Results 91 to 100 of about 7,719 (129)

Genetic variation in the choline O-acetyltransferase gene in depression and Alzheimer’s disease: The VITA and Milano studies

Journal of Psychiatric Research, 2011
Linkage studies point to the long arm of chromosome 10 being a susceptibility region for Alzheimer's disease (AD). Additionally, the gene choline O-acetyltransferase (CHAT) located on chromosome 10 was discussed for conveying risk towards AD, but the results are ambiguous.
E. Grünblatt, A. Reif, S. Jungwirth, D. Galimberti, H. Weber, E.A. Scarpini, C. Sauer, I. Wichart, M. K. Rainer, K. Huber, W. Danielczyk, K. H. Tragl, J. Deckert, P. Fischer, P. Riederer   +14 more
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Organization of central cholinergic neurons revealed by combined in situ hybridization histochemistry and choline-O-acetyltransferase immunocytochemistry

Neurochemistry International, 1992
Digoxigenin-labeled riboprobes and in situ hybridization of choline-O-acetyltransferase mRNA, both alone and in combination with immunohistochemical procedures for the synthetic enzyme of acetylcholine, were used to map the topography of putative cholinergic neurons in the rat central nervous system.
L L, Butcher, J D, Oh, N J, Woolf, R H, Edwards, A, Roghani   +4 more
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A comparison of solubilized and membrane bound forms of choline-O-acetyltransferase (EC 2.3.1.6) in mouse brain nerve endings

Brain Research, 1980
Abstract Mouse brain choline-O-acetyltransferase (EC 2.3.1.6) (ChAT) activity was studied in vitro using a 100 mM sodium phosphate buffer (pH 7.4) wash of a crude vesicular fraction containing solubilized ChAT and a washed crude vesicular fraction containing membrane bound ChAT.
C P, Smith, P T, Carroll
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Veratridine-induced breakdown of cytosolic acetylcholine in rat hippocampal minces: An intraterminal form of acetylcholinesterase or choline O-acetyltransferase?

Brain Research, 1986
Rat hippocampal minces were loaded with N-methyl-[3H]acetylcholine ([3H]ACh) in the presence of the 'poorly penetrating' acetylcholinesterase (EC 3.1.1.7, AChE) inhibitor echothiophate and the effect of the depolarizing agent veratridine determined on the subcellular storage and release of [3H]ACh and [3H]choline.
P T, Carroll, M, Badamchian, P, Craig, W H, Lyness   +3 more
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Acetylation of Choline and Homocholine by Membrane‐Bound Choline‐O‐Acetyltransferase in Mouse Forebrain Nerve Endings

Journal of Neurochemistry, 1981
Abstract: The choline analog homocholine is not acetylated in vitro by choline‐O‐acetyltransferase (ChAT, EC 2.3.1.6), which is solubilized by 100 mM‐sodium phosphate buffer washes of a crude vesicular fraction of mouse forebrain. However, both homocholine and choline are acetylated by a form of ChAT which is nonionically associated with a subcellular
C G, Benishin, P T, Carroll
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Multiple Forms of Choline‐O‐Acetyltransferase in Mouse and Rat Brain: Solubilization and Characterization

Journal of Neurochemistry, 1983
Abstract: Three forms of acetyl coenzyme A: choline‐O‐acetyltransferase (EC 2.3.1.6, ChAT) have been isolated from mouse and rat forebrain synaptosomes with a 100 mM sodium phosphate (NaP) buffer of pH 7.4, a high‐salt solution (500 mM NaCl), and a 2% Triton DN‐65 solution, respectively.
C G, Benishin, P T, Carroll
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Membrane-bound choline-O-acetyltransferase in rat hippocampal tissue is associated with synaptic vesicles

Brain Research, 1994
Some of the choline-O-acetyltransferase (EC 2.3.1.6; ChAT) in rat hippocampal nerve terminals is non-ionically associated with membranes. The intent of the present report was to ascertain whether any of this membrane-bound ChAT might be associated with synaptic vesicles.
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Immunological, isoelectric, hydrophobic and molecular weight differences between soluble and ionically membrane-bound fractions of choline-o-acetyltransferase prepared from mouse and rat brain

Neurochemistry International, 1986
Choline-O-acetyltransferase (EC 2.3.1.6; ChAT) was prepared from synaptosomal fractions (P(2)) of mouse and rat brain in the presence of proteolytic inhibitors by the method of Gray and Whittaker (1962) as modified by (Salehmoghaddam and Collier, 1976).
M, Badamchian, K J, Morrow, P T, Carroll
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Soluble and Membrane-bound Forms of Choline-o-Acetyltransferase Activity in the Purely Cholinergic Neurons of Torpedo

1986
The enzyme choline-o-acetyltransferase (EC 2.3.1.6; ChAT), which catalyses the biosynthesis of the neurotransmitter acetylcholine (ACh) from choline and acetylcoenzyme A (AcCoA), was traditionally thought to exist solely in a soluble form in the cytoplasm of cholinergic nerve endings.
L. Eder-Colli, S. Amato, Y. Froment
openaire   +1 more source

SOX2OT inhibition enhances the choline O-Acetyltransferase gene expression in neuronal differentiation model of NT2 cells

Tissue and Cell
This experimental study aimed to investigate the role of SOX2OT in NT2 cell neuronal differentiation to elucidate its specific function in this process, which remains unclear despite previous research highlighting its importance in central nervous system development.We utilized the NT2 cell line to create a constitutive SOX2OT knocked-down cell clone ...
Marie, Saghaeian Jazi, Soroush, Akbar, Saeed, Mohammadi, Lorena, Zentilin   +3 more
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