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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
5
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pubmed:dateCreated |
1986-7-1
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pubmed:abstractText |
Tetanus toxin is known to bind neuronal tissue selectively. To study the interactions of this potent neurotoxin in an intact cell system, the binding of 125I-tetanus toxin was characterized in a neuroblastoma retina hybrid cell line, N18-RE-105. The binding of 125I-tetanus toxin to membranes prepared from N18-RE-105 cells showed many similarities to the interactions of 125I-toxin with rat synaptic membranes. The binding was decreased with increasing temperature, ionic strength, and pH. 125I-Toxin bound to membranes with high affinity: KD = 0.62 +/- 0.05 nM; Bmax = 196 +/- 45 pmol/mg protein. Quantitative thin-layer chromatography and acid-degradation analysis revealed that N18-RE-105 cells contained polysialogangliosides GD1a and GT1b in high concentrations. An assay was developed to quantitate surface-bound and internalized 125I-tetanus toxin by exploiting the observation that surface-bound 125I-toxin is susceptible to pronase digestion. When cells were incubated with 125I-tetanus toxin at 0 degree C, all of the bound 125I-toxin could be degraded with pronase. In contrast, when the incubations were performed at 37 degrees C, within 10 min about 50% of the total cell-associated 125I-toxin was pronase-resistant. Temperature pulse experiments demonstrated that 125I-tetanus toxin that was bound to cells at 0 degree C rapidly disappeared from the surface when the cells were warmed to 37 degrees C, as revealed by the appearance of pronase-resistant radioactivity. This internalization was sensitive to metabolic inhibitors.(ABSTRACT TRUNCATED AT 250 WORDS)
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Gangliosides,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Oligomycins,
http://linkedlifedata.com/resource/pubmed/chemical/Pronase,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Cholinergic,
http://linkedlifedata.com/resource/pubmed/chemical/Rotenone,
http://linkedlifedata.com/resource/pubmed/chemical/Tetanus Toxin,
http://linkedlifedata.com/resource/pubmed/chemical/tetanus toxin receptor
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0270-6474
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
6
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1443-51
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:3711989-Animals,
pubmed-meshheading:3711989-Binding, Competitive,
pubmed-meshheading:3711989-Cell Line,
pubmed-meshheading:3711989-Chromatography, Thin Layer,
pubmed-meshheading:3711989-Drug Resistance,
pubmed-meshheading:3711989-Gangliosides,
pubmed-meshheading:3711989-Hybrid Cells,
pubmed-meshheading:3711989-Membrane Proteins,
pubmed-meshheading:3711989-Mice,
pubmed-meshheading:3711989-Neuroblastoma,
pubmed-meshheading:3711989-Oligomycins,
pubmed-meshheading:3711989-Pronase,
pubmed-meshheading:3711989-Rats,
pubmed-meshheading:3711989-Receptors, Cholinergic,
pubmed-meshheading:3711989-Rotenone,
pubmed-meshheading:3711989-Temperature,
pubmed-meshheading:3711989-Tetanus Toxin
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pubmed:year |
1986
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pubmed:articleTitle |
Characterization of the binding and internalization of tetanus toxin in a neuroblastoma hybrid cell line.
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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
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