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Isolated Light Chain of Tetanus Toxin Inhibits Exocytosis: Studies in Digitonin-Permeabilized Cells
dc.contributor.authorBittner, Mary A.en_US
dc.contributor.authorHabig, William H.en_US
dc.contributor.authorHolz, Ronald W.en_US
dc.date.accessioned2010-04-01T15:13:29Z
dc.date.available2010-04-01T15:13:29Z
dc.date.issued1989-09en_US
dc.identifier.citationBittner, Mary A.; Habig, William H.; Holz, Ronald W. (1989). "Isolated Light Chain of Tetanus Toxin Inhibits Exocytosis: Studies in Digitonin-Permeabilized Cells." Journal of Neurochemistry 53(3): 966-968. <http://hdl.handle.net/2027.42/65694>en_US
dc.identifier.issn0022-3042en_US
dc.identifier.issn1471-4159en_US
dc.identifier.urihttps://hdl.handle.net/2027.42/65694
dc.identifier.urihttp://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=2760628&dopt=citationen_US
dc.description.abstractPrevious work indicates that the heavy chain of tetanus toxin is responsible for the binding of the toxin to the neuronal membrane and its subsequent internalization. In the present study, the light chain of tetanus toxin mimicked the holotoxin in inhibiting Ca 2+ -dependent secretion of [ 3 H]norepinephrine from digitonin-permeabilized adrenal chromaffin cells. Preincubation of tetanus toxin with monoclonal antibodies to the light chain prevented the inhibition by tetanus toxin. Preincubation of tetanus toxin with nonimmune ascites fluid or with monoclonal antibodies directed against the C fragment (the C-terminal of the heavy chains or the heavy-chain portion of the B fragment did not prevent inhibition by tetanus toxin. The data indicate that the light chain is responsible for the intracellular blockade of exostosis.en_US
dc.format.extent302998 bytes
dc.format.extent3110 bytes
dc.format.mimetypeapplication/pdf
dc.format.mimetypetext/plain
dc.publisherBlackwell Publishing Ltden_US
dc.rights1989 International Society for Neurochemistryen_US
dc.subject.otherTetanus Toxinen_US
dc.subject.otherChromaffin Cellen_US
dc.subject.otherCatecholamineen_US
dc.subject.otherExocytosisen_US
dc.subject.otherDigitonin Permeabilizationen_US
dc.titleIsolated Light Chain of Tetanus Toxin Inhibits Exocytosis: Studies in Digitonin-Permeabilized Cellsen_US
dc.typeArticleen_US
dc.rights.robotsIndexNoFollowen_US
dc.subject.hlbsecondlevelNeurosciencesen_US
dc.subject.hlbtoplevelHealth Sciencesen_US
dc.description.peerreviewedPeer Revieweden_US
dc.contributor.affiliationumDepartment of Pharmacology, University of Michigan Medical School, Ann Arbor, Michigan;en_US
dc.contributor.affiliationother* Laboratory of Bacterial Toxins, Division of Bacterial Products, U.S. Food and Drug Administration, Bethesda, Maryland, U.S.A.en_US
dc.identifier.pmid2760628en_US
dc.description.bitstreamurlhttp://deepblue.lib.umich.edu/bitstream/2027.42/65694/1/j.1471-4159.1989.tb11800.x.pdf
dc.identifier.doi10.1111/j.1471-4159.1989.tb11800.xen_US
dc.identifier.sourceJournal of Neurochemistryen_US
dc.identifier.citedreferenceBittner M. A. and Holz R. W. ( 1988 ) Effects of tetanus toxin on catecholamine release from intact and digitonin-permeabilized chromaffin cells. J. Neurochem. 51, 451 – 456.en_US
dc.identifier.citedreferenceBittner M. A., DasGupta B. R., and Holz R. W. ( 1989 ) Isolated light chains of botulinum neurotoxins inhibit exocytosis: studies in digitonin-permeabilized chromaffin cells. J. Biol. Chem. ( in press ).en_US
dc.identifier.citedreferenceKenimer J. G., Habig W. H., and Hardegree M. C. ( 1983 ) Monoclonal antibodies as probes of tetanus toxin structure and function. Infect. Immun. 42, 942 – 948.en_US
dc.identifier.citedreferenceLin C. S., Habig W. H., and Hardegree M. C. ( 1985 ) Antibodies against the light chain of tetanus toxin in human sera. Infect. Immun. 49, 111 – 115.en_US
dc.identifier.citedreferencePenner R., Neher E., and Dreyer F. ( 1986 ) Intracellularly injected tetanus toxin inhibits exocytosis in bovine adrenal chromaffin cells. Nature 324, 76 – 78.en_US
dc.identifier.citedreferenceWeller U., Taylor C. F., and Habermann E. ( 1986 ) Quantitative comparison between tetanus toxin, some fragments and toxoid for binding and axonal transport in the rat. Toxicon 24, 1055 – 1063.en_US
dc.owningcollnameInterdisciplinary and Peer-Reviewed


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