Tissue Washing Improves Native Ambient Mass Spectrometry Detection of Membrane Proteins Directly from Tissue
Native ambient mass spectrometry enables the in situ analysis of proteins and their complexes directly from tissue, providing both structural and spatial information. Until recently, the approach was applied exclusively to the analysis of soluble proteins; however, there is a drive for new technique...
Gespeichert in:
Veröffentlicht in: | Journal of the American Chemical Society 2023-07, Vol.145 (29), p.15658-15662 |
---|---|
Hauptverfasser: | , , , |
Format: | Artikel |
Sprache: | eng |
Schlagworte: | |
Online-Zugang: | Volltext |
Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
container_end_page | 15662 |
---|---|
container_issue | 29 |
container_start_page | 15658 |
container_title | Journal of the American Chemical Society |
container_volume | 145 |
creator | Sisley, Emma K. Hale, Oliver J. Hughes, James W. Cooper, Helen J. |
description | Native ambient mass spectrometry enables the in situ analysis of proteins and their complexes directly from tissue, providing both structural and spatial information. Until recently, the approach was applied exclusively to the analysis of soluble proteins; however, there is a drive for new techniques that enable analysis of membrane proteins. Here we demonstrate native ambient mass spectrometry of membrane proteins, including β-barrel and α-helical (single and multipass) integral membrane proteins and membrane-associated proteins incorporating lipid anchors, by integration of a simple washing protocol to remove soluble proteins. Mass spectrometry imaging revealed that washing did not disrupt the spatial distributions of the membrane and membrane-associated proteins. Some delocalization of the remaining soluble proteins was observed. |
doi_str_mv | 10.1021/jacs.3c03454 |
format | Article |
fullrecord | <record><control><sourceid>proquest_pubme</sourceid><recordid>TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_10375469</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>2839253188</sourcerecordid><originalsourceid>FETCH-LOGICAL-a418t-6121a22c3f83a938cbd1a48c3f61feeef4136696f38b99f4ddc63c28a4d2aaf93</originalsourceid><addsrcrecordid>eNptUU1P3DAQtVARbIEbZ-RjDw34K17nVCGggMSXBIij5Thj8CqJt3ay0v57vNotpRKn0dO8eW9mHkKHlBxTwujJzNh0zC3hohRbaEJLRoqSMvkNTQghrJgqyXfR95RmGQqm6A7a5VNRVlySCWqffEoj4BeT3nz_iq-7eQwLSPjODH4B-LSrPfQDvjUp4cc52CGGDoa4xOcwZORDj4PDt9DV0fSAH2IYwPcJn_uY2-0SuzyA1y77aNuZNsHBpu6h598XT2dXxc395fXZ6U1hBFVDISmjhjHLneKm4srWDTVCZSypAwAnKJeyko6ruqqcaBoruWXKiIYZ4yq-h36tdedj3UFj8wHRtHoefWfiUgfj9f-d3r_p17DQlPBpKeRK4cdGIYY_I6RBdz5ZaNt8YxiTZopXrORUqUz9uabaGFKK4D58KNGrhPQqIb1JKNOPPu_2Qf4byT_r1dQsjLHPr_pa6x2mzZzb</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>2839253188</pqid></control><display><type>article</type><title>Tissue Washing Improves Native Ambient Mass Spectrometry Detection of Membrane Proteins Directly from Tissue</title><source>MEDLINE</source><source>ACS Publications</source><creator>Sisley, Emma K. ; Hale, Oliver J. ; Hughes, James W. ; Cooper, Helen J.</creator><creatorcontrib>Sisley, Emma K. ; Hale, Oliver J. ; Hughes, James W. ; Cooper, Helen J.</creatorcontrib><description>Native ambient mass spectrometry enables the in situ analysis of proteins and their complexes directly from tissue, providing both structural and spatial information. Until recently, the approach was applied exclusively to the analysis of soluble proteins; however, there is a drive for new techniques that enable analysis of membrane proteins. Here we demonstrate native ambient mass spectrometry of membrane proteins, including β-barrel and α-helical (single and multipass) integral membrane proteins and membrane-associated proteins incorporating lipid anchors, by integration of a simple washing protocol to remove soluble proteins. Mass spectrometry imaging revealed that washing did not disrupt the spatial distributions of the membrane and membrane-associated proteins. Some delocalization of the remaining soluble proteins was observed.