Heme oxygenases are microsomal enzymes that cleave heme to produce the antioxidant biliverdin, inorganic iron and carbon monoxide (CO). The activity of Heme Oxygenase 1 (HO-1), also designated HSP 32, is highly inducible in response to numerous stimuli, including heme, heavy metals, hormones and oxidative stress. Heme Oxygenase 2, in contrast, appears to be constituitively expressed in mammalian tissues. Heme Oxygenase 2 is involved in the production of carbon monoxide (CO) in brain, where CO is thought to act as a neurotransmitter. The CO signaling system closely parallels the signaling pathway involving nitric oxide, and regulation of the two systems is closely linked. Heme Oxygenase 3 is found in the spleen, liver, thymus, prostate, heart, kidney, brain and testis. A poor heme catalyst, Heme Oxygenase 3 has two heme regulatory motifs that may be involved in heme binding.
Background References
1. He C et al. Vasoprotective effect of PDGF-CC mediated by HMOX1 rescues retinal degeneration. Proc Natl Acad Sci U S A 111:14806-11 (2014).
2. Maruyama A et al. Non-coding RNA derived from the region adjacent to the human HO-1 E2 enhancer selectively regulates HO-1 gene induction by modulating Pol II binding. Nucleic Acids Res 42:13599-614 (2014).
mIHC analysis of human tonsil tissue (Formalin/PFA-fixed paraffin-embedded sections) with Rabbit anti-Heme Oxygenase 1 (HO-1) antibody (IRS156RB) at 1/100 dilution. The immunostaining was performed with the IRISKitCmTSA Kit (900808). Heat mediated antigen retrieval with Tris-EDTA buffer (pH 9.0) for 30 mins at 95℃. DAPI (blue) was used as a nuclear counter stain. Image acquisition was performed with Olympus VS200 Slide Scanner.
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