Loading…

Association of CD99 short and long forms with MHC class I, MHC class II and tetraspanin CD81 and recruitment into immunological synapses

CD99, a leukocyte surface glycoprotein, is broadly expressed in many cell types. On the cell surface, CD99 is expressed as two distinct isoforms, a long form and a short form. CD99 has been demonstrated to play a key role in several biological processes, including the regulation of T cell activation...

Full description

Saved in:
Bibliographic Details
Published in:BMC research notes 2011-08, Vol.4 (1), p.293-293, Article 293
Main Authors: Pata, Supansa, Otáhal, Pavel, Brdička, Tomáš, Laopajon, Witida, Mahasongkram, Kodchakorn, Kasinrerk, Watchara
Format: Article
Language:English
Subjects:
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
cited_by cdi_FETCH-LOGICAL-b5333-1cb7bd84315ce10d89bc9aa80451c5a1e4e21250a33429e2914b44d922c3ca5b3
cites cdi_FETCH-LOGICAL-b5333-1cb7bd84315ce10d89bc9aa80451c5a1e4e21250a33429e2914b44d922c3ca5b3
container_end_page 293
container_issue 1
container_start_page 293
container_title BMC research notes
container_volume 4
creator Pata, Supansa
Otáhal, Pavel
Brdička, Tomáš
Laopajon, Witida
Mahasongkram, Kodchakorn
Kasinrerk, Watchara
description CD99, a leukocyte surface glycoprotein, is broadly expressed in many cell types. On the cell surface, CD99 is expressed as two distinct isoforms, a long form and a short form. CD99 has been demonstrated to play a key role in several biological processes, including the regulation of T cell activation. However, the molecular mechanisms by which CD99 participates in such processes are unclear. As CD99 contains a short cytoplasmic tail, it is unlikely that CD99 itself takes part in its multi-functions. Association of CD99 with other membrane proteins has been suggested to be necessary for exerting its functions. In this study, we analyzed the association of CD99 with other cell surface molecules involved in T cell activation. We demonstrate the association of MHC class I, MHC class II and tetraspanin CD81 with CD99 molecules on the cell surface. Association of CD99 with its partners was observed for both isoforms. In addition, we determined that CD99 is a lipid raft-associated membrane protein and is recruited into the immunologic synapse during T cell activation. The implication of CD99 on T cell activation was investigated. Inhibition of anti-CD3 induced T cell proliferation by an anti-CD99 monoclonal antibody was observed. We provide evidence that CD99 directly interact and form the complex with the MHC class I and II, and tetraspanin CD81, and is functionally linked to the formation of the immunologic synapse. Upon T cell activation, CD99 engagement can inhibit T cell proliferation. We speculate that the CD99-MHC-CD81 complex is a tetraspanin web that plays an important role in T cell activation.
doi_str_mv 10.1186/1756-0500-4-293
format article
fullrecord <record><control><sourceid>gale_doaj_</sourceid><recordid>TN_cdi_doaj_primary_oai_doaj_org_article_b2cff61fc78b47c88e095ef6d0beb072</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><galeid>A266596025</galeid><doaj_id>oai_doaj_org_article_b2cff61fc78b47c88e095ef6d0beb072</doaj_id><sourcerecordid>A266596025</sourcerecordid><originalsourceid>FETCH-LOGICAL-b5333-1cb7bd84315ce10d89bc9aa80451c5a1e4e21250a33429e2914b44d922c3ca5b3</originalsourceid><addsrcrecordid>eNp1kk1vFCEYgCdGY2v17M2QeDAmTsvHMAMXk3X96CY1vahXAgwzSzMDW2DU_gN_tuxu3ewkNRyAl-d9wstLUbxE8BwhVl-ghtYlpBCWVYk5eVScHiKPj9YnxbMYbyCsEWPoaXGCESOMY3ha_FnE6LWVyXoHfAeWHzkHce1DAtK1YPCuB50PYwS_bFqDr5dLoAcZI1i9O96sdnQyKci4kc66LGJoFwxGh8mm0bgErEse2HGcnB98b7UcQLxzchNNfF486eQQzYv7-az4_vnTt-VleXX9ZbVcXJWKEkJKpFWjWlYRRLVBsGVcaS4lgxVFmkpkKoMRplASUmFuMEeVqqqWY6yJllSRs2K197Ze3ohNsKMMd8JLK3YBH3ohQ7J6MEJh3XU16nTDVNVoxgzk1HR1C5VRsMHZ9X7v2kxqNK3OJQY5zKTzE2fXovc_BUENJKTOgg97gbL-P4L5ifaj2HZVbLsqKpF7niVv7m8R_O1kYhKjjdoMg3TGT1EwxlFT1wRm8vWe7GUuz7rOZ6ne0mKB65ryGmKaqfMHqDxaM1rtnelsjs8S3s4SMpPM79TLKUaxuv4xZy_2rA4-xmC6Q7EIiu2XfqC8V8ePfOD__WHyF2fN77o</addsrcrecordid><sourcetype>Open