PARTICIPATION OF APOLIPOPROTEIN E IN TRANSFER AND ABSORPTION OF FATTY ACIDS BY THE CELLS And CAUSING OF HYPERLIPOPROTEINEMIA

Abstract

ApoE vector protein in association with apoB-100 directly transferring saturated and monounsaturated FA (SFA and MFA) in triglyceride form (composed of very low density lipoproteins (L)) to the cells which are assimilating FA by cooperative receptors of apoE. Only insulin dependent cells have apoe/B-l00 receptors on the cell membrane (skeletal myocytes, cardiac myocytes, periportal hepatocytes, adipocytes of subcutaneous fat and Kupffer's macrophages). Phylogenetically late apoE has a domain for protein-protein interaction unlike the other apos. Apo forms cooperative ligands: apoE/A-l, apoE/B-48 and apoE/B-100 while using this domain. At later stages of phylogenesis while apoE forms cooperative ligands it is also involved in cell transfer and absorption of polyunsatured essential fatty acids in high density L, SFA +MFA +unsatured FA in chylomicrons, SFA+MFA in very low density L. Phenotype E 33 appears to be regular. Phenotypes E2/2 and E4/4 are cause of hypertriglyceridemia of I and V types, which call destructive inflammation of arterial intima with atherothrombosis.