Thomas Lentz, MD
Professor Emeritus of Cell BiologyCards
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About
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Professor Emeritus of Cell Biology
Biography
Thomas L. Lentz is currently Professor Emeritus of Cell Biology at the Yale University School of Medicine. He went on the faculty of the medical school in 1964 and his laboratory performed research mainly on nerve cells in the fields of cell biology and neurobiology. In 1971, he published "Cell Fine Structure. An Atlas of Drawings of Whole-Cell Structure." He was Dean of Admissions for the medical school from 1972 to 2006 and Vice Chairman of the Department of Cell Biology from 1992 to 2006. He retired in 2006 but continued to teach medical histology to first year medical students until 2018. He is currently a Curatorial Affiliate at the Peabody Museum of Natural History and donated a large collection of antique microscopes, microscope slides, and scientific instruments to the museum. He lives in the town of Killingworth, CT and currently is Municipal Historian and Chairman of the Planning and Zoning Commission.
Education & Training
- MD
- Yale University (1964)
Research
Overview
Lentz first studied primitive nervous systems of lower invertebrates, such as hydra. He investigated the development of the neuromuscular junction of vertebrates employing electron microscopy and cytochemistry. A procedure was developed for the high-resolution localization of acetylcholine receptors by means of horseradish peroxidase-labeled a-bungarotoxin. This technique was applied to the study of localization of receptors at the mature and developing neuromuscular junction and central synapses. He performed research on the trophic regulation of growth, regeneration, and differentiation by the nervous system. Other research involved investigation of functional domains on the nicotinic acetylcholine receptor of the electric organ, muscle, and central nervous system. This work led to the identification of the a-bungarotoxin-binding and nicotine-binding site on the receptor and identification of amino acid residues critical to binding. He studied whether the acetylcholine receptor serves as a host cell receptor for the highly neurotropic rabies virus. Agents were identified that might act as anti-viral agents by blocking the virus-receptor interaction. He last investigated the entry and transport of rabies virus in neurons. His research was funded by the National Science Foundation and the National Institutes of Health and resulted in over 200 scientific publications.
Research at a Glance
Publications Timeline
Publications
2000
Rabies virus entry at the neuromuscular junction in nerve–muscle cocultures
Lewis P, Fu Y, Lentz T. Rabies virus entry at the neuromuscular junction in nerve–muscle cocultures. Muscle & Nerve 2000, 23: 720-730. PMID: 10797395, DOI: 10.1002/(sici)1097-4598(200005)23:5<720::aid-mus9>3.0.co;2-5.Peer-Reviewed Original ResearchCitationsMeSH Keywords and ConceptsConceptsNerve cell bodiesRabies virus entryNerve-muscle coculturesNerve terminalsNerve fibersNeuromuscular junctionRabies virusCell bodiesVirus entryMotor nerve terminalsNerve-muscle contactsNicotinic acetylcholine receptorsVirus adsorption periodAcetylcholine receptorsLucifer YellowSynapsin ISynaptic vesiclesRetrograde transportVirusProgressive increaseEarly eventsCocultureSurface of cellsMyotube surfaceNeuronsNicotine Binding to Native and Substituted Peptides Comprising Residues 188–207 of Nicotinic Acetylcholine Receptor α1, α2, α3, α4, α5, and α7 Subunits
Lentz T. Nicotine Binding to Native and Substituted Peptides Comprising Residues 188–207 of Nicotinic Acetylcholine Receptor α1, α2, α3, α4, α5, and α7 Subunits. Biochemical And Biophysical Research Communications 2000, 268: 480-484. PMID: 10679230, DOI: 10.1006/bbrc.2000.2155.Peer-Reviewed Original ResearchCitationsMeSH Keywords and ConceptsConceptsNicotinic acetylcholine receptor α1Acetylcholine receptor alpha subunitNicotinic acetylcholine receptor alpha-subunitHigh affinity binding componentDifferent alpha subunitsReceptor alpha subunitNeuronal peptidesReceptor α1Alpha subunitΑ7 subunitAlpha4 subunitSignificant decreaseNicotineBinding componentSynthetic peptidesLow affinityPeptidesHigh affinity
1999
Waglerin-1 selectively blocks the epsilon form of the muscle nicotinic acetylcholine receptor.
