<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Guo Q</submitter><funding>NIA NIH HHS</funding><funding>Foundation for the National Institutes of Health</funding><funding>NINDS NIH HHS</funding><funding>National Institutes of Health</funding><funding>NIH HHS</funding><pagination>67</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC11460197</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>19(1)</volume><pubmed_abstract>&lt;h4>Introduction&lt;/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.&lt;h4>Methods&lt;/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</pubmed_abstract><journal>Molecular neurodegeneration</journal><pubmed_title>Heparin-enriched plasma proteome is significantly altered in Alzheimer's disease.</pubmed_title><pmcid>PMC11460197</pmcid><funding_grant_id>U01 AG061357</funding_grant_id><funding_grant_id>P30 AG066511</funding_grant_id><funding_grant_id>P30AG066511</funding_grant_id><funding_grant_id>AMP-AD 2.0</funding_grant_id><funding_grant_id>RF1 AG062181</funding_grant_id><funding_grant_id>U01AG061357</funding_grant_id><funding_grant_id>RF1AG062181</funding_grant_id><funding_grant_id>U01 NS128433</funding_grant_id><pubmed_authors>Ping L</pubmed_authors><pubmed_authors>Xu K</pubmed_authors><pubmed_authors>Duong DM</pubmed_authors><pubmed_authors>Roberts BR</pubmed_authors><pubmed_authors>Levey AI</pubmed_authors><pubmed_authors>Guo Q</pubmed_authors><pubmed_authors>Golde TE</pubmed_authors><pubmed_authors>Fox EJ</pubmed_authors><pubmed_authors>Seyfried NT</pubmed_authors><pubmed_authors>Shantaraman A</pubmed_authors><pubmed_authors>Dammer EB</pubmed_authors><pubmed_authors>Lah JJ</pubmed_authors><pubmed_authors>Yin L</pubmed_authors><pubmed_authors>Johnson ECB</pubmed_authors></additional><is_claimable>false</is_claimable><name>Heparin-enriched plasma proteome is significantly altered in Alzheimer's disease.</name><description>&lt;h4>Introduction&lt;/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.&lt;h4>Methods&lt;/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</description><dates><release>2024-01-01T00:00:00Z</release><publication>2024 Oct</publication><modification>2026-07-15T17:43:53.567Z</modification><creation>2026-07-07T03:10:47.293Z</creation></dates><accession>S-EPMC11460197</accession><cross_references><pubmed>39380021</pubmed><doi>10.1186/s13024-024-00757-1</doi></cross_references></HashMap>