Website</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>889176630</pqid></control><display><type>article</type><title>Association of CD99 short and long forms with MHC class I, MHC class II and tetraspanin CD81 and recruitment into immunological synapses</title><source>PubMed Central (Open Access)</source><source>ProQuest - Publicly Available Content Database</source><creator>Pata, Supansa ; Otáhal, Pavel ; Brdička, Tomáš ; Laopajon, Witida ; Mahasongkram, Kodchakorn ; Kasinrerk, Watchara</creator><creatorcontrib>Pata, Supansa ; Otáhal, Pavel ; Brdička, Tomáš ; Laopajon, Witida ; Mahasongkram, Kodchakorn ; Kasinrerk, Watchara</creatorcontrib><description>CD99, a leukocyte surface glycoprotein, is broadly expressed in many cell types. On the cell surface, CD99 is expressed as two distinct isoforms, a long form and a short form. CD99 has been demonstrated to play a key role in several biological processes, including the regulation of T cell activation. However, the molecular mechanisms by which CD99 participates in such processes are unclear. As CD99 contains a short cytoplasmic tail, it is unlikely that CD99 itself takes part in its multi-functions. Association of CD99 with other membrane proteins has been suggested to be necessary for exerting its functions. In this study, we analyzed the association of CD99 with other cell surface molecules involved in T cell activation. We demonstrate the association of MHC class I, MHC class II and tetraspanin CD81 with CD99 molecules on the cell surface. Association of CD99 with its partners was observed for both isoforms. In addition, we determined that CD99 is a lipid raft-associated membrane protein and is recruited into the immunologic synapse during T cell activation. The implication of CD99 on T cell activation was investigated. Inhibition of anti-CD3 induced T cell proliferation by an anti-CD99 monoclonal antibody was observed. We provide evidence that CD99 directly interact and form the complex with the MHC class I and II, and tetraspanin CD81, and is functionally linked to the formation of the immunologic synapse. Upon T cell activation, CD99 engagement can inhibit T cell proliferation. We speculate that the CD99-MHC-CD81 complex is a tetraspanin web that plays an important role in T cell activation.</description><identifier>ISSN: 1756-0500</identifier><identifier>EISSN: 1756-0500</identifier><identifier>DOI: 10.1186/1756-0500-4-293</identifier><identifier>PMID: 21838920</identifier><language>eng</language><publisher>England: BioMed Central Ltd</publisher><subject>Glycoproteins ; Major histocompatibility complex ; Physiological aspects ; T cells</subject><ispartof>BMC research notes, 2011-08, Vol.4 (1), p.293-293, Article 293</ispartof><rights>COPYRIGHT 2011 BioMed Central Ltd.</rights><rights>Copyright ©2011 Kasinrerk et al; licensee BioMed Central Ltd. 2011 Kasinrerk et al; licensee BioMed Central Ltd.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-b5333-1cb7bd84315ce10d89bc9aa80451c5a1e4e21250a33429e2914b44d922c3ca5b3</citedby><cites>FETCH-LOGICAL-b5333-1cb7bd84315ce10d89bc9aa80451c5a1e4e21250a33429e2914b44d922c3ca5b3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3170336/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3170336/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,727,780,784,885,27924,27925,37013,53791,53793</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/21838920$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Pata, Supansa</creatorcontrib><creatorcontrib>Otáhal, Pavel</creatorcontrib><creatorcontrib>Brdička, Tomáš</creatorcontrib><creatorcontrib>Laopajon, Witida</creatorcontrib><creatorcontrib>Mahasongkram, Kodchakorn</creatorcontrib><creatorcontrib>Kasinrerk, Watchara</creatorcontrib><title>Association of CD99 short and long forms with MHC class I, MHC class II and tetraspanin CD81 and recruitment into immunological synapses</title><title>BMC research notes</title><addtitle>BMC Res Notes</addtitle><description>CD99, a leukocyte surface glycoprotein, is broadly expressed in many cell types. On the cell surface, CD99 is expressed as two distinct