McArdle J, Lentz T, Witzemann V, Schwarz H, Weinstein S, Schmidt J. Waglerin-1 selectively blocks the epsilon form of the muscle nicotinic acetylcholine receptor. Journal Of Pharmacology And Experimental Therapeutics 1999, 289: 543-50. PMID: 10087048.Peer-Reviewed Original ResearchCitationsAltmetricMeSH Keywords and ConceptsConceptsWild-type miceEnd-plate potentialsAdult wild-type miceNicotinic acetylcholine receptorsWaglerin-1Miniature end-plate potentialsKO miceMuscle nicotinic acetylcholine receptorACh responseAcetylcholine receptorsEnd-plate responsesHeterozygous KO miceHomozygous KO miceNeonatal wild-type miceSpontaneous miniature end-plate potentialsMouse muscle nicotinic acetylcholine receptorHeterozygous litter matesAdult knockout miceLethal effectsNeonatal miceSuppressant effectKnockout miceLitter matesMiceAcetylcholine
1998
Rabies Virus Entry into Endosomes in IMR-32 Human Neuroblastoma Cells
Lewis P, Fu Y, Lentz T. Rabies Virus Entry into Endosomes in IMR-32 Human Neuroblastoma Cells. Experimental Neurology 1998, 153: 65-73. PMID: 9743568, DOI: 10.1006/exnr.1998.6879.Peer-Reviewed Original ResearchCitationsMeSH Keywords and ConceptsConceptsIMR-32 human neuroblastoma cellsRabies virus entryHuman neuroblastoma cellsRabies virusNeuroblastoma cellsNerve terminalsCell bodiesVirus entryIMR-32 neuroblastoma cellsSynaptic vesicle markersLucifer YellowCell surfaceSynapsin ITransferrin receptorVirusTexas Red dextranEarly eventsVesicle markersVirus particlesImmunofluorescence microscopyRabies virus entry into cultured rat hippo campalneurons
Lewis P, Lentz T. Rabies virus entry into cultured rat hippo campalneurons. Brain Cell Biology 1998, 27: 559-573. PMID: 10405023, DOI: 10.1023/a:1006912610044.Peer-Reviewed Original ResearchCitationsMeSH Keywords and ConceptsConceptsRabies virus entryCultured hippocampal neuronsViral antigensHippocampal neuronsRabies virusVirus entryRabies virus infectionSynaptic vesicle markersAxon terminalsNerve terminalsVirus infectionLysosomotropic agent chloroquineSomatodendritic domainCell bodiesVirus-containing endosomesLucifer YellowNeuronsSynapsin IInfectionAntigenTransferrin receptorVirusWheat germ agglutininAgent chloroquineVesicle markersAmino Acids within Residues 181–200 of the Nicotinic Acetylcholine Receptor α1 Subunit Involved in Nicotine Binding
Lentz T, Chaturvedi V, Conti-Fine B. Amino Acids within Residues 181–200 of the Nicotinic Acetylcholine Receptor α1 Subunit Involved in Nicotine Binding. Biochemical Pharmacology 1998, 55: 341-347. PMID: 9484801, DOI: 10.1016/s0006-2952(97)00474-7.Peer-Reviewed Original ResearchCitationsMeSH Keywords and ConceptsConceptsNicotine bindingCys-192Cys-193Alpha1 subunitReceptor alpha1 subunitReceptor α1 subunitTyr-190Tyr-198Acetylcholine receptorsΑ1 subunitGreater reductionAsp-195Significant reductionFusion proteinPro-194Single concentrationThr-196Apparent KdAmino acidsSynthetic peptidesAsp-200Position 181Individual amino acidsResidues 181Previous studies
1997
Rabies virus infection of IMR-32 human neuroblastoma cells and effect of neurochemical and other agents
