choline acetyltransferase

And a lack of estrogen could be one reason choline acetyltransferase levels fall in the first place.

Differentiated cells also have choline acetyltransferase and acetyl cholinesterase activities.

He and others pointed out that estrogen also spurred the production of an important enzyme in the brain called choline acetyltransferase.

It stimulates the action of the enzyme choline acetyltransferase, resulting in increased acetylcholine production.

In humans, the choline acetyltransferase enyzme is encoded by the CHAT gene.

Choline acetyltransferase (abbreviated "ChAT") is an enzyme that is synthesized within the body of a neuron.

Organic mercurial compounds, such as methylmercury, have a high affinity for sulfhydryl groups, which causes dysfunction of the enzyme choline acetyltransferase.

Acetylcholine is synthesized in certain neurons by the enzyme choline acetyltransferase from the compounds choline and acetyl-CoA.

Several NVP derivatives have been synthesized and evaluated for their ability to inhibit choline acetyltransferase and protect against nerve toxins.

The role of choline acetyltransferase is to join Acetyl-CoA to choline, resulting in the formation of the neurotransmitter acetylcholine.

However, NVP's method of acetylcholine (ACh) antagonism involves inhibiting the enzyme choline acetyltransferase.

Choline, in combination with acetyl-CoA, is catalyzed by the enzyme choline acetyltransferase to produce acetylcholine and a Coenzyme A byproduct.

However, no data are currently available on the possible coexpression of PLD1 and/or PLD2 and cholinergic markers (e.g. choline acetyltransferase) in vivo.

Acetylcholine is synthesized from choline and a donated acetyl group from acetyl-CoA, by the action of choline acetyltransferase (ChAT).

The liberated choline is taken up again by the pre-synaptic nerve and ACh is synthetized by combining with acetyl-CoA through the action of choline acetyltransferase.

Explaining Brain Impairment Researchers have long known that in those afflicted by Alzheimer's, the level of choline acetyltransferase is anywhere from 60 to 90 percent below what it is in normal people.

The enzyme choline acetyltransferase, important in the signaling between nerve cells in the brain, is decreased as much as 40 to 90 percent below normal in some areas of the brains of Alzheimer's patients.

Several lines of evidence suggest that patients with Alzheimer's disease are deficient in enzymes that regulate the creation and recycling of the major neurotransmitter, acetylcholine (choline acetyltransferase and acetylcholine esterase, respectively).

Diaschisis was originally believed to be a result of disruption to neural tissue, but more recent evidence implicates increased activity levels of choline acetyltransferase, the enzyme responsible for the production of acetylcholine, as a major cause.

It is also used to treat many of the congenital myasthenic syndromes, particularly those with defects in choline acetyltransferase, downstream kinase 7, and those where any kind of defect causes "fast channel" behaviour of the acetylcholine receptor.

Particles containing acetylcholine and its synthesizing enzyme choline acetyltransferase were originally isolated by Hebb and Whittaker (1958) at the Agricultural Research Council, Institute of Animal Physiology, Babraham, Cambridge, UK.

This improvement in cognitive ability in phytoestrogen treated females may be due in part to the increased presence of choline acetyltransferase messenger RNA in the frontal cortex, which has been shown to be associated with protection and enhancement of cognitive function [ 45 ] .

Nucleus basalis of Meynert, abbreviated NBM and also known as the nucleus basalis, is a group of neurons in the substantia innominata of the basal forebrain which has wide projections to the neocortex and is rich in acetylcholine and choline acetyltransferase.