Protein secretion by choroid plexus: Isolated apical fragments synthesize protein in vitro

Protein synthesis was studied in the isolated rat choroid plexus. When the choroid plexus was studied by transmission electron microscopy, membrane-bound structures were often observed in the ventricular space. These structures appear to bud from the apical surface of the epithelial cells. In the pr...

Ausführliche Beschreibung

Gespeichert in:
Bibliographische Detailangaben
Veröffentlicht in:Tissue & cell 1987, Vol.19 (1), p.101-109
Hauptverfasser: Gudeman, David M., Nelson, Stanley R., Merisko, Elaine M.
Format: Artikel
Sprache:eng
Schlagworte:
Online-Zugang:Volltext
Tags: Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
container_end_page 109
container_issue 1
container_start_page 101
container_title Tissue & cell
container_volume 19
creator Gudeman, David M.
Nelson, Stanley R.
Merisko, Elaine M.
description Protein synthesis was studied in the isolated rat choroid plexus. When the choroid plexus was studied by transmission electron microscopy, membrane-bound structures were often observed in the ventricular space. These structures appear to bud from the apical surface of the epithelial cells. In the present study, we attempted to isolate these membrane-bound cellular fragments from the choroid plexus and to determine their ability to synthesize proteins. The apical fragments (aposomes) were isolated from the choroid plexus by allowing tissue explants to incubate in media (37 °C) for 1 h. The tissue was removed and the media, now containing aposomes, was incubated with [S 35]methionine (100 μCi). The media was collected and analysed by SDS-PAGE followed by fluorography. Parallel [S 35]methionine incubations were done with whole tissue expiants. The SDS-PAGE protein derived from the aposomes was similar to the profile derived from the tissue. In addition, proteins detected in CSF had relative molecular weights comparable to the products synthesized by aposomes. These observations suggest that aposomes provide an additional route of entry for proteins into CSF.
doi_str_mv 10.1016/0040-8166(87)90061-9
format Article
fullrecord <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_77459028</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>0040816687900619</els_id><sourcerecordid>77459028</sourcerecordid><originalsourceid>FETCH-LOGICAL-c272t-11214bb1e1598c25e1f0fc40ab85f21b25c95833de437c14dfdd7fff50d8f7453</originalsourceid><addsrcrecordid>eNp9kE9LAzEQxYMotVa_gUJOoofVJLvZZD0IUvwHBT3oxUvYTSY2st3UJC3WT-_WFo_CwBzmvTczP4SOKbmghJaXhBQkk7Qsz6Q4rwgpaVbtoCHlOctyItguGv5J9tFBjB-EEFFQMUCDnJd5VckhensOPoHrcAQdIDnf4WaF9dQH7wyet_C1iFf4Mfq2TmBwPXe6brEN9fsMuhRxXHVpCtF9A55vk_pauhT8IdqzdRvhaNtH6PXu9mX8kE2e7h_HN5NMM8FSRimjRdNQoLySmnGgllhdkLqR3DLaMK4rLvPcQJELTQtjjRHWWk6MtKLg-QidbnL7Az4XEJOauaihbesO_CIq0YsqwmQvLDZCHXyMAayaBzerw0pRotZI1ZqXWvNSUqhfpKrqbSfb_EUzA_Nn2jLs59ebOfRPLh0EFbWDToNxAXRSxrv_F_wAYRmGzg</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>77459028</pqid></control><display><type>article</type><title>Protein secretion by choroid plexus: Isolated apical fragments synthesize protein in vitro</title><source>MEDLINE</source><source>ScienceDirect Journals (5 years ago - present)</source><creator>Gudeman, David M. ; Nelson, Stanley R. ; Merisko, Elaine M.</creator><creatorcontrib>Gudeman, David M. ; Nelson, Stanley R. ; Merisko, Elaine M.</creatorcontrib><description>Protein synthesis was studied in the isolated rat choroid plexus. When the choroid plexus was studied by transmission electron microscopy, membrane-bound structures were often observed in the ventricular space. These structures appear to bud from the apical surface of the epithelial cells. In the present study, we attempted to isolate these membrane-bound cellular fragments from the choroid plexus and to determine their ability to synthesize proteins. The apical fragments (aposomes) were isolated from the choroid plexus by allowing tissue explants to incubate in media (37 °C) for 1 h. The tissue was removed and the media, now containing aposomes, was incubated with [S 35]methionine (100 μCi). The media was collected and analysed by SDS-PAGE followed by fluorography. Parallel [S 35]methionine incubations were done with whole tissue expiants. The SDS-PAGE protein derived from the aposomes was similar to the profile derived from the tissue. In addition, proteins detected in CSF had relative molecular weights comparable to the products synthesized by aposomes. These observations suggest that aposomes provide an additional route of entry for proteins into CSF.