• 제목/요약/키워드: Cytochrome $c_3$

검색결과 735건 처리시간 0.027초

Role of Kupffer Cells in Hepatic Drug Metabolizing Functions during Sepsis in Rats

  • Lee, S.H.;Lee, S.M.
    • 한국응용약물학회:학술대회논문집
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    • 한국응용약물학회 2001년도 추계학술대회 및 정기총회
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    • pp.109-109
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    • 2001
  • The present study was done to investigate the relationship between Kupffer cells and alteration of cytochrome P-450 (CYP)-dependent drug metabolizing enzyme activities during polymicrobial sepsis. Male rats were subjected to polymicrobial sepsis by cecal ligation and puncture (CLP) followed by fluid resuscitation. The gadolinium chloride (GdC1$_3$, 10 mg/kg), blocker of Kupffer cells, was pretreated intravenously at 48 h and 24 h prior to the induction of CLP. All assay parameters were determined at 24 h after CLP or sham operation. In CLP-treated rats, the mortality rate of animals increased to 50% and serum alanine (ALT) and aspartate aminotransferase (AST) levels also significantly elevated. However, this increase was not suppressed by GdC1$_3$ pretreatment. Microsomal lipid peroxidation markedly increased after CLP operation. This increase was significantly attenuated by pretreatment. Total cytochrome P-450 content and NADPH-cytochrome P-450 reductase activity were not changed after CLP operation, but GdC1$_3$pretreatment reduced total cytochrome P-450 content, The hepatic microsomal CYP 1A1, 1A2, 2Bl and 2El activities in CLP-induced rats were also not significantly different from sham-operated rats. However, GdC1$_3$pretreatment showed a moderate increase in CYP1A1 and 1A2 activities. Our findings suggest that Kupffer cells may be partly responsible for producing hepatocellular dysfunction during sepsis.

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Paraquat Induces Apoptosis through Cytochrome C Release and ERK Activation

  • Seo, Hong Joo;Choi, Sang Joon;Lee, Jung-Hee
    • Biomolecules & Therapeutics
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    • 제22권6호
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    • pp.503-509
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    • 2014
  • Paraquat has been suggested to induce apoptosis by generation of reactive oxygen species (ROS). However, little is known about the mechanism of paraquat-induced apoptosis. Here, we demonstrate that extracellular signal-regulated protein kinase (ERK) is required for paraquat-induced apoptosis in NIH3T3 cells. Paraquat treatment resulted in activation of ERK, and U0126, inhibitors of the MEK/ERK signaling pathway, prevented apoptosis. Moreover, paraquat-induced apoptosis was associated with cytochrome C release, which could be prevented by treatment with the MEK inhibitors. Taken together, our findings suggest that ERK activation plays an active role in mediating paraquat-induced apoptosis of NIH3T3 cells.

Investigation of the electrode reaction of cytochrome c and pyrroliquinoline quinone at self-assembled monolayers of amino acid

  • Kim Imsook;Kwak Juhyoun
    • 전기화학회지
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    • 제2권1호
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    • pp.27-30
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    • 1999
  • Self-Assembled monolayers of carboxyl-terminated alkanethiols, which is negatively charged in pH 7.0, were usually used to facilitate the electron transfer between the positively charged protein and the electrode. In case of L-cysteine, as it has both positive and negative group, it can be a candidate for a new modifier to facilitate positively charged protein or negatively charged protein. Our investigation of L-cysteine shows that the electron transfer occurs successfully to both cytochrome c (cyt. c) and pyrroloquinoline quinone (PQQ). By using 1-ethyl-3-(3-dime-thlyaminopropyl) carbodiimide (EDC), we made a covalent bond between cyt. c and monolayer. Then PQQ was electrostatically adsorbed to the same monolayer. Cyclic voltammograms show that both molecules do not interfere each other and electron transfer is appreciable.

Properties of Electron Carriers in the Process of Methanol Oxidation in a New Restricted Facultative Marine Methylotrophic Bacterium, Methylophaga sp. MP

