• YAKHAK HOEJI
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• v.45 no.1
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• pp.78-84
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• 2001

Heme oxygenase is a rate-limiting enzyme in heme catabolism that cleaves heme to form biliverdin, iron, and carbon monoxide. Heme oxygenase-1 is expressed in many types of cells and tissues and is highly induced in response to oxidative stress. Carbon monoxide, one of the products of heme oxygenase, can stimulate soluble guanylate cyclase and dilate the vascular smooth muscle. So, the induction of heme oxygenase by lipopolysaccharide (LPS)-induced oxydative stress and the effect of the resultant carbon monoxide on aortic contractility were examined in this study. Zinc protoporphyrine IX (ZnPP), a inhibitor of heme oxygenase, elicited weak contraction of thoracic aortic ring, and this effect was more potent in aorta of LPS-treated rats than control and was blocked by methylene blue. The hyperreactivity to ZnPP in LPS-treated group was blocked by co-treatment with aminoguanidine. In the aortic ring of LPS-treated rats, ZnPP didn't change the vasoreactivity to phenylephrine or acetylcholine. ZnPP elicited hyper-tensive effect in concious rats, and pretreatment with LPS did not affect this effect. Prazosin significantly diminished the hypertensive effect of ZnPP. These results indicate that LPS induced heme oxygenase in aotra, and the resultant carbon monoxide diminished the aortic reactivity to vasoconstrictor.

• Journal of Food Hygiene and Safety
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• v.9 no.4
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• pp.205-211
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• 1994

From 120 soil and activated sludge, the strains able to grow on benzoate and m-Toluate have been isolated after selective enrichment which were later identified as Psudomonas sp. according to its morphological and biochemical characteristics. Ben-2 strain contained two plasmid DNA having about 120 Kb and below 2.0 Kb by agarose gel electrophoresis. Form the comparative investigation of catechol 1,2-oxygenase and catechol 2,3-oxygenase activities in Ben-2 strain and its cured strain, Ben-2 strain has both of these two enzymes while cured strain has catechol 1,2-oxygenase only.

• Microbiology and Biotechnology Letters
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• v.37 no.3
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• pp.197-203
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• 2009

An indole oxygenase originated from Rhodococcus sp. RHA1 was cloned into the expression vector, pTrc99A, in Escherichia coli, and designated pTCAN1. The pTCAN2 was constructed from pTCAN1 by the deletion of $lacI^q$ for the constitutive expression of indole oxygenase without adding IPTG in the medium. The complete open reading frame of indole oxygenase was 1,224 bp long, which encodes a protein of 407amino acids. Crude extracts of E. coli $DH5{\alpha}$/pTCAN1 and pTCAN2, respectively, were prepared and subjected to SDS-PAGE analysis. A band corresponding to molecular mass of about 43 kDa was appeared and this result correlated with the predicted molecular mass of cloned indole oxygenase. The E. coli harboring pTCAN1 and pTCAN2, respectively, showed blue color colony in LB plate. The pigment showing blue color was prepared from E. coli $DH5{\alpha}$/pTCAN2, and identified as indigo by experiments using spectrophotometer, HPLC, and TLC. The indigo-forming activity of indole oxygenases from the whole cell of E. coli $DH5{\alpha}/pTCAN1$ cultured at LB medium added 1mM of IPTG and that of E. coli/pTCAN2 showed about 1.75nmol/min/mg DCW (dry cell weight) and 3.85 nmol/min/mg DCW, respectively. Also, the E. coli $DH5{\alpha}$/pTCAN2 produced about $236{\mu}M$ of indigo after 48 hours incubation in TB medium supplemented with 2.5 mM of tryptophan.

• Journal of Microbiology and Biotechnology
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• v.17 no.3
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• pp.379-392
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• 2007

• Journal of Physiology & Pathology in Korean Medicine
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• v.20 no.5
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• pp.1295-1302
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• 2006

Our preliminary aim is to elucidate the pharmacokinetic features of the PNS(Panax notoginseng Buck F.H. Chen. (Arialiaceae) root). First, we assessed the prevention of neurtrophil functions. A Panax notoginseng inhibited neutrophil functions, including degranulation, superoxide generation, and leukotriene B4 production, without any effect on 5-lipoxygenase activity. This Panax notoginseng reduced nitric oxide (NO) and prostaglandin E2 production in mouse peritoneal macrophages stimulated with lipopolysaccharide, whereas no influence on the activity of inducible NO synthase, cyclo-oxygenase-2 or cyclo-oxygenase-1 was observed. Panax notoginseng significantly reduced mouse paw oedema induced by carrageenan. The results indicate that Panax notoginseng exerts anti-inflammatory effects related to the inhibition of neutrophil functions and of NO and prostaglandin E2 production, which could be due to a decreased expression of inducible NO synthase and cyclo-oxygenase-2.

