Influence of oxygenated fuel additives and their metabolites on the binding of a convulsant ligand of the γ-aminobutyric acidA (GABAA) receptor in rat brain membrane preparations

2002 ◽  
Vol 129 (3) ◽  
pp. 219-226 ◽  
Author(s):  
Joseph V Martin ◽  
Nesli M Bilgin ◽  
M.Michael Iba
Keyword(s):  
Rat Brain ◽  
Gabaa Receptor ◽  
Fuel Additives ◽  
Brain Membrane ◽  
Oxygenated Fuel

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

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

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

Neurosteroids may differentially affect the function of two native GABAA receptor subtypes in the rat brain

1998 ◽  
Vol 357 (4) ◽  
pp. 401-407 ◽  
Author(s):  
Giovanna Schmid ◽  
Roberta Sala ◽  
Giambattista Bonanno ◽  
M. Raiteri
Keyword(s):  
Rat Brain ◽  
Gabaa Receptor ◽  
Receptor Subtypes ◽  
Gabaa Receptor Subtypes

Immunocytochemical localization of the GABAA receptor in the rat brain

1987 ◽  
Vol 136 (3) ◽  
pp. 451-453 ◽  
Author(s):  
Javier Vitorica ◽  
Dongeun Park ◽  
Angel L. De Blas
Keyword(s):  
Rat Brain ◽  
Gabaa Receptor ◽  
Immunocytochemical Localization
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