• Title/Summary/Keyword: Ornithine decarboxylase

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Gene Cloning, Expression, and Functional Characterization of an Ornithine Decarboxylase Protein from Serratia liquefaciens IFI65

  • De Las Rivas Blanca;Carrascosa Alfonso V.;Munoz Rosario
    • Journal of Microbiology and Biotechnology
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    • v.17 no.3
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    • pp.408-413
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    • 2007
  • Putrescine has a negative effect on health and is also used as an indicator of quality on meat products. We investigated the genes involved in putrescine production by Serratia liquefaciens IFI65 isolated from a spoiled Spanish dry-cured ham. We report here the genetic organization of its ornithine decarboxylase encoding region. The 5,506-bp DNA region showed the presence of three complete and two partial open reading frames. Putative functions have been assigned to several gene products by sequence comparison with proteins included in the databases. The second gene putatively coded for an ornithine decarboxylase. The functionality of this decarboxylase has been experimentally demonstrated by complementation to an E. coli defective mutant. Based on sequence comparisons of some enterobacterial ornithine decarboxylase regions, we have elaborated a hypothetical pathway for the acquisition of putrescine biosynthetic genes in some Enterobacteriaceae strains.

Activity Change of Ornithine Decarboxylase(ODC) after Hepatectomy

  • Chang Sung;Jou, Kab-Yeo;Ha, Duk-Mo
    • Journal of the Korean Society of Food Science and Nutrition
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    • v.24 no.3
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    • pp.415-419
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    • 1995
  • Ornithine decarboxylase(ODC) catalyzes the first and key step in the polyamine biosynthetic pathway. Ornithine decarboxylase is known to the enzyme that increase substantially its activity in regenerating liver. We found that activity and mRNA level for ODC increase significantly after partial hepatectomy in the rat. After laparotomy, there was significant decrease in activity ; however, mRNA content was unaltered in contrast to previous reports of no change in ornithine decarboxylase and thymidine kinase after sham hepatectomy. This may be mediated by the decrease in food intake after hepatectomy. Therefore it is necessary to examine the effect of food intake after hepatectomy on the ODC activity and mRNA level in the future.

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Cell Biological Studies on the Mechanism of Development and Differentiation Ⅷ 1. Participation of Ornithine Decarboxylase in the Putrescine Biosynthesis in Corn Embryo. (생체발생 및 분화기구의 세포생물학적 연구Ⅷ 1. 옥수수 배에서 Putrescine 합성에 관여하는 Ornithine Decarboxylase)

  • Young Dong Cho
    • Journal of Plant Biology
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    • v.27 no.1
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    • pp.1-6
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    • 1984
  • Kinetin(4.7$\times$10\ulcornerM) and 6-benzylaminopurine (2.2$\times$10\ulcornerM) were found to increase ca. 1.5-fold putrescice content in corn grown in medium containing kinetin and 6-benzylaminopurine(6-BAP) for 3days whereas kinetin was found to decrase ca. 30% spermidine and spermine, respectively. KCI (3$\times$10\ulcornerM) was found to decrease more than 50% putrescine content. After germination, ornithine decarboxylase activity was observed to increase constantly whereas arginine decarboxylase activity remained constant, suggesting involvement in putrescine biosynthesis. 6-benzylaminopurine was shown to increase more activities of arginine ornithine decarboxylase than kinetin when they were added to medium.

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Effect of Cnidii Rhizoma on Proliferation of Breast Cancer Cell, Nitric Oxide Production and Ornithine Decarboxylase Activity (천궁이 유방암세포 증식, Nitric Oxide 생성 및 Ornithine Decarboxylase 활성에 미치는 영향)

