Using ligand blotting techniques, with low-density lipoprotein (LDL) as ligand, we have previously described the existence of atypical lipoprotein-binding proteins (105 kDa and 130 kDa) in membranes from human aortic medial tissue. The present study demonstrates that these proteins are also present in membranes from cultured human (aortic and mesenteric) and rat (aortic) vascular smooth-muscle cells (VSMCs). To assess the relationship of 105 and 130 kDa lipoprotein-binding proteins to known lipoprotein receptors, ligand binding specificity was studied. We tested effects of substances known to antagonize ligand binding to either the LDL [apolipoprotein B,E (apo B,E)] receptor (dextran sulphate, heparin, pentosan polysulphate, protamine, spermine, histone), the scavenger receptor (dextran sulphate, fucoidin), the very-low-density-lipoprotein (VLDL) receptor [receptor-associated protein (RAP)], or LDL receptor-related protein (RAP, α2-macroglobulin, lipoprotein lipase, exotoxin-A). None of these substances, with the exception of dextran sulphate, influenced binding of LDL to either 105 or 130 kDa proteins. Sodium oleate or oleic acid, known stimuli for the lipoprotein binding activity of the lipolysis-stimulated receptor, were also without effect. LDL binding to 105 and 130 kDa proteins was inhibited by anti-LDL (apo B) antibodies. LDL and VLDL bound to 105 and 130 kDa proteins with similar affinities (蝶50 μg/ml). The unique ligand selectivity of 105 and 130 kDa proteins supports the existence of a novel lipoprotein-binding protein that is distinct from all other currently identified LDL receptor family members. The similar ligand selectivity of 105 and 130 kDa proteins suggests that they may represent variant forms of an atypical lipoprotein-binding protein.
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July 1996
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Research Article|
July 01 1996
Ligand selectivity of 105 kDa and 130 kDa lipoprotein-binding proteins in vascular-smooth-muscle-cell membranes is unique
Valery N. BOCHKOV;
Valery N. BOCHKOV
*Laboratory of Molecular Endocrinology, Institute of Experimental Cardiology, Cardiology Research Center, Moscow, Russia
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Vsevolod A. TKACHUK;
Vsevolod A. TKACHUK
*Laboratory of Molecular Endocrinology, Institute of Experimental Cardiology, Cardiology Research Center, Moscow, Russia
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Maria P. PHILIPPOVA;
Maria P. PHILIPPOVA
*Laboratory of Molecular Endocrinology, Institute of Experimental Cardiology, Cardiology Research Center, Moscow, Russia
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Dimitri V. STAMBOLSKY;
Dimitri V. STAMBOLSKY
*Laboratory of Molecular Endocrinology, Institute of Experimental Cardiology, Cardiology Research Center, Moscow, Russia
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Fritz R. BÜHLER;
Fritz R. BÜHLER
*Laboratory of Molecular Endocrinology, Institute of Experimental Cardiology, Cardiology Research Center, Moscow, Russia
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Thérèse J. RESINK
Thérèse J. RESINK
‡
†Department of Research, Basel University Hospital, CH 4031 Basel, Switzerland
‡To whom correspondence should be addressed.
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Publisher: Portland Press Ltd
Received:
November 02 1995
Revision Received:
March 11 1996
Accepted:
March 18 1996
Online ISSN: 1470-8728
Print ISSN: 0264-6021
The Biochemical Society, London © 1996
1996
Biochem J (1996) 317 (1): 297–304.
Article history
Received:
November 02 1995
Revision Received:
March 11 1996
Accepted:
March 18 1996
Citation
Valery N. BOCHKOV, Vsevolod A. TKACHUK, Maria P. PHILIPPOVA, Dimitri V. STAMBOLSKY, Fritz R. BÜHLER, Thérèse J. RESINK; Ligand selectivity of 105 kDa and 130 kDa lipoprotein-binding proteins in vascular-smooth-muscle-cell membranes is unique. Biochem J 1 July 1996; 317 (1): 297–304. doi: https://doi.org/10.1042/bj3170297
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