Linked Life Data

2168883

Source:http://linkedlifedata.com/resource/pubmed/id/2168883

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
27
pubmed:dateCreated
1990-10-18
pubmed:abstractText
Two glutamate-binding proteins (71 and 63 kDa) were previously purified from synaptic plasma membranes (Chen, J.-W., Cunningham, M.D., Galton, V., and Michaelis, E. K. (1988) J. Biol. Chem. 263, 417-426). These proteins may play a role in glutamate neurotransmission in brain. Polyclonal antibodies were raised against the denatured glutamate-binding proteins in rabbits, including sets of antibodies against each of the binding proteins. The antibodies reacted specifically against both 71- and 63-kDa proteins. The antibodies recognized the denatured form of the proteins in Western blots and the native state of the proteins in enzyme-linked immunosorbent assays and in immunoaffinity chromatography and extraction procedures. All antibodies labeled most strongly the 71-kDa protein in Western blots, but extracted both proteins from solubilized synaptic membrane preparations. These findings indicate that the two proteins are closely related immunologically but the reactivity on Western blots differs between these two proteins. Immunoextraction of the 71- and 63-kDa proteins led to a approximately 60% decrease in L-[3H]glutamate-binding activity associated with synaptic membrane proteins. Of the brain subcellular fractions examined, the isolated synaptic plasma membranes had the strongest reaction in enzyme-linked immunosorbent assays toward the antiglutamate-binding protein antisera. Electron microscopy combined with gold particle immunohistochemistry revealed the sites labeled by the antibodies as entities present either on the surface or within the postsynaptic membranes and the associated densities of brain nerve ending particles (synaptosomes). Immunohistochemical procedures of gold labeling with silver enhancement of labeled sites revealed selective neuronal labeling in brain regions enriched in glutamate neurotransmitter pathways such as the hippocampus. Labeling was along dendrites and around cell bodies of pyramidal neurons. Based on the pattern of histochemical labeling, the distribution of immune reactivity in synaptic membranes, and the extractions of a major component of membrane glutamate-recognizing proteins by the antibodies, the glutamate-binding proteins must play a role in glutamate neurotransmission.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
25
pubmed:volume
265
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
16195-204
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:2168883-Animals, pubmed-meshheading:2168883-Antibodies, pubmed-meshheading:2168883-Brain, pubmed-meshheading:2168883-Chromatography, Affinity, pubmed-meshheading:2168883-Electrophoresis, Polyacrylamide Gel, pubmed-meshheading:2168883-Enzyme-Linked Immunosorbent Assay, pubmed-meshheading:2168883-Glutamates, pubmed-meshheading:2168883-Immunoblotting, pubmed-meshheading:2168883-Immunoglobulin G, pubmed-meshheading:2168883-Immunohistochemistry, pubmed-meshheading:2168883-Kinetics, pubmed-meshheading:2168883-Male, pubmed-meshheading:2168883-Molecular Weight, pubmed-meshheading:2168883-Rats, pubmed-meshheading:2168883-Rats, Inbred Strains, pubmed-meshheading:2168883-Receptors, Glutamate, pubmed-meshheading:2168883-Receptors, Neurotransmitter, pubmed-meshheading:2168883-Synaptic Membranes
pubmed:year
1990
pubmed:articleTitle
Immunochemical characterization of brain synaptic membrane glutamate-binding proteins.
pubmed:affiliation
Department of Biochemistry, University of Kansas, Lawrence 66045.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S., Research Support, Non-U.S. Gov't