• 제목/요약/키워드: Ornithine decarboxylase

검색결과 75건 처리시간 0.03초

Induction of Ornithine Decarboxylase and Tumor Promotion by N-Methyl-N′-Nitro-N-Nitrosoguanidine, Sodium Chloride, and Dimethyl Itaconate

  • Aeree moon, Aeree-Moon;Kim, Dae-Joong;Han, Beom-Seok;Hwang, Moon-Ok;Kim, Chang-Ok;Choi, Kwang-Sik
    • Biomolecules & Therapeutics
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    • 제1권2호
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    • pp.137-142
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    • 1993
  • The possible tumor-promoting activities of sodium chloride (NaCl) and dimethyl itaconate (DMI), one of the quinone reductase inducers, were examined on stomach of male Wistar rats treated with N-methyl-N'-nitro-N-nitrosoguanidine (MNNG). Administrations of NaCl and DMI after the initiation by MNNG resulted in various sized masses in the rat forestomach. Histopathologic studies showed that the combination of NaCl and DMI made an enhancing effect on the MNNG-induced carcinogenesis, resulting in papilloma in 5 weeks and squamous cell carcinoma in 20 weeks in submucosal area of forestomach. We also used an in vivo shortterm method for evaluating possible tumor-promoting activity with ornithine decarboxylase (ODC) as a marker. The markable inductions of the ODC activities by MNNG, NaCl, and DMI were found in the pyloric mucosa of rat stomach in time-dependent manners. A single administration of MNNG induced ODC activity up to 288 pmol $CO_2$/hr/mg protein at 24 hr after the administration. NaCl caused induction of ODC with a maximum of 179 pmol $CO_2$/hr/mg protein at 8 hr after the administration. ODC was induced up to 539 pmol $CO_2$/hr/mg protein at 16 hr after the administration of DMI. Additional treatment of NaCl and NaCl plus DMl caused 2 fold and 7 fold increases, respectively, in the ODC activity of the MNNG-alone group at 24 hr after the administration. These results suggest that NaCl and DMI have promoting activities in the rat gastric carcinogenesis initiated by MNNG.

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Insect Ornithine Decarboxylase (ODC) Complements SPE1 Knock-Out of Yeast Saccharomyces cerevisiae

  • Choi, Soon-Yong;Park, Hee Yun;Paek, Aron;Kim, Gil Seob;Jeong, Seong Eun
    • Molecules and Cells
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    • 제28권6호
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    • pp.575-581
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    • 2009
  • Ornithine decarboxylase (ODC) is a rate-limiting enzyme in the biosynthesis of polyamines, which are essential for cell growth, differentiation, and proliferation. This report presents the characterization of an ODC-encoding cDNA (SlitODC) isolated from a moth species, the tobacco cutworm, Spodoptera litura (Lepidoptera); its expression in a polyamine-deficient strain of yeast, S. cerevisiae; and the recovery in polyamine levels and proliferation rate with the introduction of the insect enzyme. SlitODC encodes 448 amino acid residues, 4 amino acids longer than B. mori ODC that has 71% identity, and has a longer C-terminus, consistent with B. mori ODC, than the reported dipteran enzymes. The null mutant yeast strain in the ODC gene, SPE1, showed remarkably depleted polyamine levels; in putrescine, spermidine, and spermine, the levels were > 7, > 1, and > 4%, respectively, of the levels in the wild-type strain. This consequently caused a significant arrest in cell proliferation of > 4% of the wild-type strain in polyamine-free media. The transformed strain, with the substituted SlitODC for the deleted endogenous ODC, grew and proliferated rapidly at even a higher rate than the wild-type strain. Furthermore, its polyamine content was significantly higher than even that in the wild-type strain as well as the spe1-null mutant, particularly with a very continuously enhanced putrescine level, reflecting no inhibition mechanism operating in the putrescine synthesis step by any corresponding insect ODC antizymes to SlitODC in this yeast system.

Phase I, phase II 효소 및 ornithine decarboxylase에 미치는 해양심층수의 영향 (Effect of Deep Sea Water on Phase I, Phase II and Ornithine Decarboxylase.)