isoforms, a long form and a short form. CD99 has been demonstrated to play a key role in several biological processes, including the regulation of T cell activation. However, the molecular mechanisms by which CD99 participates in such processes are unclear. As CD99 contains a short cytoplasmic tail, it is unlikely that CD99 itself takes part in its multi-functions. Association of CD99 with other membrane proteins has been suggested to be necessary for exerting its functions. In this study, we analyzed the association of CD99 with other cell surface molecules involved in T cell activation. We demonstrate the association of MHC class I, MHC class II and tetraspanin CD81 with CD99 molecules on the cell surface. Association of CD99 with its partners was observed for both isoforms. In addition, we determined that CD99 is a lipid raft-associated membrane protein and is recruited into the immunologic synapse during T cell activation. The implication of CD99 on T cell activation was investigated. Inhibition of anti-CD3 induced T cell proliferation by an anti-CD99 monoclonal antibody was observed. We provide evidence that CD99 directly interact and form the complex with the MHC class I and II, and tetraspanin CD81, and is functionally linked to the formation of the immunologic synapse. Upon T cell activation, CD99 engagement can inhibit T cell proliferation. We speculate that the CD99-MHC-CD81 complex is a tetraspanin web that plays an important role in T cell activation.</description><subject>Glycoproteins</subject><subject>Major histocompatibility complex</subject><subject>Physiological aspects</subject><subject>T cells</subject><issn>1756-0500</issn><issn>1756-0500</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2011</creationdate><recordtype>article</recordtype><sourceid>DOA</sourceid><recordid>eNp1kk1vFCEYgCdGY2v17M2QeDAmTsvHMAMXk3X96CY1vahXAgwzSzMDW2DU_gN_tuxu3ewkNRyAl-d9wstLUbxE8BwhVl-ghtYlpBCWVYk5eVScHiKPj9YnxbMYbyCsEWPoaXGCESOMY3ha_FnE6LWVyXoHfAeWHzkHce1DAtK1YPCuB50PYwS_bFqDr5dLoAcZI1i9O96sdnQyKci4kc66LGJoFwxGh8mm0bgErEse2HGcnB98b7UcQLxzchNNfF486eQQzYv7-az4_vnTt-VleXX9ZbVcXJWKEkJKpFWjWlYRRLVBsGVcaS4lgxVFmkpkKoMRplASUmFuMEeVqqqWY6yJllSRs2K197Ze3ohNsKMMd8JLK3YBH3ohQ7J6MEJh3XU16nTDVNVoxgzk1HR1C5VRsMHZ9X7v2kxqNK3OJQY5zKTzE2fXovc_BUENJKTOgg97gbL-P4L5ifaj2HZVbLsqKpF7niVv7m8R_O1kYhKjjdoMg3TGT1EwxlFT1wRm8vWe7GUuz7rOZ6ne0mKB65ryGmKaqfMHqDxaM1rtnelsjs8S3s4SMpPM79TLKUaxuv4xZy_2rA4-xmC6Q7EIiu2XfqC8V8ePfOD__WHyF2fN77o</recordid><startdate>20110813</startdate><enddate>20110813</enddate><creator>Pata, Supansa</creator><creator>Otáhal, Pavel</creator><creator>Brdička, Tomáš</creator><creator>Laopajon, Witida</creator><creator>Mahasongkram, Kodchakorn</creator><creator>Kasinrerk, Watchara</creator><general>BioMed Central Ltd</general><general>BioMed Central</general><general>BMC</general><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>IOV</scope><scope>7X8</scope><scope>5PM</scope><scope>DOA</scope></search><sort><creationdate>20110813</creationdate><title>Association of CD99 short and long forms with MHC class I, MHC class II and tetraspanin CD81 and recruitment into immunological synapses</title><author>Pata, Supansa ; Otáhal, Pavel ; Brdička, Tomáš ; Laopajon, Witida ; Mahasongkram, Kodchakorn ; Kasinrerk, Watchara</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-b5333-1cb7bd84315ce10d89bc9aa80451c5a1e4e21250a33429e2914b44d922c3ca5b3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2011</creationdate><topic>Glycoproteins</topic><topic>Major histocompatibility complex</topic><topic>Physiological aspects</topic><topic>T cells</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Pata, Supansa</creatorcontrib><creatorcontrib>Otáhal, Pavel</creatorcontrib><creatorcontrib>Brdička, Tomáš</creatorcontrib><creatorcontrib>Laopajon, Witida</creatorcontrib><creatorcontrib>Mahasongkram, Kodchakorn</creatorcontrib><creatorcontrib>Kasinrerk, Watchara</creatorcontrib><collection>PubMed</collection><collection>CrossRef</collection><collection>Gale In Context: Opposing Viewpoints</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><collection>Open