Relevance of the amino acid conversions L144R (Zaragoza) and L159P (Zavalla) in the apolipoprotein A-I binding site for haptoglobin

Luisa Cigliano, Luca D. D'Andrea, Bernardetta Maresca, Milena Serino, Alessandro Carlucci, Alfonso Salvatore, Maria Stefania Spagnuolo, Graziana Scigliuolo, Carlo Pedone, Paolo Abrescia

Research output: Contribution to journalArticlepeer-review


The high-density lipoprotein apolipoprotein A-I (ApoA-I) stimulates the enzyme lecithin-cholesterol acyltransferase (LCAT) in the reverse cholesterol transport pathway. Two ApoA-I variants, Zaragoza (L144R) and Zavalla (L159P), are associated with low levels of HDL-cholesterol but normal LCAT activity. Haptoglobin interacts with ApoA-I, impairing LCAT stimulation. Synthetic peptides matching the haptoglobin-binding site of native or variant ApoA-I (native, P2a; variants, Zav-pep and Zar-pep) bound haptoglobin with different activity: Zar-pep>P2a>Zav-pep. They also differently rescued LCAT in vitro activity in the presence of haptoglobin (P2a=Zar-pep>Zav-pep). Therefore, both amino acid conversions affect haptoglobin binding and LCAT regulation. We highlight the role of haptoglobin in LCAT regulation in subjects with ApoA-I variants.

Original languageEnglish
Pages (from-to)1421-1426
Number of pages6
JournalBiological Chemistry
Issue number11
Publication statusPublished - Nov 1 2008


  • ApoA-I Zaragoza
  • ApoA-I Zavalla
  • High-density lipoprotein
  • Lecithin-cholesterol acyltransferase
  • Peptides
  • Reverse cholesterol transport

ASJC Scopus subject areas

  • Biochemistry
  • Clinical Biochemistry
  • Molecular Biology


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