Conversion of Individual Phosphatidates into Rat Brain Lipid in vitro

1977 ◽  
Vol 5 (1) ◽  
pp. 175-178 ◽  
Author(s):  
LUCIANO BINAGLIA ◽  
RITA ROBERTI ◽  
GIUSEPPE PORCELLATI
Keyword(s):  
Rat Brain ◽  
Brain Lipid

scholarly journals Incorporation of 14c-hydralazine into rat brain lipid fraction in vitro.

1980 ◽  
Vol 30 ◽  
pp. 69
Author(s):  
Shuichi Hara ◽  
Tetsuo Satoh ◽  
Haruo Kitagawa
Keyword(s):  
Rat Brain ◽  
Lipid Fraction ◽  
Brain Lipid

scholarly journals Cholesterol-rich naked mole-rat brain lipid membranes are susceptible to amyloid beta-induced damage in vitro

Aging ◽  
2020 ◽  
Vol 12 (21) ◽  
pp. 22266-22290
Author(s):  
Daniel Frankel ◽  
Matthew Davies ◽  
Bharat Bhushan ◽  
Yavuz Kulaberoglu ◽  
Paulina Urriola-Munoz ◽  
...  
Keyword(s):  
Rat Brain ◽  
Amyloid Beta ◽  
Lipid Membranes ◽  
Brain Lipid ◽  
Mole Rat ◽  
Naked Mole Rat

scholarly journals High Glycogen Levels in Brains of Rats with Minimal Environmental Stimuli: Implications for Metabolic Contributions of Working Astrocytes

2002 ◽  
Vol 22 (12) ◽  
pp. 1476-1489 ◽  
Author(s):  
Nancy F. Cruz ◽  
Gerald A. Dienel
Keyword(s):  
Rat Brain ◽  
Sensory Stimulation ◽  
Enzyme Inactivation ◽  
Biologically Active ◽  
Metabolic Labeling ◽  
Tissue Sampling ◽  
Normal Rat ◽  
Sampling Procedures ◽  
Very High

The concentration of glycogen, the major brain energy reserve localized mainly in astrocytes, is generally reported as about 2 or 3 μmol/g, but sometimes as high as 3.9 to 8 μmol/g, in normal rat brain. The authors found high but very different glycogen levels in two recent studies in which glycogen was determined by the routine amyloglucosidase procedure in 0.03N HCl digests either of frozen powders (4.8 to 6 μmol/g) or of ethanol-insoluble fractions (8 to 12 μmol/g). To evaluate the basis for these discrepant results, glycogen was assayed in parallel extracts of the same samples. Glycogen levels in ethanol extracts were twice those in 0.03N HCl digests, suggesting incomplete enzyme inactivation even with very careful thawing. The very high glycogen levels were biologically active and responsive to physiologic and pharmacological challenge. Glycogen levels fell after brief sensory stimulation, and metabolic labeling indicated its turnover under resting conditions. About 95% of the glycogen was degraded under in vitro ischemic conditions, and its “carbon equivalents” recovered mainly as glc, glc-P, and lactate. Resting glycogen stores were reduced by about 50% by chronic inhibition of nitric oxide synthase. Because neurotransmitters are known to stimulate glycogenolysis, stress or sensory activation due to animal handling and tissue-sampling procedures may stimulate glycogenolysis during an experiment, and glycogen lability during tissue sampling and extraction can further reduce glycogen levels. The very high glycogen levels in normal rat brain suggest an unrecognized role for astrocytic energy metabolism during brain activation.

In vitro interaction of ACTH with rat brain muscarinic receptors

Peptides ◽  
1986 ◽  
Vol 7 (3) ◽  
pp. 425-429 ◽  
Author(s):  
Jeroen A.D.M. Tonnaer ◽  
Marianna Van Vugt ◽  
Joop S. De Graaf
Keyword(s):  
Rat Brain ◽  
Muscarinic Receptors ◽  
In Vitro Interaction

In vitro screen of inhibitors of rat brain serotonin synthesis

1969 ◽  
Vol 47 (5) ◽  
pp. 501-506 ◽  
Author(s):  
E. G. McGeer ◽  
D. A. V. Peters
Keyword(s):  
Rat Brain ◽  
Tryptophan Hydroxylase ◽  
Inhibitory Effect ◽  
Complexing Agents ◽  
Serotonin Synthesis ◽  
Structural Requirements ◽  
Class A ◽  
Numerous Data ◽  
Comparison Of The Results