Access: DOAJ - Directory of Open Access Journals</collection><jtitle>BMC research notes</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Pata, Supansa</au><au>Otáhal, Pavel</au><au>Brdička, Tomáš</au><au>Laopajon, Witida</au><au>Mahasongkram, Kodchakorn</au><au>Kasinrerk, Watchara</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Association of CD99 short and long forms with MHC class I, MHC class II and tetraspanin CD81 and recruitment into immunological synapses</atitle><jtitle>BMC research notes</jtitle><addtitle>BMC Res Notes</addtitle><date>2011-08-13</date><risdate>2011</risdate><volume>4</volume><issue>1</issue><spage>293</spage><epage>293</epage><pages>293-293</pages><artnum>293</artnum><issn>1756-0500</issn><eissn>1756-0500</eissn><abstract>CD99, a leukocyte surface glycoprotein, is broadly expressed in many cell types. On the cell surface, CD99 is expressed as two distinct isoforms, a long form and a short form. CD99 has been demonstrated to play a key role in several biological processes, including the regulation of T cell activation. However, the molecular mechanisms by which CD99 participates in such processes are unclear. As CD99 contains a short cytoplasmic tail, it is unlikely that CD99 itself takes part in its multi-functions. Association of CD99 with other membrane proteins has been suggested to be necessary for exerting its functions. In this study, we analyzed the association of CD99 with other cell surface molecules involved in T cell activation. We demonstrate the association of MHC class I, MHC class II and tetraspanin CD81 with CD99 molecules on the cell surface. Association of CD99 with its partners was observed for both isoforms. In addition, we determined that CD99 is a lipid raft-associated membrane protein and is recruited into the immunologic synapse during T cell activation. The implication of CD99 on T cell activation was investigated. Inhibition of anti-CD3 induced T cell proliferation by an anti-CD99 monoclonal antibody was observed. We provide evidence that CD99 directly interact and form the complex with the MHC class I and II, and tetraspanin CD81, and is functionally linked to the formation of the immunologic synapse. Upon T cell activation, CD99 engagement can inhibit T cell proliferation. We speculate that the CD99-MHC-CD81 complex is a tetraspanin web that plays an important role in T cell activation.</abstract><cop>England</cop><pub>BioMed Central Ltd</pub><pmid>21838920</pmid><doi>10.1186/1756-0500-4-293</doi><oa>free_for_read</oa></addata></record>
fulltext fulltext
identifier ISSN: 1756-0500
ispartof BMC research notes, 2011-08, Vol.4 (1), p.293-293, Article 293
issn 1756-0500
1756-0500
language eng
recordid cdi_doaj_primary_oai_doaj_org_article_b2cff61fc78b47c88e095ef6d0beb072
source PubMed Central (Open Access); ProQuest - Publicly Available Content Database
subjects Glycoproteins
Major histocompatibility complex
Physiological aspects
T cells
title Association of CD99 short and long forms with MHC class I, MHC class II and tetraspanin CD81 and recruitment into immunological synapses
url http://sfxeu10.hosted.exlibrisgroup.com/loughborough?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-29T12%3A52%3A07IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-gale_doaj_&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Association%20of%20CD99%20short%20and%20long%20forms%20with%20MHC%20class%20I,%20MHC%20class%20II%20and%20tetraspanin%20CD81%20and%20recruitment%20into%20immunological%20synapses&rft.jtitle=BMC%20research%20notes&rft.au=Pata,%20Supansa&rft.date=2011-08-13&rft.volume=4&rft.issue=1&rft.spage=293&rft.epage=293&rft.pages=293-293&rft.artnum=293&rft.issn=1756-0500&rft.eissn=1756-0500&rft_id=info:doi/10.1186/1756-0500-4-293&rft_dat=%3Cgale_doaj_%3EA266596025%3C/gale_doaj_%3E%3Cgrp_id%3Ecdi_FETCH-LOGICAL-b5333-1cb7bd84315ce10d89bc9aa80451c5a1e4e21250a33429e2914b44d922c3ca5b3%3C/grp_id%3E%3Coa%3E%3C/oa%3E%3Curl%3E%3C/url%3E&rft_id=info:oai/&rft_pqid=889176630&rft_id=info:pmid/21838920&rft_galeid=A266596025&rfr_iscdi=true