  • Koh, Moon-Joo;Kim, Chun-Sung;Kim, Yun-A;Choi, Hack-Sun;Cho, Eun-Hee;Kim, Eung-Bin;Kim, Young-Min;Kim, Si-Wouk
    • Journal of Microbiology and Biotechnology
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    • 제12권3호
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    • pp.476-482
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    • 2002
  • Methanol dehydrogenase (MDH) and c-type cytochromes from marine methanol-oxidizing bacterium, Methylophaga sp. MP, were purified and characterized. The native MDH had a molecular mass of 148 kDa and its isoelectric point was 5.5. Two c-type cytochromes, $c_L\;and\;c_H$, were found, and their isoelectric points were 3.4 and 8.0, respectively. The purified MDH had higher thermal stability than that of the other soil methylotrophic bacteria. The electron flow rate from MDH to cytochrome $c_L$was higher than that from MDH to cytochrome $c_H$, indicating that the physiological primary electron acceptor for MDH is cytochrome $c_L$. The electron transfer from MDH to phenazine ethosulfate (PES, artificial electron acceptor) in the two dye (PES/DCPIP)-linked assay system was not inhibited by NaCl, whereas the electron flow from MDH to cytochrome $c_L$ in the cytochrome/DCPIP-linked assay system was suppressed significantly by NaCl. Metal chelating agents such as EDTA showed the same effects on the MDH activity.

상이한 수소이온농도에서 성장하는 Methylobacterium extorquens AM1의 메탄올 이용 관련효소와 Cytochrome c 및 폴리아민 (Polyamine, Cytochrome c and Enzymes Related to the Utilization of Methanol in Methylobacterium extorquens AMI Growing at Different pHs)

  • 박기정;이순희;김영민
    • 미생물학회지
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    • 제30권6호
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    • pp.533-538
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    • 1992
  • Methylobacterium extorquens AM1 이 pH 5.5 와 7.0 에서 메탄올을 이용하여 성장할 때의 세대 시간은 각각 25 시간과 8.3 시간이었다. pH 7.0 에서 성장한 세균들은 모두 지수성장기 중기에서 가장 높은 methanol dehydrogenase (MDH_) 의 활성을 나타내었고, MDH 함유량은 성장시기에 따른 변화를 보이지 않았다. 세포내 cytochrome c 는 정체기에서 높게 나타났고 pH 7.0 에서 성장한 세균에 더 많이 존재하였다. Putrescine 또는 spermidine 이 첨가된 pH 5.5 의 배지에서 성장한 세균에 더 많이 존재하였다. Putrescine 또는 spermidine 이 첨가된 pH 5.5 의 배지에서 성장한 세균에서는 putrescine 의 함량은 증가하였으나 spermine 의 함량은 감소하였고 spermidine 의 함량에는 변화가 없었다. Spermine 을 첨가한 배지에서 성장한 세균에서는 폴리아민함량에 변화가 없었다. Putrescine 또는 spermidine이 첨가된 배지에서 성장한 세균에서 MDH 와 hydroxypyruvate reductase 의 활성이 증가되었고 MDH 와 cytochrome c 의 함량에는 변화가 없었다. 폴리아민은 invitro 상태에서 MDH 와 hydroxypyruvate reductase 의 활성을 증가시키지 않았다.

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Molecular Cloning and Expression of Fusion Proteins Containing Human Cytochrome P450 3As and Rat NADPH-P450 Reductase in Escherichia coli

  • Chun, Young-Jin;Guengerich, F-Peter
    • Toxicological Research
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    • 제18권3호
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    • pp.249-257
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    • 2002
  • Cytochrome P450 3As such as 3A4 and 3A5 metabolize a wide range of pharmaceutical compounds. The vectors for the expression of fusion protein containing an N-terminal human P450 3A4 or P450 3A5 sequences and a C-terminal rat NADPH-cytochrome P450 reductase moiety were constructed. These plasmids were used to express the fusion protein in Escherichia coli DH5$\alpha$ cells. High levels of expression were achieved (100~200 nmol/liter) and the expressed fusion protein in E. coli membranes were catalytically active for nifedipine oxidation, a typical enzymatic activity of P450 3A4. The NADPH-P450 reductase activities of these fusion protein were also determined by measuring reduction of cytochrome c. To fine a specific Inhibitor of P450 3A4 from naturally occurring chemicals, a series of isothiocyanate compounds were evaluated for the inhibitory activity of P450 using the fusion proteins in E. coli membranes. Of the five isothiocyanates (phenethyl isothiocyanate, phenyl isothiocyanate, benzol isothiocyanate, benzoyl isothiocyanate and cyclohexyl isothiocyanate) tested, benzoyl isothiocyanate showed a strong inhibition of P450 3A4 with an $IC_{50}$value of 2.8 $\mu\textrm{M}$. Our results indicate that the self-sufficient fusion protein will be very useful tool to study the drug metabolism and benzyl isothiocyanate may be valuable for characterizing the enzymatic properties of P450 3A4.

