Disease relevance of CHAT

• After 30 days when hypertrophy and heart failure were fully established, choline acetyltransferase was quantified in vitro by a radiochemical assay [1].
• Conversely, activity of choline acetyltransferase, a marker of parasympathetic nervous function, shows transient increases during the development of acute right ventricular hypertrophy [2].
• Approximately 21% of all neurons contained only ChAT with no additional antigen present and are referred to as ChAT/-. Gastric myenteric ganglion cells were not immunoreactive for CALB, PARV, CGRP, or TH [3].
• We have constructed a recombinant retrovirus that expresses choline acetyltransferase (ChAT) by placing the porcine enzyme cDNA under the control of the 5' long terminal repeat of the retroviral vector pMMuLV [4].
• We found a significant increase in the activity of choline acetyltransferase in the sinoatrial node in response to hypoxia after 7 or 14 days [5].

Psychiatry related information on CHAT

• The peroxidase-antiperoxidase immunohistochemical method was then used to demonstrate the localization of choline acetyltransferase in formalin-fixed and paraffin-embedded human cerebellum from normal as well as from Huntington's disease brains [6].

High impact information on CHAT

• Excitatory motor neurons, immunoreactive for choline acetyltransferase, accounted for 20% +/- 3% (n = 6) of descending motor neurons and for 47% +/- 4% of local motor neurons [7].
• Immunoreactivity for choline acetyltransferase was present in 97% of retrogradely labeled nerve cell bodies, reflecting the dominant cholinergic input to the longitudinal muscle layer [8].
• Choline acetyltransferase (ChAT) has been purified from pig brain to greater than 95% homogeneity (purification factor: 646 000, specific activity of the purified enzyme: 128 mumol acetylcholine formed/min/mg) [9].
• The NH2-terminal region of CPTase contains a leucine-proline motif that is shared by carnitine acetyl- and octanoyltransferases and by choline acetyltransferase [10].
• The distribution of choline acetyltransferase (ChoAcTase)-like immunoreactivity in the superior cervical ganglion and the stellate ganglion was analyzed with immunohistochemistry [11].

Chemical compound and disease context of CHAT

• Nitric oxide synthase, choline acetyltransferase, catecholamine enzymes and neuropeptides and their colocalization in the anterior pelvic ganglion, the inferior mesenteric ganglion and the hypogastric nerve of the male guinea pig [12].
• Effect of total or partial uterus extirpation on uterus-projecting neurons in porcine inferior mesenteric ganglion. A. Changes in expression of transmitter-synthesizing enzymes--tyrosine hydroxylase, dopamine beta-hydroxylase and choline acetyltransferase [13].
• The activity of choline acetyltransferase, a neurochemical marker of parasympathetic innervation, and the density of muscarinic cholinergic receptors, measured by the binding of [3H]quinuclidinyl benzilate, were analyzed in the hearts of guinea pigs exposed to hypobaric hypoxia [5].

Biological context of CHAT

• Genomic clones of human and porcine choline acetyltransferase were obtained by screening genomic libraries with synthetic oligonucleotides [14].
• Comparison of the promoter region of the human and porcine choline acetyltransferase genes: localization of an important enhancer region [14].
• Assignment of the choline acetyltransferase gene to porcine chromosome 14q25-27 by fluorescence in situ hybridization [15].
• Molecular genetic approach to the study of mammalian choline acetyltransferase [16].
• Blood vessels from human, cat, pig and bovine retinas were analyzed for their contents of choline acetyltransferase (ChAT) and muscarinic binding sites [17].

Anatomical context of CHAT

• The activity of choline acetyltransferase was markedly elevated in banded animals at 18 weeks (32.6 +/- 2.7 nmol/hr/right ventricle) but returned to baseline by 27 weeks (22.8 +/- 1.4 nmol/hr/right ventricle).(ABSTRACT TRUNCATED AT 250 WORDS)[2]
• Choline acetyltransferase activity, which is rate limiting in acetylcholine biosynthesis, was measured in the four heart chambers of guinea pigs subjected to (1) sham surgery, (2) constriction of the ascending aorta, (3) constriction of the descending thoracic aorta, and (4) constriction of the pulmonary artery [1].
• Neurons with somata >25 microM were studied because 80% of them stained positively for choline acetyltransferase and had electrophysiological characteristics identical to those of cholinergic NB neurons previously recorded in basal forebrain slices [18].
• Nerve growth factor-mediated induction of choline acetyltransferase in PC12 cells: evaluation of the site of action of nerve growth factor and the involvement of lysosomal degradation products of nerve growth factor [19].
• The possible co-localization of choline acetyltransferase (ChAT) and vasoactive intestinal polypeptide (VIP) in the nerve fibers of cat cerebral arteries was examined by a sequential double-labeling immunohistochemical method [20].

