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Gewählte Publikation:
SHR Neuro Krebs Kardio Lipid Stoffw Microb
Krisko, A; Piantanida, I; Kveder, M; Pifat, G; Lee, A; Greilberger, J; Kipmen-Korgun, D; Jürgens, G.
The effect of heparin on structural and functional properties of low density lipoproteins.
BIOPHYS CHEM. 2006; 119(3): 234-239.
Doi: 10.1016/j.bpc.2005.09.011
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PubMed
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- Co-Autor*innen der Med Uni Graz
- Greilberger Joachim
- Jürgens Günther
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- Abstract:
- Heparin binding to human low density lipoproteins (LDL) and the effect of heparin on the ability of LDL to bind to the LDL receptor has been investigated. Emphasis has been made on the physiological conditions of temperature, pH and the ionic strength. Intrinsic fluorescence spectroscopy of LDL has been applied to follow heparin binding. Fluorescence anisotropy has been measured to describe the changes in apoB and dansyl-heparin dynamics upon binding. Eu3+-labeled LDL binding to the intact LDL receptor has been monitored by time-resolved fluorescence spectroscopy technique. We have found that heparin binds to LDL under the physiological conditions, probably by Van der Waals interactions and hydrogen bonding. Temperature seems to be the most important factor influencing the interaction. Furthermore, the presence of heparin inhibits LDL binding to the intact LDL receptor that might have consequences on the cholesterol metabolism in vivo.
- Find related publications in this database (using NLM MeSH Indexing)
- Apolipoproteins B - metabolism
- Cells, Cultured - drug effects
- Europium - metabolism
- Fibrinolytic Agents - pharmacology
- Fluorescence Polarization - pharmacology
- Heparin - analogs and derivatives
- Humans - analogs and derivatives
- Hydrogen Bonding - analogs and derivatives
- Hydrogen-Ion Concentration - analogs and derivatives
- Kidney - metabolism
- Lipoproteins, LDL - chemistry
- Receptors, LDL - metabolism
- Spectrometry, Fluorescence - metabolism
- Temperature - metabolism
- Find related publications in this database (Keywords)
- LDL
- heparin
- fluorescence
- LDL receptor
- binding