Malondialdehyde and 4-hydroxynonenal protein adducts in plasma and liver of rats with iron overload - PubMed (original) (raw)

Malondialdehyde and 4-hydroxynonenal protein adducts in plasma and liver of rats with iron overload

K Houglum et al. J Clin Invest. 1990 Dec.

Abstract

In hepatic iron overload, iron-catalyzed lipid peroxidation has been implicated in the mechanisms of hepatocellular injury. Lipid peroxidation may produce reactive aldehydes such as malondialdehyde (MDA) and 4-hydroxynonenal (4-HNE), which may form aldehyde-protein adducts. We investigated whether lipid peroxidation occurred in rats fed a diet containing 3% carbonyl iron for 5-13 wk, and if this resulted in the formation of MDA- and 4-HNE- protein adducts. Chronic iron feeding resulted in hepatic iron overload (greater than 10-fold) and concomitantly induced a 2-fold increase in hepatic lipid peroxidation. Using an antiserum specific for MDA-lysine protein adducts, we demonstrated by immunohistochemistry the presence of aldehyde-protein adducts in the cytosol of periportal hepatocytes, which co-localized with iron. In addition, MDA- and 4-HNE-lysine adducts were found in plasma proteins of animals with iron overload. Only MDA adducts were detected in albumin, while other plasma proteins including a approximately 120-kD protein had both MDA and 4-HNE adducts. In this animal model of hepatic iron overload, injury occurs primarily in periportal hepatocytes, where MDA-lysine protein adducts and excess iron co-localized.

PubMed Disclaimer

Similar articles

Cited by

References

    1. Lipids. 1984 Feb;19(2):127-33 - PubMed
    1. Biochem J. 1962 May;83:291-8 - PubMed
    1. J Appl Biochem. 1983 Aug-Oct;5(4-5):293-9 - PubMed
    1. Biochem J. 1984 Oct 1;223(1):31-8 - PubMed
    1. Biochem Biophys Res Commun. 1984 Oct 30;124(2):462-9 - PubMed

Publication types

MeSH terms

Substances

LinkOut - more resources