Search bioRxiv⌕ Search

bioRxiv · 10.64898/2026.03.11.711200

Combining Anion Exchange and Size Exclusion Chromatography for Extracellular Vesicle Enrichment from Small Volumes of Human and Mouse Plasma for Quantitative Proteomics

Abstract

Extracellular vesicles (EVs) are promising biomarkers, yet their proteomic analysis from plasma is hampered by low abundance and co-purification of contaminants (e.g., lipoproteins, platelets) and technical variability, particularly in small-volume animal models. We developed and validated a modular protocol integrating Size Exclusion Chromatography (SEC) with Strong Anion Exchange (SEC-SAX) specifically tailored for quantitative LC-MS proteomics from small starting volumes (150 l of plasma). SEC alone successfully removed 99% of Albumin, and the SAX step significantly enriched EVs over contaminating lipoproteins. Downstream single pot solid phase enhanced (SP3) sample prep and STAGE tip solid phase extraction ensured maximum proteome depth. Critical confounding factors were objectively assessed: Platelet Factor 4 (PF4) was confirmed as a highly sensitive platelet marker, confirming the necessity of meticulous plasma preparation. Sample hemolysis impacted the plasma EV proteome data. As such, an objective measure (nanodrop spectrophotometer) of hemolysis and exclusion of hemolysed samples (heme >0.3 mg/ml) is recommended. The protocol is applicable to both human and mouse plasma as demonstrated by EV enrichment and quantification of biomarker proteins associated with neurodegenerative diseases from eight individual mouse plasma samples. Manuscript HighlightsO_LIDevelopmental workflow for a quantitative SEC-SAX protocol for EV proteomics from small plasma volumes (150 l). C_LIO_LIA range of variables tested including SAX beads amount, digestion buffer, digestion time, STAGE tip solid phase extraction, SAX elution buffer and sample filtration. C_LIO_LIThe SAX step significantly enhances EV proteome depth by increasing EV purity in relation to ApoB lipoproteins. C_LIO_LIShows the impact of the major confounding factors of sample hemolysis and platelet contamination on the EV proteome. C_LIO_LIPlatelet contamination increases the number and abundance of proteins detected including known disease biomarkers and sample hemolysis is associated with proteins derived from platelet and red blood cell derived EVs. C_LIO_LIPlatelet Factor 4 (PF4) is identified and confirmed as a sensitive marker for platelet contamination. C_LIO_LIApplicable to both human and mouse plasma. C_LI

Explore related subjects

Keep this discovery

Explore connections, maps & timelines

BibTeXRIS

Dunlop, F. M., Mason, S., Hafizi Rastabi, N., Alexander, S. E., Robatjazi, S., Davis, J., Laird, C., Kang, T., Mathivanan, S. E., Russell, A. P.. 2026-03-14. Combining Anion Exchange and Size Exclusion Chromatography for Extracellular Vesicle Enrichment from Small Volumes of Human and Mouse Plasma for Quantitative Proteomics. https://doi.org/10.64898/2026.03.11.711200

Cite the original work for its findings. Save a collection to share your selection of sources.

KEEP EXPLORING

Related preprints

A G-Quadruplex Containing First Intron Harbors a Functional Polyadenylation Signal in TP53

First introns of mammalian genes are often longer than other introns and may contain regulatory elements, suggesting that they may have roles in gene regulation. We detected a previously unannotated, low abundance intronic transcript, TP53-INT1, using long-read direct RNA sequencing data. TP53-INT1 has low coding potential and terminates within the first and longest intron of TP53. The transcript structure and 3'-end were validated by independent experimental and in silico evidence. We identified a canonical polyadenylation signal upstream of the transcript termination site and demonstrated its functionality using reporter assays. Furthermore, a potential G-quadruplex (G4)-forming sequence was identified upstream of this polyadenylation signal. The G4-forming potential was confirmed using spectroscopic and thermal stability analyses. Complementing the in vitro characterizations, treatment with Pyridostatin, a G4-stabilizing drug, was associated with decreased TP53 expression. Together, these findings characterize a previously unannotated TP53 intronic transcript and reveal a local genomic context combining accessible chromatin, a functional polyadenylation signal, and a potential G4-forming sequence that may influence full-length transcription.

molecular biology↗

An architectural RNA builds a reaction crucible through molecular concentration and activated enzyme selection

Architectural RNAs (arcRNAs) scaffold membraneless organelles (MLOs), yet how they organize functional proteins remains unclear. Nuclear stress bodies (nSBs), MLOs scaffolded by HSATIII arcRNAs, incorporate SRSFs during stress. During stress recovery, nSBs function as reaction crucibles that recruit the kinase CLK1 to accelerate SRSF rephosphorylation and normalize stress-induced splicing. Here, we identify the ASAP complex as a recruitment factor that recognizes Ser341-phosphorylated, catalytically activated CLK1. HSATIII-bound SRSFs recruit ASAP, assembling a platform for CLK1 recruitment. Biochemical reconstitution reveals that this platform enhances SRSF phosphorylation by concentrating SRSFs and CLK1 while selectively recruiting activated CLK1, establishing nSB reaction crucibles as molecular concentrators and selectors. The SRSF-ASAP-CLK1 interaction network is conserved between humans and mice, suggesting that primate-specific HSATIII arcRNAs co-opted this pre-existing network to establish reaction-crucible function in nSBs. Our findings reveal how arcRNAs organize functional proteins through quantitative enrichment and qualitative selection to build biochemically active MLOs.

molecular biology↗

Adult-like thick-filament protein stoichiometry in immature human iPSC-derived cardiomyocytes

Human induced pluripotent stem cell-derived cardiomyocytes (iPSC-CMs) retain immature sarcomeric isoforms, raising questions about their ability to recapitulate the protein stoichiometry of adult human myocardium. We integrated two independent quantitative proteomic datasets of iPSC-CMs with published fetal and region-resolved adult human heart proteomes to compare sarcomeric protein abundance. Although iPSC-CMs clustered with fetal heart based on their global shared proteome and retained fetal troponin I expression, key thick-filament protein ratios closely matched those of adult myocardium. Myosin heavy-to-light chain ratios approached the expected 2:4 stoichiometry, while myosin-binding protein abundance relative to myosin heavy chains was comparable across iPSC-CMs and adult cardiac regions. These findings reveal that developmental immaturity in sarcomeric isoform expression does not entail altered thick-filament protein proportions. Preservation of adult-like myosin-binding protein stoichiometry supports the use of iPSC-CMs to investigate sarcomeric diseases associated with altered protein dosage, particularly MYBPC3-associated hypertrophic cardiomyopathy.

molecular biology↗