Low- and high-level expressions of heme oxygenase-1 in cultured cells under uninduced conditions

Biochemical and Biophysical Research Communications
Yoshihiro AndohShigeru Taketani

Abstract

Heme oxygenase-1 (HO-1) degrades heme into biliverdin, iron, and CO. The enzyme participates in adaptive and protective responses to oxidative stress and various inflammatory stimuli. We examined the regulation of HO-1 expression in culture cells under uninduced conditions. Observations by in situ hybridization and immunostaining showed that in cultured mouse fibroblast Balb/3T3 cells not subjected to treatment, 10-15% of cells highly expressed HO-1. The similar pattern of the expression of HO-1 was observed with mouse embryo liver BNL-CL2 cells and Chinese hamster ovary cells. The marked expression of HO-1 was related to the activation of stress-activated protein kinase and to the expression of cyclooxygenase (Cox)-2. When the cells were treated with arachidonic acid, a precursor of prostaglandin, induction of HO-1 in the HO-1-expressing cells but not in the low-expressing cells occurred. This increase was abrogated by the treatment with the Cox inhibitors, indomethacin, and dexamethasone. Neither prostaglandin H2, E2 nor F2a induced HO-1 expression. These results suggest that some cells respond to the cellular stress and intermediates of prostaglandin biosynthesis may act as endogenous stressors to induce HO-1.

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Citations

Jul 22, 2006·Neuroscience Letters·Bo Mi KuHyun Joon Kim
Aug 9, 2016·Acta neurochirurgica·Ruichong Ma, Colin Watts
Sep 19, 2006·Brazilian Journal of Medical and Biological Research = Revista Brasileira De Pesquisas Médicas E Biológicas·M A GloriaN O S Câmara
Oct 30, 2014·Human & Experimental Toxicology·Zhengli YanTianbao Zhang

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