• Title/Summary/Keyword: biochemistry

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JNK activation induced by ribotoxic stress is initiated from 80S monosomes but not polysomes

  • Kim, Tae-Sung;Kim, Hag Dong;Park, Yong Jun;Kong, EunBin;Yang, Hee Woong;Jung, Youjin;Kim, YongJoong;Kim, Joon
    • BMB Reports
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    • v.52 no.8
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    • pp.502-507
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    • 2019

  • Translation is a costly, but inevitable, cell maintenance process. To reduce unnecessary ATP consumption in cells, a fine-tuning mechanism is needed for both ribosome biogenesis and translation. Previous studies have suggested that the ribosome functions as a hub for many cellular signals such as ribotoxic stress response, mammalian target of rapamycin (mTOR), and ribosomal S6 kinase (RSK) signaling. Therefore, we investigated the relationship between ribosomes and mitogen-activated protein kinase (MAPK) activation under ribotoxic stress conditions and found that the activation of c-Jun N-terminal kinases (JNKs) was suppressed by ribosomal protein knockdown but that of p38 was not. In addition, we found that JNK activation is driven by the association of inactive JNK in the 80S monosomes rather than the polysomes. Overall, these data suggest that the activation of JNKs by ribotoxic stress is attributable to 80S monosomes. These 80S monosomes are active ribosomes that are ready to initiate protein translation, rather than polysomes that are already acting ribosomes involved in translation elongation.

  • https://doi.org/10.5483/BMBRep.2019.52.8.273 인용 PDF KSCI

Cytocidal Effect of TALP-32 on Human Cervical Cancer Cell HeLa (TALP-32의 인체자궁암 세포주 HeLa에 대한 세포독성)

  • Park, Ji-Hoon;Kim, Jong-Seok;Yun, Eun-Jin;Song, Kyoung-Sub;Seo, Kang-Sik;Kim, Hoon;Jung, Yeon-Joo;Yun, Wan-Hee;Lim, Kyu;Hwang, Byoung-Doo;Park, Jong-Il
    • Toxicological Research
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    • v.22 no.4
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    • pp.315-322
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    • 2006

  • TALP-32 is highly basic protein with a molecular weight of 32 kDa purified from human term placenta. Some basic proteins such as defensins and cecropins are known to induce cell death by increasing membrane permeability and some of them are under development as an anticancer drug especially targeting multi-drug resistant cancers. Therefore, we investigated cytotoxic effect and mechanism of TALP-32 When HeLa cell was incubated with TALP-32, cytotoxicity was increased in time and dose dependent manner. As time goes by, HeLa cells became round and plasma membrane was ruptured. Increase of plasma membrane permeability was determined with LDH release assay. Also in transmission electron microscopy, typical morphology of necrotic cell death, such as cell swelling and intracellular organelle disruption was observed, but DNA fragmentation and caspase activation was not. And necrotic cell death was determined with Annexin V/Pl staining. The cytotoxicity of TALP-32 was minimal and decreased or RBC and Hep3B respectively. These data suggests that TALP-32 induces necrosis on rapidly growing cells but not on slowly growing cells implicating the possibility of its development of anticancer peptide drug.

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