{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Guo Q"],"funding":["NIA NIH HHS","Foundation for the National Institutes of Health","NINDS NIH HHS","National Institutes of Health","NIH HHS"],"pagination":["67"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11460197"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["19(1)"],"pubmed_abstract":["<h4>Introduction</h4>Heparin binding proteins (HBPs) with roles in extracellular matrix assembly are strongly correlated to β-amyloid (Aβ) and tau pathology in Alzheimer's disease (AD) brain and cerebrospinal fluid (CSF). However, it remains challenging to detect these proteins in plasma using standard mass spectrometry-based proteomic approaches.<h4>Methods</h4>We employed heparin-affinity chromatography, followed by off-line fractionation and tandem mass tag mass spectrometry (TMT-MS), to enrich HBPs from plasma obtained from AD (n = 62) and control (n = 47) samples. These profiles were then correlated to Aβ, tau and phosphorylated tau (pTau) CSF biomarkers and plasma pTau181 from the same individuals, as well as a consensus brain proteome network to assess the overlap with AD brain path"],"journal":["Molecular neurodegeneration"],"pubmed_title":["Heparin-enriched plasma proteome is significantly altered in Alzheimer's disease."],"pmcid":["PMC11460197"],"funding_grant_id":["U01 AG061357","P30 AG066511","P30AG066511","AMP-AD 2.0","RF1 AG062181","U01AG061357","RF1AG062181","U01 NS128433"],"pubmed_authors":["Ping L","Xu K","Duong DM","Roberts BR","Levey AI","Guo Q","Golde TE","Fox EJ","Seyfried NT","Shantaraman A","Dammer EB","Lah JJ","Yin L","Johnson ECB"],"additional_accession":[]},"is_claimable":false,"name":"Heparin-enriched plasma proteome is significantly altered in Alzheimer's disease.","description":"<h4>Introduction</h4>Heparin binding proteins (HBPs) with roles in extracellular matrix assembly are strongly correlated to β-amyloid (Aβ) and tau pathology in Alzheimer's disease (AD) brain and cerebrospinal fluid (CSF). However, it remains challenging to detect these proteins in plasma using standard mass spectrometry-based proteomic approaches.<h4>Methods</h4>We employed heparin-affinity chromatography, followed by off-line fractionation and tandem mass tag mass spectrometry (TMT-MS), to enrich HBPs from plasma obtained from AD (n = 62) and control (n = 47) samples. These profiles were then correlated to Aβ, tau and phosphorylated tau (pTau) CSF biomarkers and plasma pTau181 from the same individuals, as well as a consensus brain proteome network to assess the overlap with AD brain path","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 Oct","modification":"2026-07-15T17:43:53.567Z","creation":"2026-07-07T03:10:47.293Z"},"accession":"S-EPMC11460197","cross_references":{"pubmed":["39380021"],"doi":["10.1186/s13024-024-00757-1"]}}