Associations of CHAT with chemical compounds

• The enzyme choline acetyltransferase catalyses the biosynthesis of the neurotransmitter acetylcholine and constitutes a specific marker of cholinergic system [16].
• The absence of significant changes in the total amount of the neuronal enzyme, choline acetyltransferase, per ventricle contrasted with the observed increases in the myocardial enzyme, carnitine acetyltransferase [1].
• Diaminobenzidine and tetramethylbenzidine were used as chromogens to distinguish ChAT (protein) and VIP (peptide) immunoreactivities [20].
• PPPFL fixative is more reliable for simultaneously preserving ChAT and VIP immunoreactivities than were periodate-lysine-paraformaldehyde (PLP) fixative, Zamboni's fixative, or 2% paraformaldehyde solution alone [20].
• ChAT was measured by the synthesis of 3H-acetylcholine in the presence of 3H-acetyl CoA and choline [17].

Co-localisations of CHAT

• Choline acetyltransferase-like immunoreactivity (co-localized with enkephalin-like immunoreactivity in the lateral system in the brainstem) and glutamic acid decarboxylase (GAD)-like immunoreactivity have also been found in olivocochlear efferents [21].

Other interactions of CHAT

• The absence of absolute reductions in choline acetyltransferase activity in hypertrophied and failing ventricle contrasts strikingly with the previously reported reductions in tyrosine hydroxylase, which is rate limiting in sympathetic neurotransmitter biosynthesis [1].
• B(2) receptors occupied 82% of the neurons that expressed immunoreactivity for neuropeptide Y, 75% of the neurons that expressed vasoactive intestinal peptide, 84% of the neurons that expressed substance P, 71% of the neurons that expressed choline acetyltransferase, and all neurons that expressed calbindin immunoreactivity [22].
• Boutons of enteric intestinofugal inputs, identified by immunoreactivity to vasoactive intestinal peptide, showed considerable heterogeneity in their immunoreactivity to synaptosome-associated protein of 25 kDa (SNAP-25), synapsin, synaptophysin, choline acetyltransferase, and vesicular acetylcholine transporter [23].
• The nerve fibers in the proximal duodenum contained nerve terminals immunoreactive for choline acetyltransferase, dynorphin, enkephalin, galanin, gastrin-releasing peptide, nitric oxide synthase, substance P, and vasoactive intestinal polypeptide [24].
• Choline acetyltransferase (CAT) was purified to homogeneity from 363 g of human neostriatum by means of ammonium sulfate and protamine sulfate fractionation, followed by chromatography on DEAE-Sephadex, hydroxyapatite, phosphocellulose, and agarose-hexane-Co A columns [25].

Analytical, diagnostic and therapeutic context of CHAT

• Choline acetyltransferase-containing neurons in rodent brain demonstrated by immunohistochemistry [26].
• Immunoprecipitation and double immunodiffusion tests showed that antisera raised against this protein specifically recognize ChAT [9].
• One of them reacted well immunohistochemically with neurons of human brain and also recognized partially purified human placenta ChAT in the ELISA [27].
• We examined this possibility using triple staining for NOS, ChAT and calbindin immunoreactivity and investigated the relationships between calbindin-immunoreactive varicosities and the cell bodies of NOS-immunoreactive neurons, using high-resolution confocal microscopy and electron microscopy [28].
• Applying retrograde neuronal tracing combined with double labelling immunofluorescence, preganglionic nerve cell bodies in the intermediate grey matter of the guinea pig thoracic spinal cord, projecting to the adrenal gland, co-exhibited immunolabelling for choline-acetyltransferase (ChAT) and sometimes, also for leu-enkephalin [29].

References