Biliverdin is the endogenous ligand of human serum α1-acid glycoprotein

Research output: Contribution to journalArticle

14 Citations (Scopus)

Abstract

α1-Acid glycoprotein (AAG), an acute phase component of the human serum, is a prominent member of the lipocalin family of proteins showing inflammatory/immunomodulatory activities and promiscuous drug binding properties. Both three-dimensional structure of AAG and its precise biological function are still unknown and only a few endogenous AAG ligands have been described to date. CD spectroscopic studies performed with commercial AAG and the separated genetic variants revealed high-affinity binding of biliverdin (BV) and biliverdin dimethyl ester to the 'F1/S' fraction of the protein. The preferential accommodation of the right-handed, P-helicity conformers of the pigments by the protein matrix resulted in strong induced CD activity, which was utilized for estimation of the binding parameters and to locate the binding site. It was concluded that both pigments are bound in the central β-barrel cavity of AAG, held principally by hydrophobic interactions. Possible biological implications of the BV binding ability of AAG with special emphasis on the heme oxygenase-1 pathway are discussed.

Original languageEnglish
Pages (from-to)503-507
Number of pages5
JournalBiochemical and Biophysical Research Communications
Volume372
Issue number3
DOIs
Publication statusPublished - Aug 1 2008

Fingerprint

Biliverdine
Glycoproteins
Ligands
Pigments
Acids
Serum
Lipocalins
Proteins
Heme Oxygenase-1
Aptitude
Acute-Phase Proteins
Protein S
Hydrophobic and Hydrophilic Interactions
Esters
Binding Sites
Pharmaceutical Preparations

Keywords

  • Acute phase reaction
  • Biliverdin
  • Genetic variants
  • Human serum α-acid glycoprotein
  • Induced circular dichroism
  • Lipocalin

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Biliverdin is the endogenous ligand of human serum α1-acid glycoprotein. / Zsila, F.; Mády, G.

In: Biochemical and Biophysical Research Communications, Vol. 372, No. 3, 01.08.2008, p. 503-507.

Research output: Contribution to journalArticle

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