Identification of a domain in cytochrome C that displaces [3H]TCP binding from rat brain membrane receptors: Synthesis of β-neuroprotectin

1990 ◽  
Vol 22 (4) ◽  
pp. 335-339 ◽  
Author(s):  
J.Blanche O'Neill ◽  
H. Jaffe ◽  
P.L. Hallberg ◽  
J.M. Buzy ◽  
T. Kingan ◽  
...  
Keyword(s):  
Cytochrome C ◽  
Rat Brain ◽  
Membrane Receptors ◽  
Brain Membrane

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.

Comparison of rat brain membrane antigens by complement mediated release of neurotransmitters from brain fractions using antisera against S-100 and THY-1

1979 ◽  
Vol 168 (1) ◽  
pp. 119-132 ◽  
Author(s):  
K.G. Haglid ◽  
A.N. Barclay ◽  
A. Hamberger ◽  
B. Hedquist ◽  
B. Nystro¨m ◽  
...  
Keyword(s):  
Rat Brain ◽  
Brain Membrane ◽  
S 100 ◽  
Membrane Antigens

Properties of 3H-cimetidine binding in rat brain membrane fractions

Life Sciences ◽  
1980 ◽  
Vol 26 (16) ◽  
pp. 1293-1302 ◽  
Author(s):  
David A. Kendall ◽  
John W. Ferkany ◽  
S.J. Enna
Keyword(s):  
Rat Brain ◽  
Brain Membrane

Characterization of Phorbol Ester Binding to Membrane-Inserted Protein Kinase C in Rat Brain Membrane

1990 ◽  
Vol 44 (1) ◽  
pp. 141-142
Author(s):  
Ken'ichi Osada ◽  
Mikio Asakura ◽  
Makiko Shibata ◽  
Tohru Tsukamoto ◽  
Jun Imafuku ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Rat Brain ◽  
Phorbol Ester ◽  
Brain Membrane ◽  
Kinase C

A neuroanatomical analysis of the effects of a memory impairing dose of scopolamine in the rat brain using cytochrome c oxidase as principle marker

2014 ◽  
Vol 59-60 ◽  
pp. 1-7 ◽  
Author(s):  
Sarah Hescham ◽  
Yasin Temel ◽  
João Casaca-Carreira ◽  
Kemal Arslantas ◽  
Youssef Yakkioui ◽  
...  
Keyword(s):  
Cytochrome C ◽  
Rat Brain ◽  
Cytochrome C Oxidase

Decreased alpha 1-adrenergic receptor-mediated inositide hydrolysis in neurons from hypertensive rat brain

1986 ◽  
Vol 251 (2) ◽  
pp. C230-C237 ◽  
Author(s):  
J. B. Feldstein ◽  
R. A. Gonzales ◽  
S. P. Baker ◽  
C. Sumners ◽  
F. T. Crews ◽  
...  
Keyword(s):  
Rat Brain ◽  
Adrenergic Receptors ◽  
Inositol Phosphates ◽  
Inositol Phosphate ◽  
Specific Binding ◽  
Membrane Receptors ◽  
Neuronal Cultures ◽  
Brain Neurons ◽  
Neuronal Membranes ◽  
Rat Brain Neurons

The expression of alpha 1-adrenergic receptors and norepinephrine (NE)-stimulated hydrolysis of inositol phospholipid has been studied in neuronal cultures from the brains of normotensive (Wistar-Kyoto, WKY) and spontaneously hypertensive (SH) rats. Binding of 125I-2-[beta-(4-hydroxyphenyl)-ethyl-aminomethyl] tetralone (HEAT) to neuronal membranes was 68-85% specific and was rapid. Competition-inhibition experiments with various agonists and antagonists suggested that 125I-HEAT bound selectively to alpha 1-adrenergic receptors. Specific binding of 125I-HEAT to neuronal membranes from SH rat brain cultures was 30-45% higher compared with binding in WKY normotensive controls. This increase was attributed to an increase in the number of alpha 1-adrenergic receptors on SH rat brain neurons. Incubation of neuronal cultures of rat brain from both strains with NE resulted in a concentration-dependent stimulation of release of inositol phosphates, although neurons from SH rat brains were 40% less responsive compared with WKY controls. The decrease in responsiveness of SH rat brain neurons to NE, even though the alpha 1-adrenergic receptors are increased, does not appear to be due to a general defect in membrane receptors and postreceptor signal transduction mechanisms. This is because neither the number of muscarinic-cholinergic receptors nor the carbachol-stimulated release of inositol phosphates is different in neuronal cultures from the brains of SH rats compared with neuronal cultures from the brains of WKY rats. These observations suggest that the increased expression of alpha 1-adrenergic receptors does not parallel the receptor-mediated inositol phosphate hydrolysis in neuronal cultures from SH rat brain.

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