Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.1.1.7 (acetylcholinesterase)
 28,390 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Immunoreactivity for two calcium binding proteins, 28 kDa calbindin and parvalbumin, was used to label cells morphologically identical to Cajal-Retzius neurons in the developing visual, prefrontal, sensory-motor and temporal cortex of Old World monkeys. At all fetal ages examined (E110-E155), Cajal-Retzius neurons throughout the cortex were immunoreactive for calbindin as well as being acetylcholinesterase positive. Between E130 and E150, the calbindin-immunoreactive Cajal-Retzius cells in the visual cortex, and a few in other cortical areas, also showed parvalbumin immunoreactivity. A reduced population of immunoreactive Cajal-Retzius cells was detected at birth, and none could be visualized by immunocytochemistry or histochemistry at later postnatal ages. Calbindin and parvalbumin immunoreactivity represents a potentially useful marker for this developmentally regulated population of neurons, and the varied expression of the two proteins suggests that Cajal-Retzius neurons may represent a neurochemically heterogeneous cell population.
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PMID:Cajal-Retzius neurons in developing monkey neocortex show immunoreactivity for calcium binding proteins. 235 29

The synthesizing enzyme, Choline-O-acetyl transferase (ChAT) (EC 2.3.1.6) and the degradation enzyme, acetylcholinesterase (EC 3.1.1.7) for the neurotransmitter acetylcholine, have been anatomically and biochemically characterized in the thymus of the BALB/C mouse. In the present study we continue to analyze the possibility of cholinergic immunomodulation of immune tissues by determining if ChAT is present in the BALB/C mouse spleen. Our enzymatic evaluation of ChAT activity in splenic extracts revealed .05 nmoles/min/mg protein as compared to .1 nmoles/min/mg of protein activity in controls prepared from whole brain extracts. No detectable levels of ChAT activity were observed in the serum. Immunoblotting and immunoprecipitating using the anti ChAT monoclonal antibody, MB16, demonstrated two bands in the brain and one band in the spleen. Membrane bound ChAT in the brain was composed of two subunits with apparent molecular weights of 28 and 50 kDa. The spleen demonstrated only one form of ChAT with an apparent molecular weight of 28 kDa. Immunoprecipitation of the enzyme from both the brain and spleen resulted in a recovery of 59% and 60% of the activity respectively.
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PMID:Characterization of choline O-acetyltransferase (ChAT) in the BALB/C mouse spleen. 796 Apr 63

Organophosphorus (OP) compounds are a diverse chemical group that includes nerve agents and pesticides. They share a common chemical signature that facilitates their binding and adduction of acetylcholinesterase (AChE) within nerve synapses to induce cholinergic toxicity. However, this group diversity results in non-uniform binding and inactivation of other secondary protein targets, some of which may be adducted and protein activity influenced, even when only a relatively minor portion of tissue AChE is inhibited. The determination of individual OP protein binding targets has been hampered by the sensitivity of methods of detection and quantification of protein-pesticide adducts. We have overcome this limitation by the employment of a microchannel plate (MCP) autoradiographic detector to monitor a radiolabelled OP tracer compound. We preincubated rat thymus tissue in vitro with the OP pesticides, azamethiphos-oxon, chlorfenvinphos-oxon, chlorpyrifos-oxon, diazinon-oxon, and malaoxon, and then subsequently radiolabelled the free OP binding sites remaining with 3H-diisopropylfluorophosphate (3H-DFP). Proteins adducted by OP pesticides were detected as a reduction in 3H-DFP radiolabelling after protein separation by one dimensional polyacrylamide gel electrophoresis and quantitative digital autoradiography using the MCP imager. Thymus tissue proteins of molecular weights -28 kDa, 59 kDa, 66 kDa, and 82 kDa displayed responsiveness to adduction by this panel of pesticides. The 59 kDa protein target (previously putatively identified as carboxylesterase I) was only significantly adducted by chlorfenvinphos-oxon (p < 0.001), chlorpyrifos-oxon (p < 0.0001), and diazinon-oxon (p < 0.01), the 66 kDa protein target (previously identified as serum albumin) similarly only adducted by the same three pesticides (p < 0.0001), (p < 0.001), and (p < 0.01), and the 82 kDa protein target (previously identified as acyl peptide hydrolase) only adducted by chlorpyrifos-oxon (p < 0.0001) and diazinon-oxon (p < 0.001), when the average values of tissue AChE inhibition were 30%, 35%, and 32% respectively. The -28 kDa protein target was shown to be heterogeneous in nature and was resolved to reveal nineteen 3H-DFP radiolabelled protein spots by two dimensional polyacrylamide gel electrophoresis and MCP autoradiography. Some of these 3H-DFP proteins spots were responsive to adduction by preincubation with chlorfenvinphos-oxon. In addition, we exploited the useful spatial resolution of the MCP imager (-70 mm) to determine pesticide micolocalisation in vivo, after animal dosing and autoradiography of brain tissue sections. Collectively, MCP autoradiographic imaging provided a means to detect targets of OP pesticides, quantify their sensitivity of adduction relative to tissue AChE inhibition, and highlighted that these common pesticides exhibit specific binding character to protein targets, and therefore their toxicity will need to be evaluated on an individual compound basis. In addition, MCP autoradiography afforded a useful method of visualisation of the localisation of a small radiolabelled tracer within brain tissue.
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PMID:Detection, quantification, and microlocalisation of targets of pesticides using microchannel plate autoradiographic imagers. 2198 13