Format

Send to

Choose Destination
Chem Phys Lipids. 2010 May;163(4-5):347-55. doi: 10.1016/j.chemphyslip.2010.02.002. Epub 2010 Feb 16.

Identification and properties of complexes formed by myeloperoxidase with lipoproteins and ceruloplasmin.

Author information

1
Institute of Experimental Medicine of the Russian Academy of Medical Sciences, Saint-Petersburg, Russia. biochem@nm.ru

Abstract

The first evidence of multi-component complexes formed by myeloperoxidase (MPO), ceruloplasmin (CP), and very low/low density lipoproteins (VLDL/LDL) obtained by electrophoresis, gel filtration, and photon-correlation spectroscopy (PCS) is presented in this paper. Complexes were observed when isolated MPO, CP, and VLDL/LDL were mixed and/or when MPO was added to the blood plasma. Complex LDL-MPO-CP was detected in 44 of 100 plasma samples taken from patients with atherosclerosis, and 33 of 44 samples also contained the VLDL-MPO-CP complex. MPO concentration in these patients' plasma exceeded 800 ng/ml. Interaction of MPO with high density lipoproteins (HDL) was not revealed, as well as binding of CP to lipoproteins in the absence of MPO. Adding antibodies against apoB-100 to VLDL-MPO-CP and LDL-MPO-CP complexes results in release of lipoproteins. Using PCS the diameters of complexes under study were evaluated. By comparing concentrations of the components in complexes formed by MPO, CP, and lipoproteins their stoichiometry was assessed as 2VLDL:1MPO:2CP and 1LDL:1MPO:2CP. Lipoproteins affected the inhibition of MPO peroxidase activity by CP. The affinity of lipoproteins to MPO-CP complex was assessed using apparent dissociation constants determined as approximately 0.3 nM for VLDL and approximately 0.14 nM for LDL.

[Indexed for MEDLINE]

Supplemental Content

Full text links

Icon for Elsevier Science
Loading ...
Support Center