  • 손윤희;김미경;장정선;정은정;남경수
    • 생명과학회지
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    • 제18권3호
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    • pp.381-386
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    • 2008
  • 동해에서 취수한 해양심층수의 암예방 효능을 얄아보고자 암발생 억제물질의 생화학적 표식자(biochemical markers)인 CYP 1A2 활성, phase II 효소인 QR과 GST의 활성, GSH 함량 및 ODC 활성에 미치는 영향을 살펴보았다. 해양심층수는 암의 개시단계(initiation)를 유발시키는 것으로 알려진 CYP 1A2 활성을 경도의존적으로 저해시켰다. 해양심층수를 Hepa 1clc7 세포에 경도별$(100{\sim}1,000)$로 처리하였을 때 phase II 생체 해독효소인 QR과 GST의 활성은 최대 20%의 증가를 나타내었고, 외부의 독성물질이나 대사산물로부터 세포를 보호하는 역할을 하는 GSH의 함량은 $26{\sim}40%$의 증가를 나타내었다. 그리고 발암과정의 촉진/진행단계에 관여하는 ODC의 활성은 해양심층수의 경도 800과 1,000에서 20%와 35%의 저해율을 나타내었으며, 경도 1,000을 처리한 군에서는 양성대조군인 DFMO와 같은 저해율을 나타내었다. 그러므로 본 연구 결과에 의하면 동해 해양심층수는 발암과정과 관련된 개시 및 촉진/진행단계를 저해시켜 암예방 효능을 나타낼 것으로 사료된다.

Chemopreventive Effect of Protein Extract of Asterina pectinifera in HT-29 Human Colon Adenocarcinoma Cells

  • Shon Yun-Hee;Nam Kyung-Soo
    • Archives of Pharmacal Research
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    • 제29권3호
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    • pp.209-212
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    • 2006
  • We investigated the effect of protein extract of Asterina pectinifera on the activity of 4 enzymes that may playa role in adenocarcinoma of the colon: quinone reductase (QR), glutathione Stransferase (GST), ornithine decarboxylase (ODC), and cyclooxygenase (COX)-2. QR and GST activity increased in HT-29 human colon adenocarcinoma cells increased that had been exposed to 4 concentrations of the protein extract (80, 160, 200, and $240{\mu}g/mL$). Additionally, 12-O-tetradecanoylphorbol-13-acetate (TPA)-induced ODC activity decreased significantly in cells exposed to the extract in concentrations of $160{\mu}g/mL$ (p<0.05), $200{\mu}g/mL$ (p<0.005), and $240{\mu}g/mL$ (p<0.005). TPA-induced COX-2 activity also decreased in cells exposed to extract concentrations of 10, 20, 40, and $60{\mu}g/mL$. COX-2 expression was also inhibited in cells exposed to this extract. These results suggest that this protein extract of A pectinifera has chemopreventive activity in HT-29 human colon adenocarcinoma cells, and therefore, may have the potential to function as a chemopreventive agent in human colorectal cancer.

단삼 에탄올추출물이 유방암 예방 및 전이에 미치는 영향 (Effect of Ethanol Extract from Salvia miltiorrhiza on Chemoprevention and Metastasis of Breast Cancer)

  • 손윤희;조현정;김미경;정은정;남경수
    • 생약학회지
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    • 제38권1호
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    • pp.62-66
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    • 2007
  • Ethanol extract from Salvia miltiorrhiza (SME) was tested for breast cancer chemoprevention and metastasis by measuring the activites of cytochrome P45O 1A1, aromatase, ornithine decarboxylase (ODC), and matrix metalloproteinase (MMP)-9. SME significantly inhibited cytochrome P45O 1A1-mediated ethoxyresorufin O-deethylase (EROD) activity in a dose-dependent manner in a concentration range of 100${\sim}$l,200 ${\mu}g/ml$ (p<0.01). Microsomal aromatase (estrogen synthase) activity was suppressed 54.9%${\sim}$77.5% by the SME at concentration of 600${\sim}$l,200 ${\mu}g/ml$. ODC activity induced by 12-O-tet-radecanoylphorbol-13-acetate (TPA) was significantly reduced by the SME 900 and 1,200 ${\mu}g/ml$ (p<0.05) in MCF-7 breast cancer cells. In addition, SME (900 and 1,200 ${\mu}g/ml$) markedly inhibited MMP-9 activity, a key role in cancer metastasis. Therefore, SME is worth further investigation with respect to breast cancer chemoprevention or therapy.