Hae Mi Joo

Korea Hydro and Nuclear Power - Central Research Institute, Sŏul, Seoul, South Korea

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Publications (2)8.27 Total impact

  • PLoS ONE 08/2015; 10(8):e0136394. DOI:10.1371/journal.pone.0136394 · 3.23 Impact Factor
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    ABSTRACT: Mast cells play important roles in many biological responses, such as those during allergic diseases and inflammatory disorders. Although laser and UV irradiation have immunosuppressive effects on inflammatory diseases by suppressing mast cells, little is known about the effects of γ-ionizing radiation on mast cells. In this study, we investigated the effects of γ-ionizing radiation on RBL-2H3 cells, a convenient model system for studying regulated secretion by mast cells. Low-dose radiation (<0.1 gray (Gy)) did not induce cell death, but high-dose radiation (>0.5 Gy) induced apoptosis. Low-dose ionizing radiation significantly suppressed the release of mediators (histamine, β-hexosaminidase, IL-4, and tumor necrosis factor-α) from immunoglobulin E (IgE)-sensitized RBL-2H3 cells. To determine the mechanism of mediator release inhibition by ionizing radiation, we examined the activation of intracellular signaling molecules such as Lyn, Syk, phospholipase Cγ, PKCs, and MAPK, and intracellular free calcium concentrations ([Ca2+]i). The phosphorylation of signaling molecules following stimulation of high-affinity IgE receptor I (FcϵRI) was specifically inhibited by low-dose ionizing radiation (0.01 Gy). These results were due to the suppression of FcϵRI expression by the low-dose ionizing radiation. Therefore, low-dose ionizing radiation (0.01 Gy) may function as a novel inhibitor of mast cell activation.
    Journal of Biological Chemistry 06/2012; 287(33):27789-95. DOI:10.1074/jbc.M112.378497 · 4.57 Impact Factor
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    ABSTRACT: Ret finger protein 2 (RFP2), a gene frequently deleted in multiple tumor types, encodes a protein with a RING finger, B-box, and coiled-coil domain that belongs to the RBCC/TRIM protein family. Although RBCC proteins are involved in diverse cellular processes such as apoptosis, proliferation, differentiation, and transcriptional regulation, the biological function of RFP2 has not been well defined. Here, we demonstrate that overexpression of RFP2 in cells induced apoptosis through proteasomal degradation of MDM2 and AKT. The expression of RFP2, which possesses RING domain-dependent E3 ubiquitin ligase activity, was increased by ionizing radiation dose- and time-dependently, and RFP2 overexpression induced cell death with increased expression of apoptotic molecules (p53, p21, and Bax). These results depended on the E3 ubiquitin ligase activity of RFP2 because mutant RFP2, which contains a mutated RING domain, failed to drive apoptosis compared with wild-type RFP2. We observed that RFP2 formed a complex with MDM2, a negative regulator of the p53 tumor suppressor, and AKT, a regulator of apoptosis inhibition at the cellular level. Additionally, we found that the interaction of RFP2 with MDM2 and AKT resulted in ubiquitination and proteasomal degradation of MDM2 and AKT in vivo and in vitro. Thus, these data suggest that irradiation causes RFP2 overexpression, which enhances ionizing radiation-induced apoptosis by increasing p53 stability and decreasing AKT kinase activity through MDM2 and AKT degradation.
    European journal of cell biology 02/2011; 90(5):420-31. DOI:10.1016/j.ejcb.2010.12.001 · 3.70 Impact Factor

Publication Stats

19 Citations
8.27 Total Impact Points


  • 2012
    • Korea Hydro and Nuclear Power - Central Research Institute
      Sŏul, Seoul, South Korea
  • 2011
    • Radiation Health Research Institute
      Sŏul, Seoul, South Korea