نتایج جستجو برای: Tyrosine hydroxylase
تعداد نتایج: 83974 فیلتر نتایج به سال:
Biogenic amines play an important role in brain metabolism and functioning, participation synaptic transmission as neurotransmitters neuromodulators (dopamine, serotonin, histamine others). Catecholamines are formed from the essential amino acid phenylalanine by hydroxylating it to tyrosine with enzyme phenylalanine-4-hydroxylase, which is subsequently converted dioxyphenylalanine (DOPA) tyrosi...
neuromelanin (nm) pigment accumulates with age in catecholaminergic neurons in man, and the ventral substantia nigra dopaminergic neurons that are the most vulnerable to degeneration in parkinson's disease (pd) contain the greatest amount of this pigment. in vitro data indicate that nm pigment is formed from the excess cytosolic catecholamine that is not accumulated into synaptic vesicles via t...
background: uterine natural killer (unk) cells are the most abundant leukocytes in pre-implantation endometrium and early pregnancy deciduas in humans and rodents. they are associated with structural changes in maternal spiral arteries but regulation of their re-cruitment and activation is incompletely understood. the major subpopulation of unk cells in humans expresses cd56, the neural cell ad...
We have studied the effects of adenosine 3':5'-monophosphate (cAMP)-dependent protein kinase on the phosphorylative and functional modification of bovine adrenal tyrosine hydroxylase. Incubation of partially purified tyrosine hydroxylase with cAMP-dependent protein kinase in the presence of [gamma32P]ATP and 5 micron cAMP led to a 3- to 5-fold activation of tyrosine hydroxylase and to incorpora...
We have studied the effects of adenosine 3’:5’-monophosphate (CAMP)-dependent protein kinase on the phosphorylative and functional modification of bovine adrenal tyrosine hydroxylase. Incubation of partially purified tyrosine hydroxylase with CAMP-dependent protein kinase in the presence of [y-32P]ATP and 5 pM CAMP led to a 3to B-fold activation of tyrosine hydroxylase and to incorporation of [...
Tyrosine hydroxylase catalyses the hydroxylation of L-tyrosine to l-DOPA, the rate-limiting step in the synthesis of catecholamines. Mutations in the TH gene encoding tyrosine hydroxylase are associated with the autosomal recessive disorder tyrosine hydroxylase deficiency, which manifests phenotypes varying from infantile parkinsonism and DOPA-responsive dystonia, also termed type A, to complex...
We have identified a 56-kilodalton protein in cultured bovine adrenal chromaffin cells that is phosphorylated when catecholamine secretion is stimulated. Immunodetection on Western blots from both one- and two-dimensional polyacrylamide gels indicated that this protein was tyrosine hydroxylase, the rate-limiting enzyme in catecholamine biosynthesis. Two-dimensional polyacrylamide gel electropho...
Tyrosine hydroxylase activity is reversibly controlled by the actions of several protein kinases. Previous studies showed that, following phosphorylation by protein kinase A, physiological concentrations of ascorbate irreversibly inactivate tyrosine hydroxylase. Several studies were performed to establish the mechanism of inactivation. We found that inactivation occurred under oxygen-free condi...
We previously reported that a factor(s) from rat choriocarcinoma (Rcho-1) cells suppresses circulating PRL levels and increases tyrosine hydroxylase activity in tuberoinfundibular dopaminergic neurons in vivo. The purposes of this study were to determine whether this factor(s) increases tyrosine hydroxylase activity in fetal hypothalamic cells in vitro and to evaluate its chemical nature. The R...
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