</description><identifier>ISSN: 0040-8166</identifier><identifier>EISSN: 1532-3072</identifier><identifier>DOI: 10.1016/0040-8166(87)90061-9</identifier><identifier>PMID: 3563998</identifier><language>eng</language><publisher>Scotland: Elsevier Ltd</publisher><subject>Animals ; apocrine secretion ; Choroid plexus ; Choroid Plexus - metabolism ; Choroid Plexus - ultrastructure ; CSF ; DNA - analysis ; In Vitro Techniques ; Male ; Methionine - metabolism ; Microscopy, Electron ; Molecular Weight ; Protein Biosynthesis ; Proteins - isolation &amp; purification ; Proteins - metabolism ; Rats ; Rats, Inbred Strains ; Sulfur Radioisotopes</subject><ispartof>Tissue &amp; cell, 1987, Vol.19 (1), p.101-109</ispartof><rights>1987</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c272t-11214bb1e1598c25e1f0fc40ab85f21b25c95833de437c14dfdd7fff50d8f7453</citedby><cites>FETCH-LOGICAL-c272t-11214bb1e1598c25e1f0fc40ab85f21b25c95833de437c14dfdd7fff50d8f7453</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/0040-8166(87)90061-9$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3548,4021,27921,27922,27923,45993</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/3563998$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Gudeman, David M.</creatorcontrib><creatorcontrib>Nelson, Stanley R.</creatorcontrib><creatorcontrib>Merisko, Elaine M.</creatorcontrib><title>Protein secretion by choroid plexus: Isolated apical fragments synthesize protein in vitro</title><title>Tissue &amp; cell</title><addtitle>Tissue Cell</addtitle><description>Protein synthesis was studied in the isolated rat choroid plexus. When the choroid plexus was studied by transmission electron microscopy, membrane-bound structures were often observed in the ventricular space. These structures appear to bud from the apical surface of the epithelial cells. In the present study, we attempted to isolate these membrane-bound cellular fragments from the choroid plexus and to determine their ability to synthesize proteins. The apical fragments (aposomes) were isolated from the choroid plexus by allowing tissue explants to incubate in media (37 °C) for 1 h. The tissue was removed and the media, now containing aposomes, was incubated with [S 35]methionine (100 μCi). The media was collected and analysed by SDS-PAGE followed by fluorography. Parallel [S 35]methionine incubations were done with whole tissue expiants. The SDS-PAGE protein derived from the aposomes was similar to the profile derived from the tissue. In addition, proteins detected in CSF had relative molecular weights comparable to the products synthesized by aposomes. These observations suggest that aposomes provide an additional route of entry for proteins into CSF.</description><subject>Animals</subject><subject>apocrine secretion</subject><subject>Choroid plexus</subject><subject>Choroid Plexus - metabolism</subject><subject>Choroid Plexus - ultrastructure</subject><subject>CSF</subject><subject>DNA - analysis</subject><subject>In Vitro Techniques</subject><subject>Male</subject><subject>Methionine - metabolism</subject><subject>Microscopy, Electron</subject><subject>Molecular Weight</subject><subject>Protein Biosynthesis</subject><subject>Proteins - isolation &amp; purification</subject><subject>Proteins - metabolism</subject><subject>Rats</subject><subject>Rats, Inbred Strains</subject><subject>Sulfur Radioisotopes</subject><issn>0040-8166</issn><issn>1532-3072</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1987</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kE9LAzEQxYMotVa_gUJOoofVJLvZZD0IUvwHBT3oxUvYTSY2st3UJC3WT-_WFo_CwBzmvTczP4SOKbmghJaXhBQkk7Qsz6Q4rwgpaVbtoCHlOctyItguGv5J9tFBjB-EEFFQMUCDnJd5VckhensOPoHrcAQdIDnf4WaF9dQH7wyet_C1iFf4Mfq2TmBwPXe6brEN9fsMuhRxXHVpCtF9A55vk_pauhT8IdqzdRvhaNtH6PXu9mX8kE2e7h_HN5NMM8FSRimjRdNQoLySmnGgllhdkLqR3DLaMK4rLvPcQJELTQtjjRHWWk6MtKLg-QidbnL7Az4XEJOauaihbesO_CIq0YsqwmQvLDZCHXyMAayaBzerw0pRotZI1ZqXWvNSUqhfpKrqbSfb_EUzA_Nn2jLs59ebOfRPLh0EFbWDToNxAXRSxrv_F_wAYRmGzg</recordid><startdate>1987</startdate><enddate>1987</enddate><creator>Gudeman, David M.</creator><creator>Nelson, Stanley R.</creator><creator>Merisko, Elaine M.