Apolipoprotein-E degradation in human very low density lipoproteins by plasma protease(s): Chemical and biological consequences Academic Article Article uri icon

Overview

MeSH Major

  • Obesity
  • Thinness
  • Weight Gain

abstract

  • 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. © 1982.

publication date

  • December 31, 1982

Research

keywords

  • Academic Article

Identity

Digital Object Identifier (DOI)

  • 10.1016/0006-291X(82)91927-1

PubMed ID

  • 6301435

Additional Document Info

start page

  • 1360

end page

  • 7

volume

  • 109

number

  • 4