Heller, Manfred; Stalder, Daniel; Schlappritzi, Evelyn; Hayn, Gertraud; Matter, Urs; Haeberli, André (2005). Mass spectrometry-based analytical tools for the molecular protein characterization of human plasma lipoproteins. Proteomics, 5(10), pp. 2619-30. Weinheim: Wiley-VCH 10.1002/pmic.200401233
Full text not available from this repository.Lipoproteins are a heterogeneous population of blood plasma particles composed of apolipoproteins and lipids. Lipoproteins transport exogenous and endogenous triglycerides and cholesterol from sites of absorption and formation to sites of storage and usage. Three major classes of lipoproteins are distinguished according to their density: high-density (HDL), low-density (LDL) and very low-density lipoproteins (VLDL). While HDLs contain mainly apolipoproteins of lower molecular weight, the two other classes contain apolipoprotein B and apolipoprotein (a) together with triglycerides and cholesterol. HDL concentrations were found to be inversely related to coronary heart disease and LDL/VLDL concentrations directly related. Although many studies have been published in this area, few have concentrated on the exact protein composition of lipoprotein particles. Lipoproteins were separated by density gradient ultracentrifugation into different subclasses. Native gel electrophoresis revealed different gel migration behaviour of the particles, with less dense particles having higher apparent hydrodynamic radii than denser particles. Apolipoprotein composition profiles were measured by matrix-assisted laser desorption/ionization-mass spectrometry on a macromizer instrument, equipped with the recently introduced cryodetector technology, and revealed differences in apolipoprotein composition between HDL subclasses. By combining these profiles with protein identifications from native and denaturing polyacrylamide gels by liquid chromatography-tandem mass spectrometry, we characterized comprehensively the exact protein composition of different lipoprotein particles. We concluded that the differential display of protein weight information acquired by macromizer mass spectrometry is an excellent tool for revealing structural variations of different lipoprotein particles, and hence the foundation is laid for the screening of cardiovascular disease risk factors associated with lipoproteins.
Item Type: |
Journal Article (Original Article) |
|---|---|
Division/Institute: |
04 Faculty of Medicine > Pre-clinic Human Medicine > BioMedical Research (DBMR) > Unit Childrens Hospital > Thromboselabor Kinderklinik [discontinued] |
UniBE Contributor: |
Heller, Manfred, Stalder, Daniel, Häberli, André |
ISSN: |
1615-9853 |
Publisher: |
Wiley-VCH |
Language: |
English |
Submitter: |
Factscience Import |
Date Deposited: |
04 Oct 2013 15:12 |
Last Modified: |
02 Mar 2023 23:23 |
Publisher DOI: |
10.1002/pmic.200401233 |
PubMed ID: |
15892164 |
Web of Science ID: |
000230363900014 |
URI: |
https://boris.unibe.ch/id/eprint/31666 (FactScience: 196314) |
Actions (login required)
 |
Edit item |