  • Nam, Kyung-Soo;Son, Ok-Lye;Lee, Kyung-Hwa;Cho, Hyun-Jung;Shon, Yun-Hee
    • Korean Journal of Pharmacognosy
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    • v.35 no.4 s.139
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    • pp.283-287
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    • 2004
  • The effect of water extract from Cnidii Rhizoma (CRW) on proliferation of human breast cancer cells, nitric oxide production, nitric oxide synthase expression, and ornithine decarboxylase activity was tested. CRW inhibited the growth of both estrogen-dependent MCF-7 and estrogen-independent MDA-MB-23I human breast cancer cells. Lipopolysaccharide-induced nitric oxide (NO) production was significantly reduced by CRW at the concentration of 0.5, 1.0 and 5.0 mg/ml. Expression of inducible nitric oxide synthase (iNOS) was also suppressed with the treatment of CRW in Raw 264.7 cells. CRW inhibited induction of ornithine decarboxylase by 12-0-tetradecanoylphorbol-13-acetate, a key enzyme of polyamine biosynthesis, which is enhanced in tumour promotion. Therefore, CRW is worth further investigation with respect to breast cancer chemoprevention or therapy.

An Experimental Study on the Effect of Electric Field the Ornithine Decarboxylase Activity Change of Myeloid Cells According to Ionizing Radiation Exposure (이온화방사선 피폭에 의한 골수세포의 Ornithine Decarboxylase 활성도의 변화에 대한 전계장의 영향에 관한 실험적 연구)

  • 정문호
    • Journal of Environmental Health Sciences
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    • v.21 no.1
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    • pp.78-85
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    • 1995
  • Ornithine decarboxylase(ODC) is an indicate enzyme in carcinogenesis. We divided Sprague Dawley rats into six groups: control, electric field exposure, X-ray only irradiation, X-ray irradiation with electric field exposure group, Sr-90 injected group and Sr-90 and electric field complex exposure group. The ODC activity was measured in rat's bone marrow cell every week. The results were summarized as follows: The ODC activitied was increased in X-ray irradiated, Sr-90 injected and Sr-90 and electric field complex exposed group as compared with that of control(p<0.05). The ODC activity was increased comparing that of control neither in X-ray and electric field complex exposed group nor electric field only exposed group. This result suggests that the electric field doesn't have myeloid carcinogenicity and myeloid cancer incidence caused by ionized radiation is suppressed by electric field exposure.

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Mutation of Cysteine-115 to Alanine in Nicotiana glutinosa Ornithine Decarboxylase Reduces Enzyme Activity

  • Lee, Yong-Sun;Cho, Young-Dong
    • BMB Reports
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    • v.34 no.5
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    • pp.472-477
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    • 2001
  • Ornithine decarboxylase (ODC, EC 4.1.1.17) is the first and key enzyme in eukaryotic polyamine biosynthesis. The cDNA encoding ornithine decarboxylase from Nicotiana glutinosa was cloned ($GeBank^{TM}$ AF 323910) and expressed in E. coli. Site directed mutagenesis were performed on several highly conserved cysteine residues. Among the mutants, C115A showed significant changes in the kinetic properties. The $K_m$ value of the C115A mutant was $1790\;{\mu}M$, which was 3-fold higher than that of the wild-type ODC. There was a dramatic decrease in the $k_{cat}$, values of the C115A mutant, compared to that of the wild-type ODC, which had a $k_{cat}$ value of $77.75\;s^{-1}$. C115A caused a shift in the optimal pH from 8.0 to 8.4. Considering these results, we suggest that cys-115 is involved in the catalytic activity of N. glutinosa ODC.

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The Stimulation of Arginine Decarboxylase Activity by alpha-Difluoromethyl$ Ornithine in Tobacco Suspension Cultured Cells

  • Lee, Sun-Hi;Kim, Yong-Bum;Lee, Myeong-Min;Park, Ki-Young
    • Journal of Plant Biology
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    • v.39 no.2
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    • pp.107-112
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    • 1996
  • To study the compensatory aspect of putrescine biosynthetic enzyme n tobacco suspension cultured cells, we examined the contents of the cellular polyamines and the activities of arginine decarboxylase (ADC, EC 4.1.1.19) and ornithine decarboxylase (ODC, EC 4.1.1.17) in the tobacco suspension cells treated with $\alpha$-difluoromethyl arginine (DFMA) or $\alpha$-difluoromethyl ornithine (DFMO). In the untreated cells, the content of the cellular putrescine was decreased during the first 3 hours and then subsequently increased. However, the content of the cellular spermidine and spermine remained constant during the incubation time. While ADC activity increased after 6 hours, ODC activity decreased following the rapid increase until 6 hours. DFMA induced the decrease in the contents of putrescine and spermidine, and the increase in that of spermine. It also caused the inhibition of ADC and ODC activities throughout the incubation time. DFMO produced the stimulation of ADC activity about 2 times of untreated cells and the decrease in the content of putrescine about 50% of them at 12 hour. The application of putrescine or cycloheximide prevented the increase of ADC activity by DFMO but that of actinomycin-D did not show any detectable effect. The stimulation of ADC activity by DFMO in tobacco suspension cultured cells was probably due to the enhancement of de novo synthesis for ADC protein, which might be regulated in the translation step by the content of the cellular putrescine.

