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Related Experiment Video

Updated: May 31, 2026

Endotoxin Activity Assay for the Detection of Whole Blood Endotoxemia in Critically Ill Patients
06:28

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Published on: June 24, 2019

High-density lipoprotein proteome dynamics in human endotoxemia.

Johannes Hm Levels1, Pierre Geurts, Helen Karlsson

  • 1Department of Experimental Vascular Medicine, Academic Medical Center, University of Amsterdam, Amsterdam, the Netherlands. h.levels@amc.uva.nl.

Proteome Science
|June 30, 2011
PubMed
Summary

High-density lipoprotein (HDL) proteome changes after endotoxin (LPS) challenge did not differ between individuals with low and high HDL cholesterol. Hierarchical clustering, not HDL proteome differences, may predict HDL functionality during acute phase responses.

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Area of Science:

  • Biochemistry
  • Immunology
  • Proteomics

Background:

  • High-density lipoprotein (HDL) is linked to inflammation, coagulation, and lipid metabolism.
  • Changes in the HDL proteome may influence HDL's diverse functions.
  • Low HDL cholesterol levels are associated with increased susceptibility to inflammatory challenges.

Purpose of the Study:

  • To investigate dynamic changes in the HDL proteome following a low-dose endotoxin (LPS) challenge.
  • To determine if differences in the HDL proteome explain varying susceptibility to LPS between individuals with low and high HDL cholesterol.
  • To explore the relationship between HDL protein composition and acute phase response.

Main Methods:

  • Surface-Enhanced Laser Desorption/Ionization Time-Of-Flight mass spectrometry (SELDI-TOF MS) was used to profile HDL proteins.
  • HDL was isolated from plasma collected over 24 hours post-LPS challenge in healthy men with low and high HDL cholesterol.
  • Proteomic data underwent hierarchical clustering and was correlated with paraoxonase 1 activity and serum amyloid A-1/2 (SAA-1/2) levels.

Main Results:

  • Profound changes in 21 HDL protein markers were observed within 1 hour of LPS administration, sustained for 24 hours, with no significant differences between low and high HDL groups.
  • Hierarchical clustering revealed three distinct protein profile clusters, independent of baseline HDL cholesterol but correlated with paraoxonase 1 activity.
  • Serum amyloid A-1/2 (SAA-1/2) was upregulated post-LPS, with variations in response and time-course of truncated variants observed in one cluster.

Conclusions:

  • Semi-quantitative differences in the HDL proteome do not explain the differential susceptibility to LPS observed between low and high HDL cholesterol groups.
  • Hierarchical clustering of HDL protein profiles shows potential for predicting HDL functionality during acute phase responses to LPS.
  • The study highlights the complexity of HDL's role in the inflammatory response beyond simple proteomic composition.