نتایج جستجو برای: tyrosine hydroxylase

تعداد نتایج: 83974  

Journal: :The Journal of biological chemistry 1988
L C Griffith H Schulman

Stimulation of rat pheochromocytoma PC12 cells with ionophore A23187, carbachol, or high K+ medium, agents which increase intracellular Ca2+, results in the phosphorylation and activation of tyrosine hydroxylase (Nose, P., Griffith, L. C., and Schulman, H. (1985) J. Cell Biol. 101, 1182-1190). We have identified three major protein kinases in PC12 cells and investigated their roles in the Ca2+-...

Journal: :Hypertension 1988
A L Rauch W G Campbell

To examine the role of the sympathetic nervous system in hypertension, the in vitro activity of tyrosine hydroxylase was examined in one-kidney, one clip (1K1C) and two-kidney, one clip (2K1C) hypertensive rabbits and their respective controls 2 weeks after surgical procedures. The in vitro activity of tyrosine hydroxylase provides a measure of catecholamine synthesis and serves as a biochemica...

Journal: :The Journal of biological chemistry 1987
M Blum B S McEwen J L Roberts

The tuberoinfundibular dopaminergic neurons in the arcuate nucleus of the rat hypothalamus project to the median eminence and release dopamine from the axon terminals into the portal vessels. The released dopamine is transported to the anterior pituitary and acts to inhibit the release of prolactin from lactotrophs. About 50% of the tuberoinfundibular neurons have been shown to have estrogen re...

Journal: :The Journal of biological chemistry 1986
S L Pocotte R W Holz

The phorbol ester 12-O-tetradecanoylphorbol 13-acetate (TPA) caused phosphorylation of phosphoproteins of 56-kDa which co-migrated with and had identical pI values to subunits of tyrosine hydroxylase. The phosphorylation was closely correlated with an increase of [3H]3,4-dihydroxyphenylalanine (DOPA) production which is a reflection of increased tyrosine hydroxylase activity. Only those phorbol...

Journal: :The Journal of biological chemistry 1982
J A Meligeni J W Haycock W F Bennett J C Waymire

Exogenous CAMP, dibutyryl CAMP, and 8-bromocAMP increased catecholamine biosynthesis from ~-[ l Cltyrosine in isolated purified bovine adrenal chromaffin cells. The acceleration of catecholamine biosynthesis occurred rapidly (within 2 min), was concentration dependent, persisted after the exogenous cAMP or cAMP analogue was removed, and dissipated after 30 min of incubation at 37 “C in the abse...

Journal: :Nucleic acids research 1986
P A Moss K E Davies C Boni J Mallet S T Reeders

Tyrosine hydroxylase is the rate-limiting enzyme in catecholamine synthesis; the gene has previously been cloned and localised to the short arm of chromosome 11. Because of the interest in tyrosine hydroxylase as a candidate gene for manic-depressive psychosis and other affective disorders, we carried out family studies to determine the linkage of tyrosine hydroxylase with insulin, beta-globin,...

Journal: :Development 1988
H M Mackey R F Payette M D Gershon

The phenotypically diverse neurones of the enteric nervous system are developmentally derived from precursors that migrate to the bowel from the vagal and sacral regions of the neuraxis. In order to gain insight into the generation of enteric neuronal diversity, we examined the expression of serotonin (5-HT), tyrosine hydroxylase and GABA in vitro. In the mature avian intestine, intrinsic neuro...

Journal: :Journal of applied physiology 2005
Evelyne Gozal Zahoor A Shah Jean-Marc Pequignot Jacqueline Pequignot Leroy R Sachleben Maria F Czyzyk-Krzeska Richard C Li Shang-Z Guo David Gozal

Tyrosine hydroxylase, a hypoxia-regulated gene, may be involved in tissue adaptation to hypoxia. Intermittent hypoxia, a characteristic feature of sleep apnea, leads to significant memory deficits, as well as to cortex and hippocampal apoptosis that are absent after sustained hypoxia. To examine the hypothesis that sustained and intermittent hypoxia induce different catecholaminergic responses,...

Journal: :Journal of neurochemistry 1987
R Roskoski P R Vulliet D B Glass

Tyrosine hydroxylase purified from rat pheochromocytoma was phosphorylated and activated by purified cyclic GMP-dependent protein kinase as well as by cyclic AMP-dependent protein kinase catalytic subunit. The extent of activation was correlated with the degree of phosphate incorporated into the enzyme. Comparable stoichiometric ratios (0.6 mol phosphate/mol tyrosine hydroxylase subunit) were o...

Journal: :Journal of Biological Chemistry 1982

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