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Cross-linking of apoproteins in high density lipoprotein by dimethylsuberimidate inhibits specific lipoprotein binding to membranes
Journal article   Open access   Peer reviewed

Cross-linking of apoproteins in high density lipoprotein by dimethylsuberimidate inhibits specific lipoprotein binding to membranes

G K Chacko, F H Mahlberg, W J Johnson and Duane Alexander Quistberg
Journal of lipid research, v 29(3), pp 319-324
01 Mar 1988
DOI: https://doi.org/10.1016/S0022-2275(20)38537-0
PMID: 3379343
Featured in Collection :   UN Sustainable Development Goals @ Drexel
url
https://doi.org/10.1016/s0022-2275(20)38537-0View
Published, Version of Record (VoR)CC BY V4.0,  Open
url
https://doi.org/10.1016/S0022-2275(20)38537-0View
Published, Version of Record (VoR) Open

Abstract

Apoprotein E-free high density lipoproteins (HDL) bind to various cells and cell membrane preparations with properties typical of ligand-receptor interactions. This specific binding can be inhibited by treatment of HDL with tetranitromethane (TNM). During treatment of HDL with TNM, in addition to the expected nitration of tyrosine residues, cross-linking of lipids to apoproteins and of apoproteins to each other occurs. We have recently shown that cross-linking of phospholipids to apoproteins is not responsible for the inhibition of binding (1987. Chacko, G. K., et al. J. Lipid Res. 28: 332-337). To determine the role of cross-linking of apoproteins to each other in the inhibition, we used the bifunctional reagent dimethylsuberimidate (DMS) to cross-link the apoproteins in HDL3. Over 80% of apoproteins in DMS-HDL3 were cross-linked, as analyzed by SDS-polyacrylamide gel electrophoresis. DMS-HDL3 was similar to control HDL3 in its lipid composition. Gel filtration chromatography did not reveal any significant difference in size between DMS-HDL3 and control HDL3. As determined by competitive binding with 125I-labeled HDL3, DMS-HDL3 was almost completely unable to bind specifically to rat liver plasma membranes and human skin fibroblasts. It is concluded from these results that TNM inhibits the specific binding of HDL3 to membranes by a mechanism that involves cross-linking of apoproteins to each other in HDL3 particles. This observation implies that the specific binding of HDL3 to cells may depend on the native quaternary structure of apoproteins in the HDL particle. Because of its reduced ability to bind to the specific binding sites, DMS-HDL3 may be useful for studies related to the functional aspects of HDL binding sites.

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Web of Science research areas
Biochemistry & Molecular Biology
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