Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1998-10-20
pubmed:abstractText
Postmitotic NT2N cells, which are derived from human NT2 teratocarcinoma cells by treatment with retinoic acid (RA) and mitotic inhibitors, are viewed as a good in vitro model for mature neurons of the human central nervous system. Although NT2N cells exhibit many morphological and biochemical characteristics of neurons, the expression of key protein components involved in regulated exocytosis have not been firmly established. Here we show by immunoblot analysis that mature morphologically differentiated NT2N cells contain readily detectable quantities of the synaptic vesicle-associated proteins, synaptobrevin, synapsin, and synaptophysin. They also express the presynaptic plasma membrane protein, SNAP-25, and a Rab GTPase implicated in the control of Ca(2+)-dependent exocytosis, Rab3A. These proteins were not detected in untreated NT2 cells or cells exposed to RA for only 6 d. The induction of an array of proteins known to be involved in the docking and fusion of synaptic vesicles with the plasma membrane provides further support for the validity of NT2N cells as a model for human cortical neurons and suggests that these cells may be useful for in vitro molecular studies of the Ca(2+)-regulated exocytic pathway in nerve terminals.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/GTP Phosphohydrolases, http://linkedlifedata.com/resource/pubmed/chemical/GTP-Binding Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Nerve Tissue Proteins, http://linkedlifedata.com/resource/pubmed/chemical/R-SNARE Proteins, http://linkedlifedata.com/resource/pubmed/chemical/SNAP25 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Synapsins, http://linkedlifedata.com/resource/pubmed/chemical/Synaptophysin, http://linkedlifedata.com/resource/pubmed/chemical/Synaptosomal-Associated Protein 25, http://linkedlifedata.com/resource/pubmed/chemical/Tumor Markers, Biological, http://linkedlifedata.com/resource/pubmed/chemical/rab3 GTP-Binding Proteins
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0895-8696
pubmed:author
pubmed:issnType
Print
pubmed:volume
10
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
121-8
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:9699153-Cell Differentiation, pubmed-meshheading:9699153-GTP Phosphohydrolases, pubmed-meshheading:9699153-GTP-Binding Proteins, pubmed-meshheading:9699153-Humans, pubmed-meshheading:9699153-Male, pubmed-meshheading:9699153-Membrane Proteins, pubmed-meshheading:9699153-Nerve Tissue Proteins, pubmed-meshheading:9699153-Neurons, pubmed-meshheading:9699153-R-SNARE Proteins, pubmed-meshheading:9699153-Synapsins, pubmed-meshheading:9699153-Synaptic Vesicles, pubmed-meshheading:9699153-Synaptophysin, pubmed-meshheading:9699153-Synaptosomal-Associated Protein 25, pubmed-meshheading:9699153-Teratocarcinoma, pubmed-meshheading:9699153-Testicular Neoplasms, pubmed-meshheading:9699153-Tumor Cells, Cultured, pubmed-meshheading:9699153-Tumor Markers, Biological, pubmed-meshheading:9699153-rab3 GTP-Binding Proteins
pubmed:year
1998
pubmed:articleTitle
Expression of Rab3A GTPase and other synaptic proteins is induced in differentiated NT2N neurons.
pubmed:affiliation
Hood Research Program, Weis Center for Research, Pennsylvania State University College of Medicine, Danville 17822-2616, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.