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Ornithine Decarboxylase: A Promising and Exploratory Candidate Target for Natural Products in Cancer Chemoprevention

  • Luqman, Suaib
    • Asian Pacific Journal of Cancer Prevention
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    • v.13 no.5
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    • pp.2425-2427
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    • 2012
  • Ornithine decarboxylase (ODC), the first enzyme in the polyamine biosynthesis, plays an important role in tumor progression, cell proliferation and differentiation. In recent years, ODC has been the subject of intense study among researchers, as a target for anti-cancer therapy and specific inhibitory agents, have the potential to suppress carcinogenesis and find applications in clinical therapy. In particular, it is suggested that ODC is a promising candidate target for natural products in cancer chemoprevention. Future exploration of ornithine decarboxyalse inhitors present in nature may offer great hope for finding new cancer chemporeventive agents.

Effect of Cnidii Rhizoma on Phase II Enzyme and Ornithine Decarboxylase Activities (천궁이 Phase II 효소 유도와 Ornithine Decarboxylase 활성에 미치는 영향)

  • Shon, Yun-Hee;Kim, Mee-Kyung;Cho, Hyun-Jung;Nam, Kyung-Soo
    • Journal of Physiology & Pathology in Korean Medicine
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    • v.20 no.6
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    • pp.1572-1575
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    • 2006
  • Water extract from Cnidii Rhizoma (CRW) was tested for colon cancer chemopreventive activity by measuring the induction of phase II detoxification enzyme activity [quinone reductase (QR) and glutathione S-transferase (GST)] and glutathion (GSH) levels and ornithine decarboxylase (ODC) activity in cultured human colorectal adenocarcinoma HT-29 cells. CRW inhibited cell proliferation in cultured HT-29 cells. CRW induced QR activity in a dose-dependent manner in a concentration range of 0.1${\sim}$5.0 $mg/m{\ell}$. GST activity was also induced with the treatment of CRW in HT-29 cells. In addition GSH levels was increased with CRW. CRW inhibited ODC activity, a key enzyme of polyamine biosynthesis, which is enhanced in tumor promotion. These results suggest that CRW has colon cancer chemopreventive activity by increasing phase II enzyme activity and GSH levels and inhibiting ODC activity in vitro.

Effect of Asterina pectinifera on Activities of Cytochrome P450 1A1 and Ornithine Decarboxylase (불가사리 단백추출물이 Cytochrome P450 1A1과 Ornithine Decarboxylase 활성에 미치는 영향)

  • Nam, Kyung-Soo;Kim, Mee-Kyung;Cho, Hyun-Jung;Shon, Yun-Hee
    • Journal of Marine Bioscience and Biotechnology
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    • v.1 no.2
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    • pp.71-75
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    • 2006
  • The effect of protein extract from Asterina pectinifera on proliferation of human breast cancer cells and activities of cytochrome P450 1A1 and ornithine decarboxylase was tested. Protein extract from Asterina pectinifera inhibited the growth of both estrogen-dependent MCF-7 and estrogen-independent MDA-MB-231 human breast cancer cells. Cytochrome P450 1A1 activity was significantly inhibited by the protein extract from Asterina pectinifera at concentrations of 80 (p<0.05), 120 (p<0.01) and $160{\mu}g/m{\ell}$ (p<0.01). The extract inhibited induction of ornithine decarboxylase by 12-O-tetradecanoylphorbol-13-acetate, a key enzyme of polyamine biosynthesis, which is enhanced in breast tumor promotion. Therefore, Asterina pectinifera is worth further investigation with respect to breast cancer chemoprevention or therapy.

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