Heme oxygenase 1, human

Obermuller-Jevic, UC. Schlegel, B. Flaccus, A., and Biesalski, HK. 2001. The effect of beta-carotene on the expression of interleukin-6 and heme oxygenase-1 in UV-irradiated human skin fibroblasts in vitro. FEBS Lett 509 186-190. 

Saikawa Y, Kaneda H, Yue L et al. Structural evidence of genomic exon-deletion mediated by Alu-Alu recombination in a human case with heme oxygenase-1 deficiency. Hum Mutat 2000 16[2] 178—179. 

Heme oxygenase catalyzes the first and rate limiting step in the degradation of heme to give biliverdin (Fig. 15). Humans and other mammals have two HO isoforms termed HO-1 and HO-2. Human HO-1 consists of 288 residues (757), whereas rat HO-2 has 316 residues (752). HO contains a C-terminal membrane anchoring sequence (753) that is... 

Mutation of His 132 to an alanine, glycine, or serine in the truncated human heme oxygenase, in accord with identification of His25 as the proximal ligand, does not alter the cpe-His band in the resonance Raman spectrum of the Fe deoxy protein (82). The mutations result in the formation of two separate fractions when the protein is expressed in... 

Truncated forms of human and rat heme oxygenase-1 have been successfully crystallized (53, 89), and the structure of the human isoform has been determined (Fig. 6) (53). The full-length human heme oxygenase is a 288-residue protein, but the protein that was crystallized... 

Erdmann K, Grosser N, Schipporeit K, Schroder H. (2006) The ACE inhibitory dipeptide Met-Tyr diminishes free radical formation in human endothehal cells via induction of heme oxygenase-1 and ferritin. J Nutr 136 2148-2152. 

Although generalizations regarding the hematological effects of fuel oils on humans cannot be made, the effect of kerosene on the first two steps of the heme synthetic pathway has been studied in an animal model. Both hepatic -aminolevulinic acid ( -ALA) dehydratase and -ALA synthetase activities were decreased in female rats after intraperitoneal injection of kerosene, while heme oxygenase was unaffected (Rao and Pandya 1980). Since -ALA synthetase is the rate-limiting enzyme of the heme biosynthesis pathway, hepatic heme biosynthesis may be inhibited by kerosene. It is conceivable that this may be related to the extramedullary hematopoiesis reported in other studies (NTP/NIH 1986) however, there are no direct data to support this. 

A dipeptide Met- , derived from sardine muscle (Matsufuji et ah, 1994), stimulates expression of the antioxidant defense protein HO-1 in a concentration-dependent manner. Previous findings revealed that HO-1 protein expression is accompanied by the induction of a secondary antioxidant protein, ferritin. In a present study, the effect of Met- on the expression of the antioxidant stress proteins, heme oxygenase-1 (HO-1), and ferritin in endothelial cells derived from the human umbilical vein and their contribution to the decrease in radical formation that occurs under the influence of this dipeptide were studied and reported potential activity (Erdmann et ah, 2006). 

There are two human heme oxygenases. The first (HO-1) is synthesized principally in the liver and spleen. Its formation is strongly induced by heme. 

Juan SH, Cheng TH, Lin HC, Chu YL, Lee WS. 2005. Mechanism of concentration-dependent induction of heme oxygenase-1 by resveratrol in human aortic smooth muscle cells. Biochem Pharmacol 69 41 48. 

Hara E., Takahashi K., Tominaga T., Kumabe T., Kayama T., Suzuki H., Fujita H., Yoshi-moto T., Shirato K., and Shibahara S. (1996). Expression of heme oxygenase and inducible nitric oxide synthase mRNA in human brain tumors. Biochem. Biophys. Res. Commun. 224 153-158. 

Ryter, Stefan W. Kvam, Egil Richman, Larry et al. A chromatographic assay for heme oxygenase activity in cultured human cells application to artificial heme oxygenase overexpression. Free Radical Biol. Med. 24(6), 959-971,1998. 

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