liu.seSök publikationer i DiVA
Ändra sökning
RefereraExporteraLänk till posten
Permanent länk

Direktlänk
Referera
Referensformat
  • apa
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • oxford
  • Annat format
Fler format
Språk
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Annat språk
Fler språk
Utmatningsformat
  • html
  • text
  • asciidoc
  • rtf
High-density Lipoprotein proteome dynamics in human endotoxemia
Department of Experimental Vascular Medicine, Academic Medical Center, University of Amsterdam, Amsterdam, the Netherlands.
Department of Electrical Engineering and Computer Science & GIGA-research, University of Liège, Belgium.
Linköpings universitet, Institutionen för klinisk och experimentell medicin, Yrkes- och miljömedicin. Linköpings universitet, Hälsouniversitetet. Östergötlands Läns Landsting, Hjärt- och Medicincentrum, Arbets- och miljömedicin.
GIGA Bioinformatics Platform, University of Liège, Belgium.
Visa övriga samt affilieringar
2011 (Engelska)Ingår i: Proteome Science, ISSN 1477-5956, E-ISSN 1477-5956, Vol. 9, nr 34Artikel i tidskrift (Refereegranskat) Published
Abstract [en]

Background: A large variety of proteins involved in inflammation, coagulation, lipid-oxidation and lipid metabolism have been associated with high-density lipoprotein (HDL) and it is anticipated that changes in the HDL proteome have implications for the multiple functions of HDL. Here, SELDI-TOF mass spectrometry (MS) was used to study the dynamic changes of HDL protein composition in a human experimental low-dose endotoxemia model. Ten healthy men with low HDL cholesterol (0.7+/-0.1 mmol/L) and 10 men with high HDL cholesterol levels (1.9+/-0.4mmol/L) were challenged with endotoxin (LPS) intravenously (1ng/kg bodyweight). We previously showed that subjects with low HDL cholesterol are more susceptible to an inflammatory challenge. The current study tested the hypothesis that this discrepancy may be related to differences in the HDL proteome.

Results: Plasma drawn at 7 time-points over a 24 hour time period after LPS challenge was used for direct capture of HDL using antibodies against apolipoprotein A-I followed by subsequent SELDI-TOF MS profiling. Upon LPS administration, profound changes in 21 markers (adjusted p-value<0.05) were observed in the proteome in both study groups. These changes were observed 1 hour after LPS infusion and sustained up to 24 hours, but unexpectedly were not different between the 2 study groups. Hierarchical clustering of the protein spectra at all time points of all individuals revealed 3 distinct clusters, which were largely independent of baseline HDL cholesterol levels but correlated with paraoxonase 1 activity. The acute phase protein serum amyloid A-1/2 (SAA-1/2) was clearly upregulated after LPS infusion in both groups and comprised both native and N-terminal truncated variants that were identified by two-dimensional gel electrophoresis and mass spectrometry. Individuals of one of the clusters were distinguished by a lower SAA-1/2 response after LPS challenge and a delayed time-response of the truncated variants.

Conclusions: This study shows that the semi-quantitative differences in the HDL proteome as assessed by SELDI-TOF MS cannot explain why subjects with low HDL cholesterol are more susceptible to a challenge with LPS than those with high HDL cholesterol. Instead the results indicate that hierarchical clustering could be useful to predict HDL functionality in acute phase responses towards LPS.

Ort, förlag, år, upplaga, sidor
BiOMed Central , 2011. Vol. 9, nr 34
Nationell ämneskategori
Medicin och hälsovetenskap
Identifikatorer
URN: urn:nbn:se:liu:diva-69581DOI: 10.1186/1477-5956-9-34ISI: 000293378400001OAI: oai:DiVA.org:liu-69581DiVA, id: diva2:429165
Anmärkning

Original Publication: Johannes HM Levels, Pierre Geurts, Helen Karlsson, Raphaël Marée, Stefan Ljunggren, Louise Fornander, Louis Wehenkel, Mats Lindahl, Erik SG Stroes, Jan A Kuivenhoven and Joost CM Meijers, High-density Lipoprotein proteome dynamics in human endotoxemia, 2011, Proteome Science, (9), 34, . http://dx.doi.org/10.1186/1477-5956-9-34 Licensee: BioMed Central http://www.biomedcentral.com/

Tillgänglig från: 2011-07-04 Skapad: 2011-07-04 Senast uppdaterad: 2017-12-11Bibliografiskt granskad

Open Access i DiVA

fulltext(1734 kB)267 nedladdningar
Filinformation
Filnamn FULLTEXT01.pdfFilstorlek 1734 kBChecksumma SHA-512
c1543a9e708bf6c1bf2d9362af82cddcc05dcc30875bd42e8d6f27ca48dc6e645b3b3712d22b35df361f0ef8d4327c3f3c3b67b3ebb6c8ca84160a6280dc9ff3
Typ fulltextMimetyp application/pdf

Övriga länkar

Förlagets fulltext

Personposter BETA

Karlsson, HelenLjunggren, StefanFornander, LouiseLindahl, Mats

Sök vidare i DiVA

Av författaren/redaktören
Karlsson, HelenLjunggren, StefanFornander, LouiseLindahl, Mats
Av organisationen
Yrkes- och miljömedicinHälsouniversitetetArbets- och miljömedicin
I samma tidskrift
Proteome Science
Medicin och hälsovetenskap

Sök vidare utanför DiVA

GoogleGoogle Scholar
Totalt: 267 nedladdningar
Antalet nedladdningar är summan av nedladdningar för alla fulltexter. Det kan inkludera t.ex tidigare versioner som nu inte längre är tillgängliga.

doi
urn-nbn

Altmetricpoäng

doi
urn-nbn
Totalt: 286 träffar
RefereraExporteraLänk till posten
Permanent länk

Direktlänk
Referera
Referensformat
  • apa
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • oxford
  • Annat format
Fler format
Språk
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Annat språk
Fler språk
Utmatningsformat
  • html
  • text
  • asciidoc
  • rtf