• 제목/요약/키워드: mechanism of translocation

검색결과 216건 처리시간 0.029초

High Mobility Group Box 1 Protein Is Methylated and Transported to Cytoplasm in Clear Cell Renal Cell Carcinoma

  • Wu, Fei;Zhao, Zuo-Hui;Ding, Sen-Tai;Wu, Hai-Hu;Lu, Jia-Ju
    • Asian Pacific Journal of Cancer Prevention
    • /
    • 제14권10호
    • /
    • pp.5789-5795
    • /
    • 2013
  • Background: The high mobility group box 1 (HMGB1) protein is a widespread nuclear protein present in most cell types. It typically locates in the nucleus and functions as a nuclear cofactor in transcription regulation. However, HMGB1 can also localize in the cytoplasm and be released into extracellular matrix, where it plays critical roles in carcinogenesis and inflammation. However, it remains elusive whether HMGB1 is relocated to cytoplasm in clear cell renal cell carcinoma (ccRCC). Methods: Nuclear and cytoplasmic proteins were extracted by different protocols from 20 ccRCC samples and corresponding adjacent renal tissues. Western blotting and immunohistochemistry were used to identify the expression of HMGB1 in ccRCC. To elucidate the potential mechanism of HMGB1 cytoplasmic translocation, HMGB1 proteins were enriched by immunoprecipitation and analyzed by mass spectrometry (MS). Results: The HMGB1 protein was overexpressed and partially localized in cytoplasm in ccRCC samples (12/20, 60%, p<0.05). Immunohistochemistry results indicated that ccRCC of high nuclear grade possess more HMGB1 relocation than those with low grade (p<0.05). Methylation of HMGB1 at lysine 112 in ccRCC was detected by MS. Bioinformatics analysis showed that post-translational modification might affect the binding ability to DNA and mediate its translocation. Conclusion: Relocation of HMGB1 to cytoplasm was confirmed in ccRCC. Methylation of HMGB1 at lysine 112 might the redistribution of this cofactor protein.

CKD-501 INDUCED GLUCOSE TRANSPORT WAS MAINLY CAUSED BY THE STIMULATION OF GLUCOSE TRANSPOTER- TRANSLOCATION IN L6-MYOTUBES

  • Moon, C.K.;Jung, A.Y.;Kim, M.H.;Lee, Y.H.;Chae, S.H.;Kim, K.S.;Jo, Y.Y.;Kim, M.H.;Moon, K.S.
    • 대한약학회:학술대회논문집
    • /
    • 대한약학회 2003년도 Proceedings of the Convention of the Pharmaceutical Society of Korea Vol.1
    • /
    • pp.157-158
    • /
    • 2003
  • A newly synthesized thiazolodinedione derivative, CKD-501, was confirmed to have antihyperglycemic effect in in vivo study. The present study was undertaken to investigate the effect of CKD-501 on glucose transport and its stimulating mechanism in L6-myotubes. L6-myoblasts were cultured and differentiated to myotubes by reducing serum concentration in media from 10% to 2%. (omitted)

  • PDF

Glutathione Depletion by L-Buthionine-S,R-Sulfoximine Induces Apoptosis of Cardiomyocytes through Activation of PKC-δ

  • Kim, Young-Ae;Kim, Mi-Young;Jung, Yi-Sook
    • Biomolecules & Therapeutics
    • /
    • 제21권5호
    • /
    • pp.358-363
    • /
    • 2013
  • In the present study, we investigated the effect of intracellular glutathione (GSH) depletion in heart-derived H9c2 cells and its mechanism. L-buthionine-S,R-sulfoximine (BSO) induced the depletion of cellular GSH, and BSO-induced reactive oxygen species (ROS) production was inhibited by glutathione monoethyl ester (GME). Additionally, GME inhibited BSO-induced caspase-3 activation, annexin V-positive cells, and annexin V-negative/propidium iodide (PI)-positive cells. Treatment with rottlerin completely blocked BSO-induced cell death and ROS generation. BSO-induced GSH depletion caused a translocation of PKC-${\delta}$ from the cytosol to the membrane fraction, which was inhibited by treatment with GME. From these results, it is suggested that BSO-induced depletion of cellular GSH causes an activation of PKC-${\delta}$ and, subsequently, generation of ROS, thereby inducing H9c2 cell death.

Regulation of Nrf2-Mediated Phase II Detoxification and Anti-oxidant Genes

  • Keum, Young-Sam
    • Biomolecules & Therapeutics
    • /
    • 제20권2호
    • /
    • pp.144-151
    • /
    • 2012
  • The molecular mechanisms by which a variety of naturally-occurring dietary compounds exert chemopreventive effects have been a subject of intense scientific investigations. Induction of phase II detoxification and anti-oxidant enzymes through activation of Nrf2/ARE-dependent gene is recognized as one of the major cellular defense mechanisms against oxidative or xenobiotic stresses and currently represents a critical chemopreventive mechanism of action. In the present review, the functional significance of Keap1/Nrf2 protein module in regulating ARE-dependent phase II detoxification and anti-oxidant gene expression is discussed. The biochemical mechanisms underlying the phosphorylation and expression of Keap1/Nrf2 proteins that are controlled by the intracellular signaling kinases and ubiquitin-mediated E3 ligase system as well as control of nucleocytoplasmic translocation of Nrf2 by its innate nuclear export signal (NES) are described.