• Journal of Microbiology
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• v.42 no.2
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• pp.160-162
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• 2004

Rhodococcus sp. strain T104 is able to utilize both limonene and biphenyl as growth substrates. Fur-thermore, T104 possesses separate pathways for the degradation of limonene and biphenyl. Previously, we found that a gene(s) involved in limonene degradation was also related to indigo-producing ability. To further corroborate this observation, we have cloned and sequenced a 8,842-bp genomic DNA region with four open reading frames, including one for indole oxygenase, which converts indole to indigo (a blue pigment). The reverse transcription PCR data demonstrated that the identified indole oxygenase gene is specifically induced by limonene, thereby implicating this gene in the degradation of limonene by T104.

• Proceedings of the Korea Environmental Mutagen Society Conference
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• 2004.11a
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• pp.158-158
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• 2004

• Journal of Environmental Health Sciences
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• v.34 no.1
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• pp.49-54
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• 2008

The induction of heme oxygenase-1(HO-1) by UV radiation provides a protective defence against oxidative stress, and has been well demonstrated in skin irradiated with UVA, but not UVB. In this study, we show that the induction of cutaneous HO-l can be attributed to UVB radiation. The expression of HO-1 mRNA was assessed in vivo by reverse transcription-polymerase chain reaction (RT-PCR) analysis, and HO-1 enzyme activity was measured in microsomal preparation from irradiated mice. The mRNA level of HO-1 increases in liver and skin from 1d to 3d after UVB $(3KJ/m^2)$ exposure. The results of gene expression were same pattern of HO-1 enzyme activity in skin, but not in liver. HO-1 mRNA in liver resulted in a progressive increase to 4d after UVB exposure, but HO-1 activity in liver increased to 2d. This finding indicates that UVB radiation is an important inducer of HO-1 and increases in HO activity may protect tissue directly or indirectly from oxidative stress.

• Parasites, Hosts and Diseases
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• v.48 no.1
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• pp.15-21
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• 2010

Astrocytes are the most abundant cells in the central nervous system that play roles in maintaining the blood-brain-barrier and in neural injury, including cerebral malaria, a severe complication of Plasmodium falciparum infection. Prostaglandin (PG) $D_2$ is abundantly produced in the brain and regulates the sleep response. Moreover, $PGD_2$ is a potential factor derived from P. falciparum within erythrocytes. Heme oxygenase-1 (HO-1) is catalyzing enzyme in heme breakdown process to release iron, carbon monoxide, and biliverdin/bilirubin, and may influence iron supply to the P. falciparum parasites. Here, we showed that treatment of a human astrocyte cell line, CCF-STTG1, with $PGD_2$ significantly increased the expression levels of HO-1 mRNA by RT-PCR. Western blot analysis showed that $PGD_2$ treatment increased the level of HO-1 protein, in a dose- and time-dependent manner. Thus, $PGD_2$ may be involved in the pathogenesis of cerebral malaria by inducing HO-1 expression in malaria patients.

• BMB Reports
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• v.45 no.4
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• pp.239-241
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• 2012

Iron availability is limited in the environment and most bacteria have developed a system to acquire iron from host hemoproteins. Heme oxygenase plays an important role by degrading heme group and releasing the essential nutrient iron. The structure of Bacillus subtilis HmoB was determined to 2.0 ${\AA}$ resolution. B. subtilis HmoB contains a typical antibiotic biosynthesis monooxygenase (ABM) domain that spans from 71 to 146 residues and belongs to the IsdG family heme oxygenases. Comparison of HmoB and IsdG family proteins showed that the C-terminal region of HmoB has similar sequence and structure to IsdG family proteins and contains conserved critical residues for heme degradation. However, HmoB is distinct from other IsdG family proteins in that HmoB is about 60 amino acids longer in the N-terminus and does not form a dimer whereas previously studied IsdG family heme oxygenases form functional homodimers. Interestingly, the structure of monomeric HmoB resembles the dimeric structure of IsdG family proteins. Hence, B. subtilis HmoB is a heme oxygenase with a novel structural feature.