tryptophan hydroxylase

The mechanism of action for this is via tryptophan hydroxylase inhibition.

Tryptophan hydroxylase is important for the brain.

Protein Kinase A, for example, can phosphorylate tryptophan hydroxylase, thus increasing its activity.

Tryptophan hydroxylase 1 gene (TPH1) moderates the influence of social support on depressive symptoms in adults.

Serotonin (a neurotransmitter), synthesized via tryptophan hydroxylase.

Tryptophan hydroxylase, an enzyme.

AGN-2979 is a tryptophan hydroxylase inhibitor.

Cells that make serotonin use tryptophan hydroxylase, a chemical reactor which, when combined with tryptophan, forms 5-hydroxytryptamine, otherwise known as serotonin.

OSM-9 controls the biosynthesis of serotonin via regulation of the expression of the enzyme tryptophan hydroxylase.

Serotonin is synthesized from tryptophan by tryptophan hydroxylase, and then further by aromatic acid decarboxylase.

The activity of tryptophan hydroxylase (i.e. the rate at which it converts L-tryptophan into the serotonin precursor L-5-hydroxytryptophan) can be increased when it undergoes phosphorylation.

(Note that normal dietary sources of serotonin precursors may have less than normal effects if tryptophan hydroxylase levels have been reduced by MDMA.)

Dopamine and serotonin concentrations, dopamine and 5HT uptake sites, and tyrosine and tryptophan hydroxylase activities are reduced after the administration of methamphetamine.

Tryptophan hydroxylase 1 (tryptophan 5-monooxygenase), also known as TPH1, is an enzyme which in humans is encoded by the TPH1 gene.

The enzyme Tryptophan hydroxylase 2, also known as TPH2, is an isozyme of Tryptophan hydroxylase found in vertebrates.

In humans, the stimulation of serotonin production by administration of tryptophan has an antidepressant effect and inhibition of tryptophan hydroxylase (e.g. by p-Chlorophenylalanine) may precipitate depression.

This has shown how its structure is very similar to that of phenylalanine hydroxylase and tryptophan hydroxylase; together the three make up a family of homologous aromatic amino acid hydroxylases.

In analogy to the enzymes phenylalanine hydroxylase, tyrosine hydroxylase, tryptophan hydroxylase and nitric oxide synthase, alkylglycerol monooxygenase critically depends on the cofactor tetrahydrobiopterin and iron.

LX1031 was designed to inhibit tryptophan hydroxylase, or TPH, the rate-limiting enzyme for serotonin production found primarily in enterochromaffin, or EC, cells of the gastrointestinal tract.

These studies found reductions in both the rate-limiting serotonin synthetic enzyme, tryptophan hydroxylase, in dorsal raphe and in serotonin transporter (SERT) expression in the cortex.

A suggested explanation for IED is a polymorphism of the gene for tryptophan hydroxylase, which produces a serotonin precursor; this genotype is found more commonly in individuals with impulsive behavior.

In addition, rhythmic regulation of the transcription of "clock controlled" genes such as tryptophan hydroxylase is important in the regulation of overt rhythms downstream of the clock [ 24, 25].

Until the discovery of TPH2 in 2003, serotonin levels in the central nervous system were believed to be regulated by serotonin synthesis in peripheral tissues, in which Tryptophan hydroxylase is the dominant form.

In social anxiety disorder (SAD) an inherited variant of the gene for tryptophan hydroxylase 2 (enzyme that synthesizes the neurotransmitter serotonin) is linked to reduced amygdala activity and greater susceptibility to the placebo effect.

In animals including humans, serotonin is synthesized from the amino acid -tryptophan by a short metabolic pathway consisting of two enzymes: tryptophan hydroxylase (TPH) and amino acid decarboxylase (DDC).