</description><identifier>ISSN: 0002-7863</identifier><identifier>EISSN: 1520-5126</identifier><identifier>DOI: 10.1021/jacs.3c03454</identifier><identifier>PMID: 37459360</identifier><language>eng</language><publisher>United States: American Chemical Society</publisher><subject>Communication ; Mass Spectrometry - methods ; Membrane Proteins - chemistry</subject><ispartof>Journal of the American Chemical Society, 2023-07, Vol.145 (29), p.15658-15662</ispartof><rights>2023 The Authors. Published by American Chemical Society</rights><rights>2023 The Authors. Published by American Chemical Society 2023 The Authors</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-a418t-6121a22c3f83a938cbd1a48c3f61feeef4136696f38b99f4ddc63c28a4d2aaf93</citedby><cites>FETCH-LOGICAL-a418t-6121a22c3f83a938cbd1a48c3f61feeef4136696f38b99f4ddc63c28a4d2aaf93</cites><orcidid>0000-0001-8721-3348 ; 0000-0003-4590-9384 ; 0000-0002-2286-5780</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://pubs.acs.org/doi/pdf/10.1021/jacs.3c03454$$EPDF$$P50$$Gacs$$H</linktopdf><linktohtml>$$Uhttps://pubs.acs.org/doi/10.1021/jacs.3c03454$$EHTML$$P50$$Gacs$$H</linktohtml><link.rule.ids>230,314,777,781,882,2752,27057,27905,27906,56719,56769</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/37459360$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Sisley, Emma K.</creatorcontrib><creatorcontrib>Hale, Oliver J.</creatorcontrib><creatorcontrib>Hughes, James W.</creatorcontrib><creatorcontrib>Cooper, Helen J.</creatorcontrib><title>Tissue Washing Improves Native Ambient Mass Spectrometry Detection of Membrane Proteins Directly from Tissue</title><title>Journal of the American Chemical Society</title><addtitle>J. Am. Chem. Soc</addtitle><description>Native ambient mass spectrometry enables the in situ analysis of proteins and their complexes directly from tissue, providing both structural and spatial information. Until recently, the approach was applied exclusively to the analysis of soluble proteins; however, there is a drive for new techniques that enable analysis of membrane proteins. Here we demonstrate native ambient mass spectrometry of membrane proteins, including β-barrel and α-helical (single and multipass) integral membrane proteins and membrane-associated proteins incorporating lipid anchors, by integration of a simple washing protocol to remove soluble proteins. Mass spectrometry imaging revealed that washing did not disrupt the spatial distributions of the membrane and membrane-associated proteins. Some delocalization of the remaining soluble proteins was observed.</description><subject>Communication</subject><subject>Mass Spectrometry - methods</subject><subject>Membrane Proteins - chemistry</subject><issn>0002-7863</issn><issn>1520-5126</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2023</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNptUU1P3DAQtVARbIEbZ-RjDw34K17nVCGggMSXBIij5Thj8CqJt3ay0v57vNotpRKn0dO8eW9mHkKHlBxTwujJzNh0zC3hohRbaEJLRoqSMvkNTQghrJgqyXfR95RmGQqm6A7a5VNRVlySCWqffEoj4BeT3nz_iq-7eQwLSPjODH4B-LSrPfQDvjUp4cc52CGGDoa4xOcwZORDj4PDt9DV0fSAH2IYwPcJn_uY2-0SuzyA1y77aNuZNsHBpu6h598XT2dXxc395fXZ6U1hBFVDISmjhjHLneKm4srWDTVCZSypAwAnKJeyko6ruqqcaBoruWXKiIYZ4yq-h36tdedj3UFj8wHRtHoefWfiUgfj9f-d3r_p17DQlPBpKeRK4cdGIYY_I6RBdz5ZaNt8YxiTZopXrORUqUz9uabaGFKK4D58KNGrhPQqIb1JKNOPPu_2Qf4byT_r1dQsjLHPr_pa6x2mzZzb</recordid><startdate>20230726</startdate><enddate>20230726</enddate><creator>Sisley, Emma K.</creator><creator>Hale, Oliver J.</creator><creator>Hughes, James W.</creator><creator>Cooper, Helen J.</creator><general>American Chemical Society</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><scope>5PM</scope><orcidid>https://orcid.org/0000-0001-8721-3348</orcidid><orcidid>https://orcid.org/0000-0003-4590-9384</orcidid><orcidid>https://orcid.org/0000-0002-2286-5780</orcidid></search><sort><creationdate>20230726</creationdate><title>Tissue Washing Improves Native Ambient Mass Spectrometry Detection of Membrane Proteins Directly from Tissue</title><author>Sisley, Emma K. ; Hale, Oliver J. ; Hughes, James W. ; Cooper, Helen J.