Gene Regulation of HBP 23 by Metalloporphyrins and Protoporphyrin IX in Liver and Hepatocyte Cultures

Heme-binding protein 23 kDa (HBP23) belongs to the antioxidant family of peroxiredoxins and binds heme with high affinity.In vivotreatment of rats with heme induced expression of HBP23 mRNA levels in liver coordinately with that of the heme degrading enzyme heme oxygenase-1 (HO-1). In primary rat he...

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Published in:Biochemical and biophysical research communications 1997-02, Vol.231 (3), p.667-670
Main Authors: Immenschuh, Stephan, Nell, Christina, Iwahara, Shin-ichiro, Katz, Norbert, Muller-Eberhard, Ursula
Format: Article
Language:English
Subjects:
Animals
Carrier Proteins - genetics
Cells, Cultured
Cycloheximide - pharmacology
Dactinomycin - pharmacology
Gene Expression - drug effects
Heme - pharmacology
Heme Oxygenase (Decyclizing) - genetics
Hemeproteins - genetics
Liver - physiology
Male
Metalloporphyrins - physiology
Protein Synthesis Inhibitors - pharmacology
Protoporphyrins - physiology
Rats
Rats, Wistar
RNA, Messenger - genetics
Transcription, Genetic - drug effects
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Summary:Heme-binding protein 23 kDa (HBP23) belongs to the antioxidant family of peroxiredoxins and binds heme with high affinity.In vivotreatment of rats with heme induced expression of HBP23 mRNA levels in liver coordinately with that of the heme degrading enzyme heme oxygenase-1 (HO-1). In primary rat hepatocyte cultures Sn-, Co-, and Zn-metalloprotoporphyrin as well as the heme precursor protoporphyrin IX increased the HBP23 mRNA expression to a level similar to that elicited by heme. Heme-dependent induction of HBP23 mRNA was prevented by pretreatment with actinomycin D, indicating a transcriptional mechanism of gene induction. The results suggest that the coordinate gene regulation pattern of HBP23 and HO-1 plays a physiological role against oxidative stress.
ISSN:0006-291X
1090-2104
DOI:10.1006/bbrc.1997.6166