Enhanced binding of phospholipase-A2-modified low density lipoprotein by human adipocytes

Biochemistry and Cell Biology = Biochimie Et Biologie Cellulaire
M K NatarajanA Angel

Abstract

Recognition of low density lipoprotein (LDL) by human adipocytes is not dependent on the classical LDL (apoprotein B-E) receptor. To assess whether LDL phospholipids have a role in adipocyte-LDL interactions, binding studies were carried out with human LDL modified with cobra venom phospholipase A2 (PLA2) and freshly isolated adipocytes and purified adipocyte plasma membranes prepared from surgical biopsies. LDL incubated with PLA2 showed increased monoacylphospholipid content, decreased diacylphospholipid content, and increased anodic migration on agarose gel electrophoresis. LDL cholesterol, triglyceride, and protein content remained unchanged. Typically, modification of 16 and 47% of LDL phospholipids enhanced specific binding of 125I-labelled LDL to plasma membranes progressively from 3.1 micrograms LDL bound/mg membrane protein (control) to 5.8 and 28.2 micrograms LDL bound/mg membrane protein, respectively. Nonspecific binding was not altered significantly. Excess unlabelled native LDL and high density lipoprotein (HDL3) effectively inhibited binding of PLA2-modified LDL. Freshly isolated adipocytes also showed enhanced binding and uptake of PLA2-modified LDL (0.1 vs. 0.9 micrograms LDL/10(6) cells x 2 h), control vs. mod...Continue Reading

Citations

Jul 11, 1997·Atherosclerosis·E Hurt-Camejo, G Camejo
Jun 13, 2002·European Journal of Clinical Investigation·Werner JarossMario Menschikowski
Jun 24, 1998·Biochimica Et Biophysica Acta·J Hoover-Plow, P Skocir
Dec 1, 1995·Atherosclerosis·M MenschikowskiW Jaross

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