Binding characteristics of high density lipoprotein subclasses to porcine liver, adrenal and skeletal muscle plasma membranes

1. 1. We compared binding characteristics of 125I-labeled high density lipoprotein (HDL) subclasses to porcine liver, adrenal and skeletal muscle plasma membranes. 2. 2. HDL subclasses were discriminated by their buoyant densities (HDL 2 and HDL 3) or by their apolipoprotein (apo) content (Lp-AI (pa...

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Veröffentlicht in:International journal of biochemistry 1989, Vol.21 (6), p.649-656
Hauptverfasser: De Crom, M.P.G., Van Haperen, M.J., Puchois, P., Fruchart, J.-C., Van Gent, T., Van Tol, A., Van Der Kamp, A.W.M.
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Sprache:eng
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Zusammenfassung:1. 1. We compared binding characteristics of 125I-labeled high density lipoprotein (HDL) subclasses to porcine liver, adrenal and skeletal muscle plasma membranes. 2. 2. HDL subclasses were discriminated by their buoyant densities (HDL 2 and HDL 3) or by their apolipoprotein (apo) content (Lp-AI (particles containing apoA-I but no apoA-II) and LpA-I/A-II (particles containing both apoA-I and apoA-II)). 3. 3. HDL 2 and HDL 3 showed saturable binding to the three types of membrane preparations. 4. 4. No differences were found in the K ds within one HDL subclass. 5. 5. K ds and maximal binding of HDL 2 were lower than these of HDL 3. Unlabeled HDL 2 and HDL 3, but not LDL, effectively displaced 125I-HDL 2 and 125I-HDL 3. 6. 6. Binding of HDL was independent of the concentration of Nad and did not require calcium. 7. 7. These results suggest a process mediated by a single specific receptor in porcine liver, adrenal and skeletal muscle plasma membranes. 8. 8. We also studied binding characteristics of HDL subclasses Lp-AI and LpA-I/A-II to porcine liver membranes. LpA-I showed the highest K d and maximal binding. 9. 9. All types of HDL subclasses studied (i.e. HDL 2, HDL 3, LpA-I and LpA-I/A-II) effectively competed for binding of both Lp-AI and LpA-I/A-II, suggesting that the HDL subclasses studied bind to the same receptor by their apoA-I moiety.
ISSN:0020-711X
DOI:10.1016/0020-711X(89)90385-6