Endocytosis of Cholera Toxin in GERL-Like Structures of Murine Neuroblastoma Cells Pretreated with GM1Ganglioside: Cholera Toxin Internalization into Neuroblastoma GERL

Cholera toxin (CT), covalently attached to horseradish peroxidase (HRP), is a specific cytochemical marker for GM1ganglioside ( GM1) and retains the ability of the native toxin to raise levels of cyclic AMP in avian erythrocytes. Using a cytochemical stain for HRP, we found that 9% of control cultur...

Ausführliche Beschreibung

Gespeichert in:
Bibliographische Detailangaben
Veröffentlicht in:The Journal of cell biology 1979-06, Vol.81 (3), p.543-554
Hauptverfasser: Joseph, Kenneth C., Stieber, Anna, Gonatas, Nicholas K.
Format: Artikel
Sprache:eng
Schlagworte:
Online-Zugang:Volltext
Tags: Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
container_end_page 554
container_issue 3
container_start_page 543
container_title The Journal of cell biology
container_volume 81
creator Joseph, Kenneth C.
Stieber, Anna
Gonatas, Nicholas K.
description Cholera toxin (CT), covalently attached to horseradish peroxidase (HRP), is a specific cytochemical marker for GM1ganglioside ( GM1) and retains the ability of the native toxin to raise levels of cyclic AMP in avian erythrocytes. Using a cytochemical stain for HRP, we found that 9% of control cultured murine neuroblastoma cells bound cholera toxin-horseradish peroxidase conjugates (CT-HRP) on their surfaces after incubations for 1 h at 4°C. Exogenous GM1, the natural receptor of CT, becomes associated in the culture medium with the plasma membranes of these cells so that 96% of cells are stained. Cells preincubated with GM1at 4°C were exposed to CT-HRP for 1 h at 4°C. After washing, cells were incubated at 37°C for 30 min-24 h. Endocytosis of CT-HRP occurred within 30 min and CT-HRP remained, throughout the 24-h period, in tubules, vesicles, and cisternae often found near the Golgi apparatus; this aggregate of peroxidase-positive elements probably corresponds to Golgi apparatus-endoplasmic reticulum-lysosomes (GERL) of neurons. In metaphase cells, CT-HRP was observed in aggregates of vesicles and tubules clustered near the centriole. Conjugates of HRP with subunit B, the GM1binding component of CT, were internalized by cells pretreated with GM1as was CT-HRP. The 9% of neuroblastoma cells binding CT-HRP in the absence of exogenous GM1internalized the ligand in a manner indistinguishable from that of the treated cells. These findings indicate that, in neuroblastoma cells, a system of vesicles, tubules, and cisternae, analogous to GERL of neurons, is the primary recipient of adsorptive endocytosis of CT bound to endogenous or exogenously introduced GM1.
format Article
fullrecord <record><control><sourceid>jstor</sourceid><recordid>TN_cdi_jstor_primary_1608763</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><jstor_id>1608763</jstor_id><sourcerecordid>1608763</sourcerecordid><originalsourceid>FETCH-jstor_primary_16087633</originalsourceid><addsrcrecordid>eNqFjs1KA0EQhOegYNS8gYd-gYXZbH7U67KuQiKiuYdOtmM6TqalpxeNT-RjuhFPuQgFdaiivjpxPe8HeXYzGozO3HlKW-_9cDIseu67io2s9iaJE8gayo0EUoS5fHKETnX1PM2m_EbwYtqurFX6Lc5a5UjwSK3KMmAy2SGUFEKCJyVTQqMGPtg2UM_yGuNr4A7S0O0R4yEaacTAX2gsB6bJ0ezhw6U7XWNI1P_zC3d1V83L-2zbdXTxrrxD3S_ysb-ejIvin_gHxQ5ZyQ</addsrcrecordid><sourcetype>Publisher</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype></control><display><type>article</type><title>Endocytosis of Cholera Toxin in GERL-Like Structures of Murine Neuroblastoma Cells Pretreated with GM1Ganglioside: Cholera Toxin Internalization into Neuroblastoma GERL</title><source>EZB-FREE-00999 freely available EZB journals</source><source>Alma/SFX Local Collection</source><creator>Joseph, Kenneth C. ; Stieber, Anna ; Gonatas, Nicholas K.</creator><creatorcontrib>Joseph, Kenneth C. ; Stieber, Anna ; Gonatas, Nicholas K.