ABSTRACT
<p><b>OBJECTIVE</b>To explore the relationship between DNA repair in vitro and in vivo after irradiation, and to describe the curves of DNA repair which can improve the accuracy of radiation dose estimation.</p><p><b>METHODS</b>The DNA double-strand break in lymphocytes of human and mouse was detected using neutral single cell gel electrophoresis (SCGE) after radiation and the curves of DNA repair individually were estimated, which were compared later.</p><p><b>RESULTS</b>Along with the time lapsing, the DNA repair of human peripheral blood and mice increased significantly and the residual damage decreased gradually, which showed significant time-effect relationship. The curve of DNA repair in vitro of human lymphocytes presented the same log model as that of mouse DNA repair in vivo. The curve showed as followed respectively: Mice: Y(TM) = 55.8256 - 10.792 lnX (R(2) = 0.629, P < 0.01) and Y(OTM) = 25.4173 - 4.5273 lnX (R(2) = 0.661, P < 0.01); Human: Y(TM) = 30.242 7 - 7.383 6 lnX (R(2) = 0.686, P < 0.01) and Y(OTM) = 17.9772 - 3.9125 lnX (R(2) = 0.752, P < 0.01).</p><p><b>CONCLUSION</b>The curve of DNA repair in vitro of human lymphocytes could be considered in biodosimetry estimation because the process of DNA repair in vitro could display the repair level and speed of DNA double-strand break in vivo.</p>
Subject(s)
Animals , Female , Humans , Male , Mice , Cell Survival , Comet Assay , DNA Damage , Radiation Effects , DNA Repair , Radiation Effects , Dose-Response Relationship, Radiation , Lymphocytes , Radiation Effects , Mice, Inbred Strains , Radiation Dosage , Single-Cell AnalysisABSTRACT
Human K(v) channel interacting protein 1 (KCHIP1) is a new member of the neural calcium binding protein superfamily. Theoretically KCHIP1 has several calcium binding domains and two myristoylation sites. In this study, we demonstrated that the calcium binding domains and myristoylation sites were functional. The first, through running SDS-PAGE gel, we testified its ability of binding Ca(2+) with obvious discrepancy of the electrophoresis migrating rate after binding Ca(2+). Then, through the techniques of fused green fluorescence protein and site-directed mutagenesis, we demonstrated that wild type KCHIP1 protein accumulated in the secretory vesicles of Golgi body. In contrast, its two mutated forms without myristoylation sites accumulated throughout the whole cytoplasm. These observations indicate that KCHIP1 protein has a myristoylation motif mediating the interaction between KCHIP1 protein and membrane.