Mechanisms for the formation of protein-bound homocysteine in human plasma

Biochem Biophys Res Commun. 2000 Nov 2;277(3):668-74. doi: 10.1006/bbrc.2000.3723.

Abstract

Hyperhomocysteinemia is an independent risk factor for cardiovascular disease. Greater than 70% of homocysteine in circulation is protein-bound. An in vitro model system using human plasma has been developed to study mechanisms of protein-bound homocysteine formation and establish the equilibrium binding capacities of plasma for homocysteine. Addition of homocysteine to plasma caused an initial rapid displacement of cysteine and a subsequent increase in protein-bound homocysteine. This rapid reaction was followed by a slower oxygen-dependent reaction forming additional protein-bound homocysteine. To determine the equilibrium binding capacity of plasma proteins for homocysteine, plasma was treated with 0.5-10 mM dl-homocysteine for 4 h at 37 degrees C under aerobic conditions. Under these conditions the equilibrium binding capacity was 4.88 +/- 0.51 and 4.74 +/- 0.68 micromol/g protein for male (n = 10) and female (n = 10) donors, respectively. The mechanism of protein-bound homocysteine formation involves both thiol-disulfide exchange and thiol oxidation reactions. We conclude that plasma proteins have a high capacity for binding homocysteine in vitro.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Blood Proteins / metabolism*
  • Female
  • Homocysteine / blood*
  • Homocysteine / metabolism
  • Humans
  • In Vitro Techniques
  • Male
  • Oxygen Consumption
  • Protein Binding
  • Time Factors

Substances

  • Blood Proteins
  • Homocysteine