Abnormal interaction of the human apolipoprotein A-I variant [Lys107→0] with high density lipoproteins

Gabriel Ponsin, Antonio Gotto, Gerd Utermann, Henry J. Pownall

Research output: Contribution to journalArticle

6 Scopus citations

Abstract

Several isoforms of apoprotein A-I [apoA-I], the major apoprotein of high density lipoproteins [HDL], have been described. We compared the in vivo and in vitro properties of normal human apoA-I with those of apoA-I [Lys107→0]. Fluorescence and circular dichroic spectra showed that deletion of Lys107 decreases apoprotein self-association. In vivo metabolic studies in the rat indicated that the interaction of apoA-I [Lys107→0] with HDL was lower than normal. We conclude that deletion of Lys107 results in a reorganization of the apoprotein structure that decreases its potential to form hydrophobic associations.

Original languageEnglish (US)
Pages (from-to)856-862
Number of pages7
JournalBiochemical and Biophysical Research Communications
Volume133
Issue number3
DOIs
StatePublished - Dec 31 1985

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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