</creatorcontrib><description>Cholera toxin (CT), covalently attached to horseradish peroxidase (HRP), is a specific cytochemical marker for GM1ganglioside ( GM1) and retains the ability of the native toxin to raise levels of cyclic AMP in avian erythrocytes. Using a cytochemical stain for HRP, we found that 9% of control cultured murine neuroblastoma cells bound cholera toxin-horseradish peroxidase conjugates (CT-HRP) on their surfaces after incubations for 1 h at 4°C. Exogenous GM1, the natural receptor of CT, becomes associated in the culture medium with the plasma membranes of these cells so that 96% of cells are stained. Cells preincubated with GM1at 4°C were exposed to CT-HRP for 1 h at 4°C. After washing, cells were incubated at 37°C for 30 min-24 h. Endocytosis of CT-HRP occurred within 30 min and CT-HRP remained, throughout the 24-h period, in tubules, vesicles, and cisternae often found near the Golgi apparatus; this aggregate of peroxidase-positive elements probably corresponds to Golgi apparatus-endoplasmic reticulum-lysosomes (GERL) of neurons. In metaphase cells, CT-HRP was observed in aggregates of vesicles and tubules clustered near the centriole. Conjugates of HRP with subunit B, the GM1binding component of CT, were internalized by cells pretreated with GM1as was CT-HRP. The 9% of neuroblastoma cells binding CT-HRP in the absence of exogenous GM1internalized the ligand in a manner indistinguishable from that of the treated cells. These findings indicate that, in neuroblastoma cells, a system of vesicles, tubules, and cisternae, analogous to GERL of neurons, is the primary recipient of adsorptive endocytosis of CT bound to endogenous or exogenously introduced GM1.</description><identifier>ISSN: 0021-9525</identifier><language>eng</language><publisher>Rockefeller University Press</publisher><subject>Cell membranes ; Cells ; Cholera ; Cultured cells ; Endocytosis ; Gangliosides ; Golgi apparatus ; Neuroblastoma ; Neurons ; Toxins</subject><ispartof>The Journal of cell biology, 1979-06, Vol.81 (3), p.543-554</ispartof><rights>Copyright 1979 The Rockefeller University Press</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784</link.rule.ids></links><search><creatorcontrib>Joseph, Kenneth C.</creatorcontrib><creatorcontrib>Stieber, Anna</creatorcontrib><creatorcontrib>Gonatas, Nicholas K.</creatorcontrib><title>Endocytosis of Cholera Toxin in GERL-Like Structures of Murine Neuroblastoma Cells Pretreated with GM1Ganglioside: Cholera Toxin Internalization into Neuroblastoma GERL</title><title>The Journal of cell biology</title><description>Cholera toxin (CT), covalently attached to horseradish peroxidase (HRP), is a specific cytochemical marker for GM1ganglioside ( GM1) and retains the ability of the native toxin to raise levels of cyclic AMP in avian erythrocytes. Using a cytochemical stain for HRP, we found that 9% of control cultured murine neuroblastoma cells bound cholera toxin-horseradish peroxidase conjugates (CT-HRP) on their surfaces after incubations for 1 h at 4°C. Exogenous GM1, the natural receptor of CT, becomes associated in the culture medium with the plasma membranes of these cells so that 96% of cells are stained. Cells preincubated with GM1at 4°C were exposed to CT-HRP for 1 h at 4°C. After washing, cells were incubated at 37°C for 30 min-24 h. Endocytosis of CT-HRP occurred within 30 min and CT-HRP remained, throughout the 24-h period, in tubules, vesicles, and cisternae often found near the Golgi apparatus; this aggregate of peroxidase-positive elements probably corresponds to Golgi apparatus-endoplasmic reticulum-lysosomes (GERL) of neurons. In metaphase cells, CT-HRP was observed in aggregates of vesicles and tubules clustered near the centriole. Conjugates of HRP with subunit B, the GM1binding component of CT, were internalized by cells pretreated with GM1as was CT-HRP. The 9% of neuroblastoma cells binding CT-HRP in the absence of exogenous GM1internalized the ligand in a manner indistinguishable from that of the treated cells. These findings indicate that, in neuroblastoma cells, a system of vesicles, tubules, and cisternae, analogous to GERL of neurons, is the primary recipient of adsorptive endocytosis of CT bound to endogenous or exogenously introduced GM1.</description><subject>Cell membranes</subject><subject>Cells</subject><subject>Cholera</subject><subject>Cultured cells</subject><subject>Endocytosis</subject><subject>Gangliosides</subject><subject>Golgi apparatus</subject><subject>Neuroblastoma</subject><subject>Neurons</subject><subject>Toxins</subject><issn>0021-9525</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1979</creationdate><recordtype>article</recordtype><sourceid/><recordid>eNqFjs1KA0EQhOegYNS8gYd-gYXZbH7U67KuQiKiuYdOtmM6TqalpxeNT-RjuhFPuQgFdaiivjpxPe8HeXYzGozO3HlKW-_9cDIseu67io2s9iaJE8gayo0EUoS5fHKETnX1PM2m_EbwYtqurFX6Lc5a5UjwSK3KMmAy2SGUFEKCJyVTQqMGPtg2UM_yGuNr4A7S0O0R4yEaacTAX2gsB6bJ0ezhw6U7XWNI1P_zC3d1V83L-2zbdXTxrrxD3S_ysb-ejIvin_gHxQ5ZyQ</recordid><startdate>19790601</startdate><enddate>19790601</enddate><creator>Joseph, Kenneth C.</creator><creator>Stieber, Anna</creator><creator>Gonatas, Nicholas K.