Mechanism of induction of heme oxygenase by metalloporphyrins in primary chick embryo liver cells: evidence against a stress-mediated response
Authors
Cable, Edward EarlGildemeister, Otto S.
Pepe, Joyce A.
Lambrecht, Richard W.
Bonkovsky, Herbert L.
UMass Chan Affiliations
Department of Biochemistry and Molecular PharmacologyGraduate School of Biomedical Sciences
Document Type
Journal ArticlePublication Date
1997-04-01Keywords
Animals; Antioxidants; Chick Embryo; Gene Expression Regulation; Heme; Heme Oxygenase (Decyclizing); Lipid Peroxidation; Liver; Metalloporphyrins; RNA, MessengerLife Sciences
Medicine and Health Sciences
Metadata
Show full item recordAbstract
Heme oxygenase catalyzes the first and rate-controlling step in heme catabolism. One of the two forms of heme oxygenase (heme oxygenase-1) has been shown to be increased by heme, metals, and in some systems, by certain environmental stresses. However, it remains uncertain whether heme induces hepatic heme oxygenase-1 by a general stress response, or a specific heme-dependent cellular response. The work communicated here explores this issue by examining possible mechanisms whereby heme and other metalloporphyrins induce heme oxygenase-1 in normal liver cells. Primary cultures of chick embryo liver cells were tested for their ability to increase heme oxygenase mRNA after exposure to selected metalloporphyrins (heme, chromium mesoporphyrin, cobalt protoporphyrin and manganese protoporphyrin). The ability of antioxidants to decrease metalloporphyrin-mediated induction of heme oxygenase-1 mRNA was also tested. Our results indicate that: 1) the increase in heme oxygenase-1 mRNA mediated by heme or other metalloporphyrins may involve a short-lived protein(s) since the increase was prevented by several inhibitors of protein synthesis; and 2) in normal liver cells, heme-dependent oxidative stress does not play a key role in the heme-mediated induction of heme oxygenase-1. We conclude that heme and other non-heme metalloporphyrins induce heme oxygenase-1 through a mechanism requiring protein synthesis, not because metalloporphyrins increase cellular oxidative or other stress.Source
Mol Cell Biochem. 1997 Apr;169(1-2):13-20.
DOI
10.1023/A:1006817207166Permanent Link to this Item
http://hdl.handle.net/20.500.14038/33052PubMed ID
9089626Related Resources
ae974a485f413a2113503eed53cd6c53
10.1023/A:1006817207166