Over 700 compounds were screened at 10−4 M concentration as inhibitors of the conversion of L-tryptophan-14C to serotonin-14C in crude rat brain homogenates. Most of the compounds had little or no inhibitory effect. Those with strong inhibitory properties were tested as inhibitors of 5-hydroxytryptophan decarboxylase and, if active on the decarboxylase, were assayed as tryptophan hydroxylase inhibitors. Except for a few oxidizing and complexing agents and for some substituted p-phenylenediamines, the compounds found to inhibit tryptophan hydroxylase by >50% belonged to the three types of inhibitors already known, i.e. catechols, phenylalanine and ring-substituted phenylalanines, and 6-substituted tryptophans. The numerous data in this screen make possible some comments as to the structural requirements for activity within each class. A comparison of the results on tryptophan hydroxylase with data on tyrosine hydroxylase inhibition in similar homogenates makes it clear that two separate, if somewhat similar, enzymes are involved.

scholarly journals The correlation between Na+ channel subunits and scorpion toxin-binding sites. A study in rat brain synaptosomes and in brain neurons developing in vitro.

1988 ◽  
Vol 263 (3) ◽  
pp. 1542-1548
Author(s):  
E Jover ◽  
A Massacrier ◽  
P Cau ◽  
M F Martin ◽  
F Couraud
Keyword(s):  
Rat Brain ◽  
Binding Sites ◽  
Scorpion Toxin ◽  
Na Channel ◽  
Brain Neurons ◽  
Rat Brain Synaptosomes ◽  
Toxin Binding ◽  
Brain Synaptosomes

Specific and nonspecific components in the oxidative metabolism of estradiol by the male rat brain in vitro

1983 ◽  
Vol 19 (1) ◽  
pp. 219-228 ◽  
Author(s):  
Jack Fishman ◽  
Baiba Norton
Keyword(s):  
Rat Brain ◽  
Oxidative Metabolism ◽  
Male Rat

scholarly journals Phosphorylation-dependent interaction of the synaptic vesicle proteins cysteine string protein and synaptotagmin I

2002 ◽  
Vol 364 (2) ◽  
pp. 343-347 ◽  
Author(s):  
Gareth J.O. EVANS ◽  
Alan MORGAN
Keyword(s):  
Rat Brain ◽  
Direct Interaction ◽  
Secretory Vesicle ◽  
Brain Membrane ◽  
Synaptotagmin I ◽  
Phosphorylated Form ◽  
Order Of Magnitude ◽  
And Function

The secretory vesicle cysteine string proteins (CSPs) are members of the DnaJ family of chaperones, and function at late stages of Ca2+-regulated exocytosis by an unknown mechanism. To determine novel binding partners of CSPs, we employed a pull-down strategy from purified rat brain membrane or cytosolic proteins using recombinant hexahistidine-tagged (His6-)CSP. Western blotting of the CSP-binding proteins identified synaptotagmin I to be a putative binding partner. Furthermore, pull-down assays using cAMP-dependent protein kinase (PKA)-phosphorylated CSP recovered significantly less synaptotagmin. Complexes containing CSP and synaptotagmin were immunoprecipitated from rat brain membranes, further suggesting that these proteins interact in vivo. Binding assays in vitro using recombinant proteins confirmed a direct interaction between the two proteins and demonstrated that the PKA-phosphorylated form of CSP binds synaptotagmin with approximately an order of magnitude lower affinity than the non-phosphorylated form. Genetic studies have implicated each of these proteins in the Ca2+-dependency of exocytosis and, since CSP does not bind Ca2+, this novel interaction might explain the Ca2+-dependent actions of CSP.

Effects of anesthetics on sodium uptake into rat brain cortex in vitro

1972 ◽  
Vol 21 (12) ◽  
pp. 1763-1773 ◽  
Author(s):  
R. Shankaran ◽  
J.H. Quastel
Keyword(s):  
Rat Brain ◽  
Brain Cortex ◽  
Sodium Uptake ◽  
Rat Brain Cortex
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