</creator><general>Elsevier Ltd</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>1987</creationdate><title>Protein secretion by choroid plexus: Isolated apical fragments synthesize protein in vitro</title><author>Gudeman, David M. ; Nelson, Stanley R. ; Merisko, Elaine M.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c272t-11214bb1e1598c25e1f0fc40ab85f21b25c95833de437c14dfdd7fff50d8f7453</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1987</creationdate><topic>Animals</topic><topic>apocrine secretion</topic><topic>Choroid plexus</topic><topic>Choroid Plexus - metabolism</topic><topic>Choroid Plexus - ultrastructure</topic><topic>CSF</topic><topic>DNA - analysis</topic><topic>In Vitro Techniques</topic><topic>Male</topic><topic>Methionine - metabolism</topic><topic>Microscopy, Electron</topic><topic>Molecular Weight</topic><topic>Protein Biosynthesis</topic><topic>Proteins - isolation &amp; purification</topic><topic>Proteins - metabolism</topic><topic>Rats</topic><topic>Rats, Inbred Strains</topic><topic>Sulfur Radioisotopes</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Gudeman, David M.</creatorcontrib><creatorcontrib>Nelson, Stanley R.</creatorcontrib><creatorcontrib>Merisko, Elaine M.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Tissue &amp; cell</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Gudeman, David M.</au><au>Nelson, Stanley R.</au><au>Merisko, Elaine M.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Protein secretion by choroid plexus: Isolated apical fragments synthesize protein in vitro</atitle><jtitle>Tissue &amp; cell</jtitle><addtitle>Tissue Cell</addtitle><date>1987</date><risdate>1987</risdate><volume>19</volume><issue>1</issue><spage>101</spage><epage>109</epage><pages>101-109</pages><issn>0040-8166</issn><eissn>1532-3072</eissn><abstract>Protein synthesis was studied in the isolated rat choroid plexus. When the choroid plexus was studied by transmission electron microscopy, membrane-bound structures were often observed in the ventricular space. These structures appear to bud from the apical surface of the epithelial cells. In the present study, we attempted to isolate these membrane-bound cellular fragments from the choroid plexus and to determine their ability to synthesize proteins. The apical fragments (aposomes) were isolated from the choroid plexus by allowing tissue explants to incubate in media (37 °C) for 1 h. The tissue was removed and the media, now containing aposomes, was incubated with [S 35]methionine (100 μCi). The media was collected and analysed by SDS-PAGE followed by fluorography. Parallel [S 35]methionine incubations were done with whole tissue expiants. The SDS-PAGE protein derived from the aposomes was similar to the profile derived from the tissue. In addition, proteins detected in CSF had relative molecular weights comparable to the products synthesized by aposomes. These observations suggest that aposomes provide an additional route of entry for proteins into CSF.</abstract><cop>Scotland</cop><pub>Elsevier Ltd</pub><pmid>3563998</pmid><doi>10.1016/0040-8166(87)90061-9</doi><tpages>9</tpages></addata></record>
fulltext fulltext
identifier ISSN: 0040-8166
ispartof Tissue & cell, 1987, Vol.19 (1), p.101-109
issn 0040-8166
1532-3072
language eng
recordid cdi_proquest_miscellaneous_77459028
source MEDLINE; ScienceDirect Journals (5 years ago - present)
subjects Animals
apocrine secretion
Choroid plexus
Choroid Plexus - metabolism
Choroid Plexus - ultrastructure
CSF
DNA - analysis
In Vitro Techniques
Male
Methionine - metabolism
Microscopy, Electron
Molecular Weight
Protein Biosynthesis
Proteins - isolation & purification
Proteins - metabolism
Rats
Rats, Inbred Strains
Sulfur Radioisotopes
title Protein secretion by choroid plexus: Isolated apical fragments synthesize protein in vitro
url https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-14T03%3A34%3A04IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Protein%20secretion%20by%20choroid%20plexus:%20Isolated%20apical%20fragments%20synthesize%20protein%20in%20vitro&rft.jtitle=Tissue%20&%20cell&rft.au=Gudeman,%20David%20M.&rft.date=1987&rft.volume=19&rft.issue=1&rft.spage=101&rft.epage=109&rft.pages=101-109&rft.issn=0040-8166&rft.eissn=1532-3072&rft_id=info:doi/10.1016/0040-8166(87)90061-9&rft_dat=%3Cproquest_cross%3E77459028%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=77459028&rft_id=info:pmid/3563998&rft_els_id=0040816687900619&rfr_iscdi=true