Identification of glycolipid binding sites for soybean agglutinin and differences in the surface glycolipids of cultured adrenergic and cholinergic sympathetic neurons☆

[摘要] Culturedadrenergicneuronsfromnewbornratsuperiorcervicalgangliabindthelectinsoybeanagglutinin(SBA)atafivefoldhigherdensitythanthesameneuronswhichhavebeeninducedtobecomecholinergic(M.SchwabandS.L.Landis,1981,Dev.Biol.84,67–78).Inthepresentexperiments,thebindingsitesforthislectinonthesurfacesoflivingneuronswereidentifiedbylabelingthesurfaceswiththegalactoseoxidase-[3H]sodiumborohydridereductiontechnique,withandwithoutpriorincubationwiththelectin.SBAbindstoandinhibitsthelabelingoftwoneutralglycolipids,aglycolipidcomigratingwithglobosideonthin-layerchromatogramsandanunidentifiedglycolipid.Whenneuronalproteinsareextractedandseparatedbypolyacrylamidegelelectrophoresisinsodiumdodecylsulfate,SBAshowsonlyveryfaintlabelingofthisfraction.ThustheSBAbindingsitesontheseneuronsappeartobetwoneutralglycolipids.FurthersupportforthisconclusioncomesfromthefindingthatthetwoneutralglycolipidsdetectedbySBAarepresentinsmalleramountsorarelessaccessibleonthecholinergicthanontheadrenergicneuronsasmeasuredbysurfacelabeling.Inadditiontothedifferenceinneutralglycolipids,externallabelingrevealedquantitativedifferencesinthemajorgangliosidesofthetwotypesofculturedneurons.Thus,byusingpureculturesofsympatheticneuronswhichcanbeinducedtobecomeeitheradrenergicorcholinergic,specificglycolipidprofileswerecorrelatedwiththetwoneurotransmitterphenotypes.

[学科分类] 生物科学（综合）