Paramagnetic Inversion of the Sign of the Interference Contribution to the Transverse Relaxation of the Imido Protons of the Coordinated Imidazoles in the Uniformly $^{15}N$ Labeled Cytochrome $c_3$

  • ;정인철;심윤보;강신원;박장수
    • Bulletin of the Korean Chemical Society
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    • 제22권11호
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    • pp.1197-1201
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    • 2001
  • In the spectrum of uniformly 15N labeled cytochrome c3, the relative linewidths of the doublet peaks of the 15N-coupled imido proton of the coordinated imidazole group were reversed on oxidation. This inversion was explained by the interference relaxation process between the electron-proton dipolar and 15N-1H dipolear interactions. The inversion can be used to assign the imido protons of the coordinated imidazole groups in heme proteins.

심경, 신경의 오수혈 침자가 Mitochondrial Respiratory Chain Complexes에 미치는 영향 (The Effects of Acupuncture at Heart and Kidney Meridian on Mitochondrial Respiratory Chain Complexes Activities in Rats)

  • 최동희;이유미;김미래;박정혜;김혜란;나창수;윤대환
    • Korean Journal of Acupuncture
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    • 제37권1호
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    • pp.37-45
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    • 2020
  • Objectives : Mitochondria are typically known as intracellular double membrane-bound structures that supply energy for intracellular metabolism including Krebs cycle and beta-oxidation. Also, acupuncture has been known to stimulate the flow of energy. To explore the effect of acupuncture on the mitochondrial respiratory chain activities in rat's heart and kidneys, the activities of mitochondrial respiratory chain complexes I to IV were observed. Methods : The rats were divided into 11 groups; Normal (no acupuncture treatment and under anesthesia for 10 min), heart meridian five-transport-points (acupuncture treatment at HT9, HT8, HT7, HT4 and HT3 under anesthesia for 10 min), and kidney meridian five-transport-points (acupuncture treatment at KI1, KI2, KI3, KI7 and KI10 under anesthesia for 10 min). All rats were sacrificed and the heart and kidneys were examined for the changes of respiratory chain activities. Results : Acupuncture at HT7 increased the activity of succinate dehydrogenase; acupuncture at KI2 increased the activity of ubiquinol cytochrome C oxidoreductase; and acupuncture at HT9, HT8, HT3 and KI1 increased activities of cytochrome C oxidase. Conclusions : Acupuncture assists mitochondrial repiratory chain activity via the Cytochrome C oxidase signaling pathway in heart and kidney of rats.

Differential Efflux of Mitochondrial Endonuclease G by hNoxa and tBid

  • Seo, Young-Woo;Park, Sun-Young;Yun, Cheol-Won;Kim, Tae-Hyoung
    • BMB Reports
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    • 제39권5호
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    • pp.556-559
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    • 2006
  • The Bcl-2 family of proteins regulates mitochondrial functions during cell death by modulating the efflux of death-promoting proteins such as cytochrome c and endonuclease G. Upon the binding of death ligands to their receptors, caspase-8 cleaves Bid, a BH3-only protein, into tBid that causes the mitochondrial damages resulting in the release of cytochrome c and endonuclease G. Also, another BH3-only protein, hNoxa, has been shown to induce the efflux of cytochrome c from the mitochondria. Whether the efflux proteins from the mitochondria in response to tBid or hNoxa are the same or different, however, has not been addressed. We have demonstrated that endonuclease G activities are not detectable among the proteins released from isolated mitochondria by hNoxa but are detectable in that by tBid. These results suggest that the efflux of proteins from the mitochondria are differentially modulated by tBid and hNoxa.

고압산소요법시(高壓酸素療法時) 약물요법병행(藥物療法倂行)의 효과에 관(關)한 연구(硏究) (A study on the Effects of Hyperbaric Oxygenation Combined with the Drug Administration in the Treatment of CO poisoning)

  • 윤덕로;김익수
    • Journal of Preventive Medicine and Public Health
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    • 제6권1호
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    • pp.71-76
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    • 1973
  • 1) The oxygen consumption was studied with albino rats under normal environment after they were given Cytochrome C intravenously (10mg/kg). The cosumption was 74.6cc/kg min. with that of control, 75.4cc/kg. min. The difference of the consumptions was not statistically significant. However, under 0.5% CO environment, the oxygen consumption of the Cytochrome C treated rats (62.5cc/kg min) was significantly greater than the control (42.1cc/kg min.) 2) The recovery time of rat acutely poisoned by 1% CO was studied. The recovery time of the Cytochrome C treated group was 37.2 minutes and in control group it was 52.2 minutes. Also significant difference of fatality was noted between the treated group (21.8%) and the untreated group (49.7%) 3) The combined effects of the hyperbaric oxygenation (100% $O_2$ at 3 atmospheric pressures) and the Cytochrome C administration was compared with the effect of the simple hyperbaric oxygenation. There was no significant difference of recovery time between the experimental group while the fatality of the experiment group was lower than control group.

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