Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0027819 (neuroblastoma)
 27,800 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Neuro-p24 is a novel neuronal membrane protein that is specifically localized in neural processes, particularly in growing neurites. To explore the roles of Neuro-p24, we examined the immunocytochemical localization of this protein in cultured neurons during neural induction, and performed an antisense oligonucleotide transfection using two culture models, the mouse dorsal root ganglia (DRG) and the neuro2a neuroblastoma cell line. Intense Neuro-p24 immunoreactivity was observed in the soma and small vesicles in neurites at the early stage of culture, but it gradually disappeared as cultures proceeded. Intense immunoreactivity was often observed at the growing distal end of the neurites. Morphological changes in neurites after Neuro-p24 antisense oligonucleotide transfection were examined in DRG neurons by the continual observation of a group of identical neurons. Affected cells retracted neurites transiently, followed by the re-elongation and branching of newly formed neurites. The control oligonucleotide-treated neurons appeared unaffected. When neuro2a cells were similarly treated with antisense oligonucleotides, the results were similar to those obtained in the DRG neurons. The binding of Neuro-p24 to tubulin was confirmed by both in vivo and in vitro pull-down assays. The present results support our idea that Neuro-p24 plays an essential role in neurite extension through a vesicle transport system via microtubules.
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PMID:Neuro-p24 plays an essential role in neurite extension: antisense oligonucleotide inhibition of neurite extension in cultured DRG neurons and neuroblastoma cells. 1538 Mar 27

We have isolated and characterized a novel cDNA encoding a small neuronal membrane protein showing high sequence homology to Neuro-p24/Neurensin-1, a protein containing a microtubule-associated domain at the carboxyl-terminus and exclusively localized to small vesicles of neurons. The newly identified Neurensin-2 constitutes two-membrane spanning domains but not the microtubule-binding domain, with a molecular mass of 28 kDa. Neurensin-2 mRNA is expressed only in brain, whereas the protein expressed in various neurons including those of the thalamus/hypothalamus and hippocampus, of postnatally developing mice. While the levels of Neurensin-1 mRNA and protein in retinoic acid-exposed mouse neuroblastoma Neuro2a cells increased, those of Neurensin-2 mRNA and protein remained unchanged. When the Neurensin-2 cDNA was transfected into Neuro2a cells, Neurensin-2 was expressed in small vesicles including lysosomes in the perinuclear region. On the cotransfection of Neurensin-1 and -2 cDNA into Neuro2a cells, Neurensin-2 was mainly found in small vesicles of the cell body and Neurensin-1 in those of growth cones. In nerve growth factor-stimulated PC12 cells, the intracellular localization of these proteins also differed. Furthermore, immunochemical staining of mouse brain revealed that Neurensin-1 and -2 had a similar distribution in many regions such as the Diagonal band, hippocampus, amygdaloid nucleus, and habenula nucleus, but differed in the intracellular localization as follows: Neurensin-1 was found mainly in neuritic processes, while Neurensin-2 was found in cell bodies. Thus, both Neurensin-1, and -2 are localized in small vesicles in neural cells, but their localizations of the vesicles are not always the same by each other, suggesting that they are under separate regulation.
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PMID:Molecular characterization of a transport vesicle protein Neurensin-2, a homologue of Neurensin-1, expressed in neural cells. 1652 58