Lentz T, Fu Y, Lewis P. Rabies virus infection of IMR-32 human neuroblastoma cells and effect of neurochemical and other agents. Antiviral Research 1997, 35: 29-39. PMID: 9224959, DOI: 10.1016/s0166-3542(97)01036-x.Peer-Reviewed Original ResearchCitationsMeSH Keywords and ConceptsConceptsIMR-32 human neuroblastoma cellsIMR-32 cellsHuman neuroblastoma cellsNeuroblastoma cellsNeuronal nicotinic acetylcholine receptorsCentral nervous system receptorsRabies virusRabies virus infectionLysosomotropic agentsReceptor alpha1 subunitNicotinic acetylcholine receptorsNerve cell lineAttachment of virusNeurotropic virusesCholinergic agonistsViral antigensVirus infectionHuman neuronsAcetylcholine receptorsSynthetic peptidesCell bodiesInfectionAlpha1 subunitCholinergic ligandsBinding receptors
1996
Rabies virus binding to the nicotinic acetylcholine receptor α subunit demonstrated by virus overlay protein binding assay
Gastka M, Horvath J, Lentz T. Rabies virus binding to the nicotinic acetylcholine receptor α subunit demonstrated by virus overlay protein binding assay. Journal Of General Virology 1996, 77: 2437-2440. PMID: 8887475, DOI: 10.1099/0022-1317-77-10-2437.Peer-Reviewed Original ResearchCitationsAltmetricMeSH Keywords and ConceptsConceptsAlpha subunitNicotinic acetylcholine receptor α subunitAcetylcholine receptor α subunitElectric organ membranesVirus overlay proteinVirus overlay protein binding assaysTransfer of proteinsReceptor α subunitProtein binding assaysAChR alpha subunitOverlay proteinRabies virusΑ-subunitSubunitsGel electrophoresisAcetylcholine receptorsBinding assaysCuraremimetic neurotoxinsProteinMembraneVirusBindingAChRBlot
1995
Differential binding of nicotine and alpha-bungarotoxin to residues 173-204 of the nicotinic acetylcholine receptor alpha 1 subunit.
Lentz T. Differential binding of nicotine and alpha-bungarotoxin to residues 173-204 of the nicotinic acetylcholine receptor alpha 1 subunit. Biochemistry 1995, 34: 1316-22. PMID: 7827079, DOI: 10.1021/bi00004a026.Peer-Reviewed Original ResearchCitationsMeSH Keywords and Concepts
1993
Effects of mutations of Torpedo acetylcholine receptor alpha 1 subunit residues 184-200 on alpha-bungarotoxin binding in a recombinant fusion protein.
Chaturvedi V, Donnelly-Roberts D, Lentz T. Effects of mutations of Torpedo acetylcholine receptor alpha 1 subunit residues 184-200 on alpha-bungarotoxin binding in a recombinant fusion protein. Biochemistry 1993, 32: 9570-6. PMID: 8373764, DOI: 10.1021/bi00088a008.Peer-Reviewed Original ResearchCitationsMeSH Keywords and ConceptsConceptsAlpha 1 subunitFusion proteinAlpha-bungarotoxin bindingFusion protein containingOligonucleotide-directed mutagenesisEffects of mutationsPossible structure-function relationshipsStructure-function relationshipsTyr-189Dissimilar residuesPro-194Recombinant fusion proteinHigher apparent affinityAlpha subunitTyr-198Asp-195Cys-192Cys-193Protein containingFunctional interactionAmino acidsSubunitsResiduesMutationsPosition 184
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- Electron micrograph of neuromuscular junction