|Heme oxygenase-1 expression levels are cell cycle dependent.|
|PMID: 12927819 Owner: NLM Status: MEDLINE|
|Heme oxygenase-1 (HO-1) is a stress protein, which has been suggested to participate in defense mechanisms against agents that may induce oxidative injury, such as angiotensin II (Ang II). The purpose of the present study was to examine the role of human HO-1 in cell-cycle progression. We investigated the effect of Ang II on HO-1 gene expression in serum-deprived media to drive human endothelial cells into G(0)/G(1) (1% FBS) compared to exponentially grown cells (10% FBS). The addition of Ang II (100 ng/ml) to endothelial cells increased HO-1 protein and activity in G(0)/G(1) in a time-dependent manner, reaching a maximum HO-1 level at 16 h. Real-time RT-PCR demonstrated that Ang II increased the levels of HO-1 mRNA in G(0)/G(1) as early as 1 h. The rate of HO-1 induction in response to Ang II was several-fold higher in serum-starved cells compared to cells cultured in continuous 10% FBS. The addition of Ang II increased the generation of 8-epi-isoprostane PGF(2 alpha). Inhibition of HO-1, by Stannis mesoporphyrin (SnMP), potentiated Ang II-mediated DNA damage and generation of 8-epi-isoprostane PGF(2 alpha). These results imply that expression of HO-1 in G(0)/G(1), in the presence of Ang II, may be a key player in attenuating DNA damage during cell-cycle progression. Thus, exposure of endothelial cells to Ang II causes a complex response involving generation of superoxide anion, which may be involved in DNA damage. Upregulation of HO-1 ensures the generation of bilirubin and carbon monoxide (CO) in G(0)/G(1) phase to counteract Ang II-mediated oxidative DNA damage. Inducibility of HO-1 in G(0)/G(1) phase is essential and probably regulated by a complex system involving oxygen species to assure controlled cell growth.|
|C Colombrita; G Lombardo; G Scapagnini; N G Abraham|
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|Type: Journal Article; Research Support, U.S. Gov't, P.H.S.|
|Title: Biochemical and biophysical research communications Volume: 308 ISSN: 0006-291X ISO Abbreviation: Biochem. Biophys. Res. Commun. Publication Date: 2003 Sep|
|Created Date: 2003-08-20 Completed Date: 2003-10-14 Revised Date: 2007-11-14|
Medline Journal Info:
|Nlm Unique ID: 0372516 Medline TA: Biochem Biophys Res Commun Country: United States|
|Languages: eng Pagination: 1001-8 Citation Subset: IM|
|Department of Pharmacology, New York Medical College, Valhalla, NY 10595, USA.|
|APA/MLA Format Download EndNote Download BibTex|
Bilirubin / metabolism
Carbon Monoxide / metabolism
Culture Media, Serum-Free / pharmacology
Dinoprost* / analogs & derivatives*
Endothelium, Vascular / metabolism
F2-Isoprostanes / biosynthesis
Heme Oxygenase (Decyclizing) / biosynthesis*
Mesoporphyrins / pharmacology
Oxygen / metabolism
Reverse Transcriptase Polymerase Chain Reaction
Superoxides / metabolism
|HL31069/HL/NHLBI NIH HHS; HL34300/HL/NHLBI NIH HHS; HL55601/HL/NHLBI NIH HHS|
|0/Anions; 0/Culture Media, Serum-Free; 0/F2-Isoprostanes; 0/Membrane Proteins; 0/Mesoporphyrins; 11062-77-4/Superoxides; 27415-26-5/8-epi-prostaglandin F2alpha; 551-11-1/Dinoprost; 630-08-0/Carbon Monoxide; 635-65-4/Bilirubin; 7782-44-7/Oxygen; EC 188.8.131.52/HMOX1 protein, human; EC 184.108.40.206/Heme Oxygenase (Decyclizing); EC 220.127.116.11/Heme Oxygenase-1|
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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