Chimera of Apolipophorin III and C-terminal Domain of Apolipoprotein E to Study Apolipoprotein Structure Function

Primary structure and comparative sequence analysis of an insect apolipoprotein. Apolipophorin-III from Manduca sexta.

The amino acid sequence of an insect apolipoprotein, apolipophorin-III from Manduca sexta, was determined by a combination of cDNA and protein sequencing. The mature hemolymph protein consists of 166 amino acids. The cDNA also encodes for an amino-terminal extension of 23 amino acids which is not represented in the mature hemolymph protein. The existence of a precursor protein was confirmed by ...

Lipids: Apolipoprotein A-1 Apolipoprotein A-II Apolipoprotein B Apolipoprotein C-II Apolipoprotein C-III Apolipoprotein E Cholesterol Direct HDL Cholesterol Direct LDL Cholesterol Lipoprotein (a) sLDL Triglycerides

Orientation and mode of lipid-binding interaction of human apolipoprotein E C-terminal domain.

ApoE (apolipoprotein E) is an anti-atherogenic lipid transport protein that plays an integral role in lipoprotein metabolism and cholesterol homoeostasis. Lipid association educes critical functional features of apoE, mediating reduction in plasma and cellular cholesterol levels. The 10-kDa CT (C-terminal) domain of apoE facilitates helix-helix interactions in lipid-free state to promote apoE s...

Apolipoprotein C-III displacement of apolipoprotein E from VLDL: effect of particle size.

ApoC-III and apoE are important determinants of intravascular lipolysis and clearance of triglyceride-rich chylomicrons and VLDL from the blood plasma. Interactions of these two apolipoproteins were studied by adding purified human apoC-III to human plasma at levels observed in hypertriglyceridemic subjects and incubating under specific conditions (2 h, 37 degrees C). As plasma concentrations o...

Association of Apolipoprotein E Polymorphism with Susceptibility to Multiple Sclerosis