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

William A. Bradley, Ellen B. Gilliam, Antonio Gotto, Sandra H. Gianturco

Research output: Contribution to journalArticle

38 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)1360-1367
Number of pages8
JournalBiochemical and Biophysical Research Communications
Volume109
Issue number4
DOIs
StatePublished - Dec 31 1982

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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