Serine proteases coisolate with human very low density lipoproteins (VLDL) which degrade apolipoprotein E and cause hypertriglyceridemic VLDL to lose the ability to interact with the LDL receptor of human skin fibroblasts. We identified proteolytic fragments of apolipoprotein-E in isolated VLDL which can be produced by the action of thrombin on purified apoE. There are two major thrombin cleavage products: Mr ∼ 22,000 (E-22) and Mr ∼ 12,000 (E-12), the N- and C-terminal fragments, respectively, of apoE. We conclude that the structural integrity and the ability of VLDL to interact with cell receptors are a function of not only VLDL constituents but also of the extent to which VLDL apoprotein E has been degraded.
|Original language||English (US)|
|Number of pages||8|
|Journal||Biochemical and Biophysical Research Communications|
|State||Published - Dec 31 1982|
ASJC Scopus subject areas
- Molecular Biology
- Cell Biology