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a418t-6121a22c3f83a938cbd1a48c3f61feeef4136696f38b99f4ddc63c28a4d2aaf93</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2023</creationdate><topic>Communication</topic><topic>Mass Spectrometry - methods</topic><topic>Membrane Proteins - chemistry</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Sisley, Emma K.</creatorcontrib><creatorcontrib>Hale, Oliver J.</creatorcontrib><creatorcontrib>Hughes, James W.</creatorcontrib><creatorcontrib>Cooper, Helen J.</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><collection>PubMed Central (Full Participant titles)</collection><jtitle>Journal of the American Chemical Society</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Sisley, Emma K.</au><au>Hale, Oliver J.</au><au>Hughes, James W.</au><au>Cooper, Helen J.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Tissue Washing Improves Native Ambient Mass Spectrometry Detection of Membrane Proteins Directly from Tissue</atitle><jtitle>Journal of the American Chemical Society</jtitle><addtitle>J. Am. Chem. Soc</addtitle><date>2023-07-26</date><risdate>2023</risdate><volume>145</volume><issue>29</issue><spage>15658</spage><epage>15662</epage><pages>15658-15662</pages><issn>0002-7863</issn><eissn>1520-5126</eissn><abstract>Native ambient mass spectrometry enables the in situ analysis of proteins and their complexes directly from tissue, providing both structural and spatial information. Until recently, the approach was applied exclusively to the analysis of soluble proteins; however, there is a drive for new techniques that enable analysis of membrane proteins. Here we demonstrate native ambient mass spectrometry of membrane proteins, including β-barrel and α-helical (single and multipass) integral membrane proteins and membrane-associated proteins incorporating lipid anchors, by integration of a simple washing protocol to remove soluble proteins. Mass spectrometry imaging revealed that washing did not disrupt the spatial distributions of the membrane and membrane-associated proteins. Some delocalization of the remaining soluble proteins was observed.</abstract><cop>United States</cop><pub>American Chemical Society</pub><pmid>37459360</pmid><doi>10.1021/jacs.3c03454</doi><tpages>5</tpages><orcidid>https://orcid.org/0000-0001-8721-3348</orcidid><orcidid>https://orcid.org/0000-0003-4590-9384</orcidid><orcidid>https://orcid.org/0000-0002-2286-5780</orcidid><oa>free_for_read</oa></addata></record> |
fulltext | fulltext |
identifier | ISSN: 0002-7863 |
ispartof | Journal of the American Chemical Society, 2023-07, Vol.145 (29), p.15658-15662 |
issn | 0002-7863 1520-5126 |
language | eng |
recordid | cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_10375469 |
source | MEDLINE; ACS Publications |
subjects | Communication Mass Spectrometry - methods Membrane Proteins - chemistry |
title | Tissue Washing Improves Native Ambient Mass Spectrometry Detection of Membrane Proteins Directly from Tissue |
url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-19T16%3A08%3A25IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_pubme&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Tissue%20Washing%20Improves%20Native%20Ambient%20Mass%20Spectrometry%20Detection%20of%20Membrane%20Proteins%20Directly%20from%20Tissue&rft.jtitle=Journal%20of%20the%20American%20Chemical%20Society&rft.au=Sisley,%20Emma%20K.&rft.date=2023-07-26&rft.volume=145&rft.issue=29&rft.spage=15658&rft.epage=15662&rft.pages=15658-15662&rft.issn=0002-7863&rft.eissn=1520-5126&rft_id=info:doi/10.1021/jacs.3c03454&rft_dat=%3Cproquest_pubme%3E2839253188%3C/proquest_pubme%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=2839253188&rft_id=info:pmid/37459360&rfr_iscdi=true |