Document Detail


Heme oxygenase-1 expression levels are cell cycle dependent.
MedLine Citation:
PMID:  12927819     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
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.
Authors:
C Colombrita; G Lombardo; G Scapagnini; N G Abraham
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Publication Detail:
Type:  Journal Article; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Biochemical and biophysical research communications     Volume:  308     ISSN:  0006-291X     ISO Abbreviation:  Biochem. Biophys. Res. Commun.     Publication Date:  2003 Sep 
Date Detail:
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    
Other Details:
Languages:  eng     Pagination:  1001-8     Citation Subset:  IM    
Affiliation:
Department of Pharmacology, New York Medical College, Valhalla, NY 10595, USA.
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MeSH Terms
Descriptor/Qualifier:
Anions
Bilirubin / metabolism
Blotting, Western
Carbon Monoxide / metabolism
Cell Cycle*
Cell Division
Cells, Cultured
Culture Media, Serum-Free / pharmacology
DNA Damage
Dinoprost* / analogs & derivatives*
Endothelium, Vascular / metabolism
F2-Isoprostanes / biosynthesis
G0 Phase
G1 Phase
Heme Oxygenase (Decyclizing) / biosynthesis*
Heme Oxygenase-1
Humans
Membrane Proteins
Mesoporphyrins / pharmacology
Microscopy, Confocal
Oxidative Stress
Oxygen / metabolism
Reverse Transcriptase Polymerase Chain Reaction
Superoxides / metabolism
Temperature
Time Factors
Up-Regulation
Grant Support
ID/Acronym/Agency:
HL31069/HL/NHLBI NIH HHS; HL34300/HL/NHLBI NIH HHS; HL55601/HL/NHLBI NIH HHS
Chemical
Reg. No./Substance:
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 1.14.99.3/HMOX1 protein, human; EC 1.14.99.3/Heme Oxygenase (Decyclizing); EC 1.14.99.3/Heme Oxygenase-1

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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