</creator><general>Rockefeller University Press</general><scope/></search><sort><creationdate>19790601</creationdate><title>Endocytosis of Cholera Toxin in GERL-Like Structures of Murine Neuroblastoma Cells Pretreated with GM1Ganglioside: Cholera Toxin Internalization into Neuroblastoma GERL</title><author>Joseph, Kenneth C. ; Stieber, Anna ; Gonatas, Nicholas K.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-jstor_primary_16087633</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1979</creationdate><topic>Cell membranes</topic><topic>Cells</topic><topic>Cholera</topic><topic>Cultured cells</topic><topic>Endocytosis</topic><topic>Gangliosides</topic><topic>Golgi apparatus</topic><topic>Neuroblastoma</topic><topic>Neurons</topic><topic>Toxins</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Joseph, Kenneth C.</creatorcontrib><creatorcontrib>Stieber, Anna</creatorcontrib><creatorcontrib>Gonatas, Nicholas K.</creatorcontrib><jtitle>The Journal of cell biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Joseph, Kenneth C.</au><au>Stieber, Anna</au><au>Gonatas, Nicholas K.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Endocytosis of Cholera Toxin in GERL-Like Structures of Murine Neuroblastoma Cells Pretreated with GM1Ganglioside: Cholera Toxin Internalization into Neuroblastoma GERL</atitle><jtitle>The Journal of cell biology</jtitle><date>1979-06-01</date><risdate>1979</risdate><volume>81</volume><issue>3</issue><spage>543</spage><epage>554</epage><pages>543-554</pages><issn>0021-9525</issn><abstract>Cholera toxin (CT), covalently attached to horseradish peroxidase (HRP), is a specific cytochemical marker for GM1ganglioside ( GM1) and retains the ability of the native toxin to raise levels of cyclic AMP in avian erythrocytes. Using a cytochemical stain for HRP, we found that 9% of control cultured murine neuroblastoma cells bound cholera toxin-horseradish peroxidase conjugates (CT-HRP) on their surfaces after incubations for 1 h at 4°C. Exogenous GM1, the natural receptor of CT, becomes associated in the culture medium with the plasma membranes of these cells so that 96% of cells are stained. Cells preincubated with GM1at 4°C were exposed to CT-HRP for 1 h at 4°C. After washing, cells were incubated at 37°C for 30 min-24 h. Endocytosis of CT-HRP occurred within 30 min and CT-HRP remained, throughout the 24-h period, in tubules, vesicles, and cisternae often found near the Golgi apparatus; this aggregate of peroxidase-positive elements probably corresponds to Golgi apparatus-endoplasmic reticulum-lysosomes (GERL) of neurons. In metaphase cells, CT-HRP was observed in aggregates of vesicles and tubules clustered near the centriole. Conjugates of HRP with subunit B, the GM1binding component of CT, were internalized by cells pretreated with GM1as was CT-HRP. The 9% of neuroblastoma cells binding CT-HRP in the absence of exogenous GM1internalized the ligand in a manner indistinguishable from that of the treated cells. These findings indicate that, in neuroblastoma cells, a system of vesicles, tubules, and cisternae, analogous to GERL of neurons, is the primary recipient of adsorptive endocytosis of CT bound to endogenous or exogenously introduced GM1.</abstract><pub>Rockefeller University Press</pub></addata></record>
fulltext fulltext
identifier ISSN: 0021-9525
ispartof The Journal of cell biology, 1979-06, Vol.81 (3), p.543-554
issn 0021-9525
language eng
recordid cdi_jstor_primary_1608763
source EZB-FREE-00999 freely available EZB journals; Alma/SFX Local Collection
subjects Cell membranes
Cells
Cholera
Cultured cells
Endocytosis
Gangliosides
Golgi apparatus
Neuroblastoma
Neurons
Toxins
title Endocytosis of Cholera Toxin in GERL-Like Structures of Murine Neuroblastoma Cells Pretreated with GM1Ganglioside: Cholera Toxin Internalization into Neuroblastoma GERL
url https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-24T04%3A20%3A13IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-jstor&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Endocytosis%20of%20Cholera%20Toxin%20in%20GERL-Like%20Structures%20of%20Murine%20Neuroblastoma%20Cells%20Pretreated%20with%20GM1Ganglioside:%20Cholera%20Toxin%20Internalization%20into%20Neuroblastoma%20GERL&rft.jtitle=The%20Journal%20of%20cell%20biology&rft.au=Joseph,%20Kenneth%20C.&rft.date=1979-06-01&rft.volume=81&rft.issue=3&rft.spage=543&rft.epage=554&rft.pages=543-554&rft.issn=0021-9525&rft_id=info:doi/&rft_dat=%3Cjstor%3E1608763%3C/jstor%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_id=info:pmid/&rft_jstor_id=1608763&rfr_iscdi=true