The effects of calcium channel agonists and antagonists on the binding of [3H]nitrendipine to synaptic membrane and postsynaptic density fractions isolated from canine cerebral cortex. Evidence for a separate-site model for agonists and antagonists

1990 ◽  
pp. 61-72 ◽  
Author(s):  
PHILIP SIEKEVITZ ◽  
MARIE LEDOUX
Keyword(s):  
Cerebral Cortex ◽  
Calcium Channel ◽  
Postsynaptic Density ◽  
Synaptic Membrane ◽  
Density Fractions ◽  
Site Model ◽  
Separate Site

scholarly journals Function of a calmodulin in postsynaptic densities. III. Calmodulin-binding proteins of the postsynaptic density.

1981 ◽  
Vol 89 (3) ◽  
pp. 449-455 ◽  
Author(s):  
R K Carlin ◽  
D J Grab ◽  
P Siekevitz
Keyword(s):  
Cerebral Cortex ◽  
Membrane Fraction ◽  
Binding Proteins ◽  
Postsynaptic Density ◽  
M Protein ◽  
Synaptic Membranes ◽  
Synaptic Membrane ◽  
Calmodulin Binding ◽  
Chloramine T ◽  
Excitatory Responses

A method has been developed for binding calmodulin, radioiodinated by the lactoperoxidase method, to denaturing gels and has been used to attempt to identify the calmodulin-binding proteins of cerebral cortex postsynaptic densities (PSDs). Calmodulin primarily bound to the major 51,000 Mr protein in a saturatable manner; secondarily bound to the 60,000 Mr region, 140,000 Mr region, and 230,000 Mr protein; and bound in lesser amounts to a number of other proteins. The major 51,000 Mr calmodulin-binding protein is one of unknown identity. Binding of iodinated calmodulin to these proteins was blocked by EDTA, EGTA, chlorpromazine, and preincubation with unlabeled calmodulin. Calmodulin iodinated by the chloramine-T method, which inactivates calmodulin did not bind to the PSD but bound nonspecifically to histone. Calmodulin did not bind to proteins from a variety of sources for which calmodulin interactions have not been found. Except for three proteins, all of the proteins of synaptic membranes that bind calmodulin could be accounted for by proteins of the PSD which are a part of the synaptic membrane fraction. The major 51,000 M, protein and the corresponding iodinated calmodulin binding were greatly reduced in cerebellar PSDs and this difference between cerebral cortex and cerebellar PSDs is discussed in light of the possible function of calmodulin in synaptic excitatory responses.

Characterization of protein kinase C activities in postsynaptic density fractions prepared from cerebral cortex, hippocampus, and cerebellum

1993 ◽  
Vol 619 (1-2) ◽  
pp. 69-75 ◽  
Author(s):  
Tatsuo Suzuki ◽  
Kuniko Okumura-Noji ◽  
Ryo Tanaka ◽  
Akihiko Ogura ◽  
Kyoko Nakamura ◽  
...  
Keyword(s):  
Cerebral Cortex ◽  
Protein Kinase C ◽  
Protein Kinase ◽  
Postsynaptic Density ◽  
Density Fractions ◽  
Kinase C

Selective localization of amyloid precursor-like protein 1 in the cerebral cortex postsynaptic density

1995 ◽  
Vol 32 (1) ◽  
pp. 36-44 ◽  
Author(s):  
Tae-Wan Kim ◽  
Kuo Wu ◽  
Jia-Ling Xu ◽  
Geoff McAuliffe ◽  
Rudolph E. Tanzi ◽  
...  
Keyword(s):  
Cerebral Cortex ◽  
Postsynaptic Density ◽  
Selective Localization

scholarly journals Phosphorylation of synaptic-membrane proteins from ox cerebral cortex in vitro. Preparation of fractions enriched in phosphorylated proteins by using extraction with detergents and urea, and gel filtration

1977 ◽  
Vol 163 (2) ◽  
pp. 369-378 ◽  
Author(s):  
P R Dunkley ◽  
H Holmes ◽  
R Rodnight
Keyword(s):  
Cerebral Cortex ◽  
Cyclic Amp ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Polyacrylamide Gel ◽  
Synaptic Membrane ◽  
Hydroxyl Groups ◽  
Phosphorylated Proteins

Synaptic-membrane fragments from ox cerebral cortex contain basal and cyclic AMP-stimulated protein kinase(s) that transfer 32P from [gamma-32P]ATP to hydroxyl groups of serine and threonine residues in membrane-protein substrates. In the present work, labelled membrane fragments were partitioned into soluble and insoluble fractions with Triton X-100, Nonidet P. 40, sodium deoxycholate and urea, and the distribution of 32P-labelled protein in the fractions was determined by polyacrylamide-gel electrophoresis and radioautography. A high percentage of phosphorylated protein sustrates remained insoluble, including those whose phosphorylation was most highly stimulated by cyclic AMP. Whole membrane fragments and samples prepared by detergent extraction were fractionated on Sepharose 6B columns in the presence of low concentrations of sodium dodecyl sulphate and pooled fractions were analysed by polyacrylamide-gel electrophoresis and radioautography. Phosphorylated proteins were fractionated on the basis of their molecular weight, but homogeneous protein was not obtained. The results are discussed in relation to the techniques used and the results obtained in other laboratories.

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