Synthetic ; Cholinesterases/analysis ; Cholinesterases/metabolism ; Esters/chemistry ; Female ; Humans ; Hydrolysis ; Kinetics ; Molecular Structure ; Neuroimaging/methods
    Chemical Substances Esters ; Cholinesterases (EC 3.1.1.8)
    Language English
    Publishing date 2013-06
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2082578-X
    ISSN 1475-6374 ; 1475-6366
    ISSN (online) 1475-6374
    ISSN 1475-6366
    DOI 10.3109/14756366.2011.647008
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article ; Online: Alzheimer's disease as an autoimmune disorder of innate immunity endogenously modulated by tryptophan metabolites.

    Meier-Stephenson, Felix S / Meier-Stephenson, Vanessa C / Carter, Michael D / Meek, Autumn R / Wang, Yanfei / Pan, Luzhe / Chen, Qiangwei / Jacobo, Sheila / Wu, Fan / Lu, Erhu / Simms, Gordon A / Fisher, Laural / McGrath, Alaina J / Fermo, Virgil / Barden, Christopher J / Clair, Harman D S / Galloway, Todd N / Yadav, Arun / Campágna-Slater, Valérie /
    Hadden, Mark / Reed, Mark / Taylor, Marcia / Kelly, Brendan / Diez-Cecilia, Elena / Kolaj, Igri / Santos, Clarissa / Liyanage, Imindu / Sweeting, Braden / Stafford, Paul / Boudreau, Robert / Reid, G Andrew / Noyce, Ryan S / Stevens, Leanne / Staniszewski, Agnieszka / Zhang, Hong / Murty, Mamidanna R V S / Lemaire, Pascale / Chardonnet, Solenne / Richardson, Christopher D / Gabelica, Valérie / DePauw, Edwin / Brown, Richard / Darvesh, Sultan / Arancio, Ottavio / Weaver, Donald F

    Alzheimer's & dementia (New York, N. Y.)

    2022  Volume 8, Issue 1, Page(s) e12283

    Abstract: Introduction: Alzheimer's disease (AD) is characterized by neurotoxic immuno-inflammation concomitant with cytotoxic oligomerization of amyloid beta (Aβ) and tau, culminating in concurrent, interdependent immunopathic and proteopathic pathogeneses.: ... ...

    Abstract Introduction: Alzheimer's disease (AD) is characterized by neurotoxic immuno-inflammation concomitant with cytotoxic oligomerization of amyloid beta (Aβ) and tau, culminating in concurrent, interdependent immunopathic and proteopathic pathogeneses.
    Methods: We performed a comprehensive series of in silico, in vitro, and in vivo studies explicitly evaluating the atomistic-molecular mechanisms of cytokine-mediated and Aβ-mediated neurotoxicities in AD.  Next, 471 new chemical entities were designed and synthesized to probe the pathways identified by these molecular mechanism studies and to provide prototypic starting points in the development of small-molecule therapeutics for AD.
    Results: In response to various stimuli (e.g., infection, trauma, ischemia, air pollution, depression), Aβ is released as an early responder immunopeptide triggering an innate immunity cascade in which Aβ exhibits both immunomodulatory and antimicrobial properties (whether bacteria are present, or not), resulting in a misdirected attack upon "self" neurons, arising from analogous electronegative surface topologies between neurons and bacteria, and rendering them similarly susceptible to membrane-penetrating attack by antimicrobial peptides (AMPs) such as Aβ. After this self-attack, the resulting necrotic (but not apoptotic) neuronal breakdown products diffuse to adjacent neurons eliciting further release of Aβ, leading to a chronic self-perpetuating autoimmune cycle.  AD thus emerges as a brain-centric autoimmune disorder of innate immunity. Based upon the hypothesis that autoimmune processes are susceptible to endogenous regulatory processes, a subsequent comprehensive screening program of 1137 small molecules normally present in human brain identified tryptophan metabolism as a regulator of brain innate immunity and a source of potential endogenous anti-AD molecules capable of chemical modification into multi-site therapeutic modulators targeting AD's complex immunopathic-proteopathic pathogenesis.
    Discussion:  Conceptualizing AD as an autoimmune disease, identifying endogenous regulators of this autoimmunity, and designing small molecule drug-like analogues of these endogenous regulators represents a novel therapeutic approach for AD.
    Language English
    Publishing date 2022-04-06
    Publishing country United States
    Document type Journal Article
    ZDB-ID 2832891-7
    ISSN 2352-8737 ; 2352-8737
    ISSN (online) 2352-8737
    ISSN 2352-8737
    DOI 10.1002/trc2.12283
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  6. Article ; Online: Synthesis and preliminary evaluation of piperidinyl and pyrrolidinyl iodobenzoates as imaging agents for butyrylcholinesterase.

    Macdonald, Ian R / Reid, G Andrew / Joy, E Eric / Pottie, Ian R / Matte, Gilbert / Burrell, Steven / Mawko, George / Martin, Earl / Darvesh, Sultan

    Molecular imaging and biology

    2010  Volume 13, Issue 6, Page(s) 1250–1261

    Abstract: Purpose: The purpose of this study is to synthesize and evaluate specific agents for molecular imaging of butyrylcholinesterase (BuChE), known to be associated with neuritic plaques and neurofibrillary tangles in Alzheimer's disease (AD). In this study, ...

