{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Su P"],"funding":["NIDA NIH HHS","NIDDK NIH HHS","NIEHS NIH HHS","NCI NIH HHS","NIGMS NIH HHS"],"pagination":["eabp9929"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9365283"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["8(32)"],"pubmed_abstract":["Imaging of proteoforms in human tissues is hindered by low molecular specificity and limited proteome coverage. Here, we introduce proteoform imaging mass spectrometry (PiMS), which increases the size limit for proteoform detection and identification by fourfold compared to reported methods and reveals tissue localization of proteoforms at <80-μm spatial resolution. PiMS advances proteoform imaging by combining ambient nanospray desorption electrospray ionization with ion detection using individual ion mass spectrometry. We demonstrate highly multiplexed proteoform imaging of human kidney, annotating 169 of 400 proteoforms of <70 kDa using top-down MS and a database lookup of ~1000 kidney candidate proteoforms, including dozens of key enzymes in primary metabolism. PiMS images reveal distinct spatial localizations of proteoforms to both anatomical structures and cellular neighborhoods in the vasculature, medulla, and cortex regions of the human kidney. The benefits of PiMS are poised to increase proteome coverage for label-free protein imaging of tissues."],"journal":["Science advances"],"pubmed_title":["Highly multiplexed, label-free proteoform imaging of tissues by individual ion mass spectrometry."],"pmcid":["PMC9365283"],"funding_grant_id":["U54 DK120058","T32 ES007028","P30 CA060553","P30 DA018310","UH3 CA246635","UH3 CA255132","P41 GM108569","F32 CA246894"],"pubmed_authors":["Camarillo JM","Allen JL","Neumann EK","Drown BS","Yang M","Greer JB","Hollas MAR","Kafader JO","Fellers RT","Spraggins JM","Durbin KR","Early BP","Laskin J","Su P","McGee JP","Kelleher NL","Butun FA"],"additional_accession":[]},"is_claimable":false,"name":"Highly multiplexed, label-free proteoform imaging of tissues by individual ion mass spectrometry.","description":"Imaging of proteoforms in human tissues is hindered by low molecular specificity and limited proteome coverage. Here, we introduce proteoform imaging mass spectrometry (PiMS), which increases the size limit for proteoform detection and identification by fourfold compared to reported methods and reveals tissue localization of proteoforms at <80-μm spatial resolution. PiMS advances proteoform imaging by combining ambient nanospray desorption electrospray ionization with ion detection using individual ion mass spectrometry. We demonstrate highly multiplexed proteoform imaging of human kidney, annotating 169 of 400 proteoforms of <70 kDa using top-down MS and a database lookup of ~1000 kidney candidate proteoforms, including dozens of key enzymes in primary metabolism. PiMS images reveal distinct spatial localizations of proteoforms to both anatomical structures and cellular neighborhoods in the vasculature, medulla, and cortex regions of the human kidney. The benefits of PiMS are poised to increase proteome coverage for label-free protein imaging of tissues.","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Aug","modification":"2024-11-07T00:40:39.365Z","creation":"2024-11-07T00:40:39.365Z"},"accession":"S-EPMC9365283","cross_references":{"pubmed":["35947651"],"doi":["10.1126/sciadv.abp9929"]}}