From Cytosol to Mitochondria: The Bax Translocation Story

  • Khaled, Annette R.;Durum, Scott. K.
    • BMB Reports
    • /
    • 제34권5호
    • /
    • pp.391-394
    • /
    • 2001
  • The balance between life and death of a cell regulates essential developmental processes in multicellular organisms. Apoptotic cell death is a complex, stepwise program involving multiple protein components that trigger and execute the demise of the cell. Of the many triggers of apoptosis, most are not well understood, but some key components have been identified, such as those of the Bcl-2 family, which function as anti-apoptotic or proapoptotic factors. Bax, a pro-apoptotic member of this family, has been shown to serve as a component of many apoptotic triggering cascades and its mechanism of action is the focus of intense study. Herein we discuss current, differing ideas on the function of Bax and its structure, and suggest novel mechanisms for how this death protein targets mitochondria, triggering apoptosis.

  • PDF

gInhibition effect of nitric oxide production and NF-kB nuclear translocation by 2-hydroxycinnamaldehyde in RAW 264.7 cells

  • Lee, Seung-Ho;Lee, Sun-Young;Park, Hye-Ji;Lee, Yoot-Mo;Lee, Hee-Soon;Song, Suk-Gil;Yoo, Hwan-Soo;Oh, Ki-Wan;Kwon, Byoung-Mog
    • 대한약학회:학술대회논문집
    • /
    • 대한약학회 2003년도 Proceedings of the Convention of the Pharmaceutical Society of Korea Vol.2-2
    • /
    • pp.99.1-99.1
    • /
    • 2003
  • Cinnamaldehyde is the main component of cinnamon bark oil and show several biological activities such as anti-tumor, anti-fungal, anti-mutagenic and anti-inflammatory effects. A couple of studies have investigated how the natural compound exerts its anti-inflammatory effect. In despite of numerous investigations, the biological mechanism of effects belong to cinnamaldehyde remain unclear. We isolated 2-hydroxycinnamaldehyde(HCA) from the bark of Cinnamomun cassia Blume and reported a various of biological activities of HCA. (omitted)

  • PDF

광합성산물의 아포플라스트 체관부적재 기작 (Apoplastic Phloem Loading of Photoassimilate)

  • 김성문;허장현;한대성
    • 한국잡초학회지
    • /
    • 제17권4호
    • /
    • pp.345-361
    • /
    • 1997
  • Photoassimilates translocate from regions of carbohydrate synthensis(source) to regions of carbohydrate utilization or storage(sink). In the source, assimilate loads into the phloem for long-distance transport. Current evidence suggests that there are twig loading mechanisms : one involves assimilate transfer via the apoplasm and then load into the phloem by carrier-mediated proton-sucrose cotransport, while the other involves movement through the continuous symplastic connections between the mesophyll cells and the phloem. Inspite of problems associated with the interpretation of experiments, the evidence for apoplastic loading remains convincing because the apoplastic loading systems explains well the observed accumulation capacity arid the selectivity of assimilate uptake by tile phloem.

  • PDF

Regulation of Nrf2 Mediated Phase II Enzymes by Luteolin in human Hepatocyte

  • Park, Chung Mu
    • 대한의생명과학회지
    • /
    • 제20권2호
    • /
    • pp.56-61
    • /
    • 2014
  • This study attempted to confirm the antioxidative potential of luteolin against tert-butyl hydroperoxide (t-BHP) induced oxidative damage and to investigate its molecular mechanism related to glutathione (GSH)-dependent enzymes in HepG2 cells. Treatment with luteolin resulted in attenuation of t-BHP induced generation of reactive oxygen species (ROS) and oxidative stress-mediated cell death. In addition, accelerated expression of GSH-dependent antioxidative enzymes, glutathione peroxidase (GPx) and glutathione reductase (GR), and heme oxygenase (HO)-1, as well as strengthened GSH content was induced by treatment with luteolin, which was in accordance with increased nuclear translocation of nuclear factor-erythroid 2 p45-related factor 2 (Nrf2), a transcription factor for phase 2 enzymes, in a dose-dependent manner. These results suggest that the cytoprotective potential of luteolin against oxidative damage can be attributed to fortified GSH-mediated antioxidative pathway and HO-1 expression through regulation of Nrf2 in HepG2 cells.

Researches Using Radio-labelled Insecticides in Korea

  • Lee, Kyu-Seung
    • 한국환경농학회지
    • /
    • 제26권4호
    • /
    • pp.351-363
    • /
    • 2007
  • The scientific articles using radio labelled insecticides performed by Korean researchers were reviewed. The research works were divided into 4 categories such as soil, plant, animal and insect. All researches used $^{14}C$-labelled chemicals, and the $^{14}C$-carbofuran was widely used among them. Fate of insecticides, bound-residues and metabolic process were staple concerning area in soil study. And the uptake and translocation, metabolism and metabolites also a major interests in plant study. As well as the degradation, metabolic pathway and metabolites, and distribution of chemicals in animal tissue were another point of consideration in animal study. And finally, the penetration ratio into body and resistant mechanism were the major concerning views of study with insects.

P62 and the Sequestosome, a Novel Mechanism for Protein Metabolism

  • Shin, Jae-Kyoon
    • Archives of Pharmacal Research
    • /
    • 제21권6호
    • /
    • pp.629-633
    • /
    • 1998
  • In addition to selecting proteins for degradation by the 26S proteasome, ubiqitination appears to serve other regulatory functions, including for endosomal/lysosomal targeting, protein translocation, and enzyme modification. Currently, little is known how multiubiquitin chains are recognized by these cellular mechanisms. Within the 26S proteasome, one subunit (Mcb1/S5a) has been identified that has affinity for multiubiquitin chains and may function as a ubiquitin receptor. We recently found that a non-proteasomal protein p62 also preferentially binds multiubiquitin chains and forms a novel cytoplasmic structure "sequestosome" which serves as a storage place for ubiquitinated proteins. In the present manuscript, the role and regulation of p62 in relation to the sequestosomal function will be reviewed.

  • PDF