    Abstract Purpose: The purpose of this study is to synthesize and evaluate specific agents for molecular imaging of butyrylcholinesterase (BuChE), known to be associated with neuritic plaques and neurofibrillary tangles in Alzheimer's disease (AD). In this study, these agents were tested in a normal rat model. The distribution of radiolabel was compared with known BuChE histochemical distribution in the rat brain.
    Procedures: Iodobenzoate esters were synthesized and tested, through spectrophotometric analysis, as specific substrates for BuChE. These compounds were converted to the corresponding (123)I esters from tributyltin intermediates and purified for studies in the rat model. Whole body dynamic scintigraphic images were obtained for biodistribution studies. Autoradiograms of brain sections were obtained and compared to histochemical distribution of the enzyme in this model system.
    Results: The three iodobenzoate esters studied were specific substrates for BuChE. Whole body biodistribution studies with (123)I-labeled compounds showed rapid disappearance from the body while radioactivity was retained in the head region. Brain section autoradiography of animals injected with these labeled compounds indicated that most areas known to contain BuChE corresponded to areas of radioactivity accumulation.
    Conclusion: BuChE-specific radiolabeled iodobenzoates enter the brain and, in general, label areas known to exhibit BuChE activity in histochemical studies. Such molecules may represent a new direction for the development of agents for the molecular imaging of BuChE in the living brain, especially in regions where BuChE-containing neuropathological structures appear in AD.
    MeSH term(s) Acetylcholinesterase/metabolism ; Alzheimer Disease/enzymology ; Alzheimer Disease/pathology ; Amyloid/metabolism ; Animals ; Autoradiography ; Brain/metabolism ; Brain/pathology ; Butyrylcholinesterase/metabolism ; Evaluation Studies as Topic ; Immunohistochemistry ; Iodine Radioisotopes ; Iodobenzoates/chemical synthesis ; Iodobenzoates/chemistry ; Kinetics ; Ligands ; Male ; Molecular Conformation ; Molecular Imaging/methods ; Piperidines/chemical synthesis ; Piperidines/chemistry ; Pyrrolidines/chemical synthesis ; Pyrrolidines/chemistry ; Rats ; Rats, Wistar ; Tissue Distribution ; Trialkyltin Compounds/chemistry
    Chemical Substances Amyloid ; Iodine Radioisotopes ; Iodobenzoates ; Ligands ; Piperidines ; Pyrrolidines ; Trialkyltin Compounds ; tributyltin (4XDX163P3D) ; Acetylcholinesterase (EC 3.1.1.7) ; Butyrylcholinesterase (EC 3.1.1.8)
    Language English
    Publishing date 2010-10-26
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2079160-4
    ISSN 1860-2002 ; 1536-1632
    ISSN (online) 1860-2002
    ISSN 1536-1632
    DOI 10.1007/s11307-010-0448-0
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Zs.A 6468: Show issues Location:
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  7. Article: A significant reduction of the diaphragm in mdx:MyoD-/-(9th) embryos suggests a role for MyoD in the diaphragm development.

    Inanlou, Mohammad R / Dhillon, Gurmohan S / Belliveau, Anne C / Reid, G Andrew M / Ying, Chuyan / Rudnicki, Michael A / Kablar, Boris

    Developmental biology

    2003  Volume 261, Issue 2, Page(s) 324–336

    Abstract: To further investigate the role of MyoD during skeletal myogenesis, we backcrossed mdx mutant mice (lacking dystrophin) with MyoD knock-out mice to obtain viable mice with MyoD allele on a pure mdx background. However, after nine generations of ... ...

    Abstract To further investigate the role of MyoD during skeletal myogenesis, we backcrossed mdx mutant mice (lacking dystrophin) with MyoD knock-out mice to obtain viable mice with MyoD allele on a pure mdx background. However, after nine generations of backcrossing, it was not possible to obtain a viable mdx:MyoD-/- phenotype (designated as: mdx:MyoD-/-(9th)). The compound-mutant embryos were examined just before birth. Essentially normal Myf5-dependent and most of the MyoD-dependent musculature was observed. By contrast, the skeletal muscle compartment of the diaphragm was significantly reduced. The mesenchymal compartment of the diaphragm was intact and no herniations were observed. Other examined organs (e.g., liver, kidney, brain, etc.) showed no histological abnormalities. Pulmonary hypoplasia was determined as the cause of neonatal death. Therefore, using a different approach, our new data supplement our previous findings and suggest an essential role for MyoD in development of skeletal muscle of the diaphragm. The failure of mdx:MyoD-/-(9th) diaphragm to develop normally is not caused by a reduced number of satellite cells, but from the inability of stem cells to progress through the myogenic program. Our data also suggest that functions of MyoD and Myf5 (and the respective muscle precursor cell sub-populations) are not entirely redundant by term, as previously suggested, since Myf5 is not capable of fully substituting for MyoD in the diaphragm development.
    MeSH term(s) Animals ; DNA-Binding Proteins ; Diaphragm/embryology ; Dystrophin/genetics ; Dystrophin/metabolism ; Extremities/embryology ; Genes, Lethal ; Mice ; Mice, Inbred mdx ; Muscle Development/physiology ; Muscle Proteins/metabolism ; Muscle, Skeletal/embryology ; MyoD Protein/genetics ; MyoD Protein/metabolism ; Myogenic Regulatory Factor 5 ; Trans-Activators
    Chemical Substances DNA-Binding Proteins ; Dystrophin ; Muscle Proteins ; Myf5 protein, mouse ; MyoD Protein ; Myogenic Regulatory Factor 5 ; Trans-Activators
    Language English
    Publishing date 2003-09-15
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, P.H.S.
    ZDB-ID 1114-9
    ISSN 1095-564X ; 0012-1606
    ISSN (online) 1095-564X
    ISSN 0012-1606
    DOI 10.1016/s0012-1606(03)00319-1
    Database MEDical Literature Analysis and Retrieval System OnLINE

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