نتایج جستجو برای: tyrosine hydroxylase

تعداد نتایج: 83974  

Journal: :Journal of neurochemistry 1987
R Roskoski L M Roskoski

Tyrosine hydroxylase, the rate-limiting enzyme in catecholamine biosynthesis, is subject to regulation by a variety of agents. Previous workers have found that cyclic AMP-dependent protein kinase and calcium-stimulated protein kinases activate tyrosine hydroxylase. We wanted to determine whether cyclic GMP might also be involved in the regulation of tyrosine hydroxylase activity. We found that ...

Journal: :Journal of neurochemistry 1991
R Roskoski P Ritchie

The enzyme tyrosine hydroxylase catalyzes the first step in the biosynthesis of dopamine, norepinephrine, and epinephrine. Tyrosine hydroxylase is a substrate for cyclic AMP-dependent protein kinase as well as other protein kinases. We determined the Km and Vmax of rat pheochromocytoma tyrosine hydroxylase for cyclic AMP-dependent protein kinase and obtained values of 136 microM and 7.1 mumol/m...

Journal: :Proceedings of the National Academy of Sciences of the United States of America 1974
X O Breakefield M W Nirenberg

A selection procedure was devised for neurons and related cells that depends upon the ability of the cells to synthesize certain amine neurotransmitters. The rationale for selection is that tyrosine is an essential amino acid for most mammalian cells and that three enzymes from mammalian sources can catalyze the synthesis of tyrosine: phenylalanine hydroxylase (EC 1.14.16.1), tyrosine hydroxyla...

Journal: :Histology and histopathology 1995
C K Tan Y L Zhang W C Wong

The present paper describes tyrosine hydroxylase-like immunoreactivity in the ciliary ganglion of monkey (Macaca fascicularis) and cat. Under the light microscope, in the monkey, about 7.6% of neurons were observed to be intensely stained, 27.7% moderately stained and 32.5% lightly stained. In the cat, 1.2% of neurons were intensely stained, 5.4% moderately stained and 10.1% lightly stained. Ul...

Journal: :The Journal of antibiotics 1968
S Ayukawa T Takeuchi M Sezaki T Hara H Umezawa

Aquayamycin was found to be a strong inhibitor of tyrosine hydroxylase. It inhibits tyrosine hydroxylase by 50 % at 3.7x10~7M. The inhibition is noncompetitive with tyrosine. The inhibition by 4x10~7 Maquayamycin increases when the concentration of 2-amino-4-hydroxy-6,7-dimethyltetrahydropteridine is increased from 2x10~4M to 1x10~3M. The inhibition of tyrosine hydroxylase by aquayamycin is rev...

Journal: :Brain : a journal of neurology 2010
Michèl A Willemsen Marcel M Verbeek Erik-Jan Kamsteeg Johanneke F de Rijk-van Andel Alec Aeby Nenad Blau Alberto Burlina Maria A Donati Ben Geurtz Padraic J Grattan-Smith Martin Haeussler Georg F Hoffmann Hans Jung Johannis B de Klerk Marjo S van der Knaap Fernando Kok Vincenzo Leuzzi Pascale de Lonlay Andre Megarbane Hugh Monaghan Willy O Renier Pierre Rondot Monique M Ryan Jürgen Seeger Jan A Smeitink Gerry C Steenbergen-Spanjers Evangeline Wassmer Bernhard Weschke Frits A Wijburg Bridget Wilcken Dimitrios I Zafeiriou Ron A Wevers

Tyrosine hydroxylase deficiency is an autosomal recessive disorder resulting from cerebral catecholamine deficiency. Tyrosine hydroxylase deficiency has been reported in fewer than 40 patients worldwide. To recapitulate all available evidence on clinical phenotypes and rational diagnostic and therapeutic approaches for this devastating, but treatable, neurometabolic disorder, we studied 36 pati...

Journal: :The Biochemical journal 1993
L G Gahn R Roskoski

The activity of tyrosine hydroxylase in vitro is affected by many factors, including pH, phosphorylation by several protein kinases, and polyanions. We investigated the activation of tyrosine hydroxylase by RNA or DNA (polyanions), using purified rat PC12 cell enzyme. RNA and DNA each increased tyrosine hydroxylase activity in the presence of subsaturating (125 microM) tetrahydrobiopterin at pH...

Journal: :The Journal of comparative neurology 1993
S E Asmus S W Newman

Chemosensory and hormonal signals, both of which are essential for mating in the male Syrian hamster, are relayed through a distinct forebrain circuit. Immunocytochemistry for tyrosine hydroxylase, a catecholamine biosynthetic enzyme, previously revealed immunoreactive neurons in the anterior and posterior medial amygdaloid nucleus, one of the nuclei within this pathway. In addition, dopamine-i...

2002
Ruth G. Perez Jack C. Waymire Eva Lin Jen J. Liu Fengli Guo Michael J. Zigmond

The -synuclein gene is implicated in the pathogenesis of Parkinson’s disease. Although -synuclein function is uncertain, the protein has homology to the chaperone molecule 14-3-3. In addition, -synuclein can bind to 14-3-3, and both -synuclein and 14-3-3 bind to many of the same proteins. Because 14-3-3 binds to and activates tyrosine hydroxylase, the rate-limiting enzyme in dopamine (DA) biosy...

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