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Proteomic analysis of hepatic iron overload
Author(s) -
Petrak Jiri,
Myslivcova Denisa,
Man Petr,
Vyoral Daniel
Publication year - 2006
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.20.5.lb118
Subject(s) - hemochromatosis , hereditary hemochromatosis , proteomics , urea cycle , proteome , ferritin , cirrhosis , biochemistry , chemistry , biology , endocrinology , medicine , amino acid , arginine , gene
Iron‐mediated liver damage is common in patients with iron overload diseases, namely hereditary hemochromatosis. Massive iron deposition causes liver dysfunction, fibrosis and cirrhosis. Our understanding of the complex molecular mechanisms of liver response to iron overload is limited and requires employment of new techniques. Therefore, we used a proteomic approach, combining two‐dimensional electrophoresis and mass spectrometry to assess changes in liver protein expression in mice nutritionally overloaded with iron. Mice (C57/BL6) were fed a high iron diet for 8 weeks whereas control animals were maintained on a defined control diet. Liver homogenates were analyzed by 2D‐PAGE and compared between iron overloaded and control animals. From approximately 1000 observed spots we found 32 proteins to be differentially expressed in response to iron overload. Employing MALDI‐TOF mass spectrometry we identified 30 of the differentially expressed proteins. Thirteen proteins were up‐regulated by iron overload, 17 were down‐regulated. Among the differentially expressed proteins we found (in addition to the iron‐storage protein ferritin) enzymes of lipid, steroid and glucose metabolism, molecules involved in urea cycle as well as proteins engaged in stress response and protein folding. This work was supported by a grant 303/04/0003 from the Czech Science Foundation (GACR).