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Volume 51 (12): 1621-1631, 2003
Copyright ©The Histochemical Society, Inc.
Differential Cellular and Subcellular Localization of Heme-Binding Protein 23/Peroxiredoxin I and Heme Oxygenase-1 in Rat Liver
Institute of Clinical Chemistry and Pathobiochemistry, University of Giessen, Giessen, Germany (SI); Institute for Anatomy and Cell Biology, University of Giessen, Giessen, Germany (EBV); Center of Internal Medicine, Department of Gastroenterology and Endocrinology, University of Göttingen, Germany (MT,GR); Department of Biochemistry, Nippon Medical School, Tokyo, Japan (S-II); and Institute for Anatomy and Cell Biology, University of Heidelberg, Heidelberg, Germany (HDF)
Correspondence to: Dr. Stephan Immenschuh, Institut für Klinische Chemie und Pathobiochemie, Justus-Liebig-Universität Giessen, Gaffkystr. 11, 35392 Giessen, Germany. E-mail: Stephan.Immenschuh{at}klinchemie.med.uni-giessen.de
Heme-binding protein 23 (HBP23), also termed peroxiredoxin (Prx) I, and heme oxygenase-1 (HO-1) are distinct antioxidant stress proteins that are co-ordinately induced by oxidative stress. HBP23/Prx I has thioredoxin-dependent peroxidase activity with high binding affinity for the pro-oxidant heme, while HO-1 is the inducible isoform of the rate-limiting enzyme of heme degradation. We investigated the cellular and subcellular localization of both proteins in rat liver. Whereas by immunohistochemistry (IHC) a uniformly high level of HBP23/Prx I expression was observed in liver parenchymal and different sinusoidal cells, HO-1 expression was restricted to Kupffer cells. By immunoelectron microscopy using the protein A–gold technique, HBP23/Prx I immunoreactivity was detected in cytoplasm, nuclear matrix, mitochondria, and peroxisomes of parenchymal and non-parenchymal liver cell populations. In contrast, the secretory pathway, i.e., the endoplasmic reticulum and Golgi complex, was free of label. As determined by immunocytochemical (ICC) studies in liver cell cultures and by Western and Northern blotting analysis, HBP23/Prx I was highly expressed in cultures of isolated hepatocytes and Kupffer cells. In contrast, HO-1 was constitutively expressed only in Kupffer cell cultures but was also inducible in hepatocytes. These data suggest that HBP23/Prx I and HO-1 may have complementary antioxidant functions in different cell populations in rat liver. (J Histochem Cytochem 51:1621–1631, 2003)
Key Words: heme-binding protein • 23/peroxiredoxin I • heme oxygenase-1 • liver • oxidative stress • hepatocytes • Kupffer cells • immunocytochemistry • protein A–gold
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