IMAGING OF ADENOVIRUS-MEDIATED GENE TRANSFER OF HUMAN SODIUM IODIDE SYMPORTER BY TC-99M PERTECHNETATE SCINTIGRAPHY IN MICE
作者单位：Departments of Nuclear Medicine Asan Medical CenterUniversity of Ulsan College of MedicineSeoulKorea Departments of Nuclear Medicine Asan Medical CenterUniversity of Ulsan College of MedicineSeoulKorea Departments of Microbiology Asan Medical CenterUniversity of Ulsan College of MedicineSeoulKorea Departments of Microbiology Asan Medical CenterUniversity of Ulsan College of MedicineSeoulKorea Departments of Microbiology Asan Medical CenterUniversity of Ulsan College of MedicineSeoulKorea Departments of Microbiology Asan Medical CenterUniversity of Ulsan College of MedicineSeoulKorea
会议名称：《首届中日韩核医学会议》
会议日期：2002年
学科分类：0831[工学-生物医学工程（可授工学、理学、医学学位）] 100207[医学-影像医学与核医学] 1006[医学-中西医结合] 1002[医学-临床医学] 1001[医学-基础医学(可授医学、理学学位)] 08[工学] 1010[医学-医学技术（可授医学、理学学位）] 100106[医学-放射医学] 100602[医学-中西医结合临床] 10[医学]
摘 要：正Objectives: Human sodium iodide symporter （hNIS） is naturally present in the plasma membrane of human thyroid cells, which mediates the active transport of iodide. The aim of this study was to explore the possibility of imaging the adenovirus-mediated gene transfer of hNIS by Tc-99m pertechnetate （TcO4） scintigraphy in mice. Methods: Replication-defective recombinant adenovirus was prepared, which encoded either hNIS （Rad-hNIS） or LacZ （Rad-LacZ） gene expression cassette. hNIS gene expression was examined by western blotting in hNIS defective thyroid cancer cell line （FRO） infected with Rad-hNIS 48hr post-infection. The uptake of TcO4 was then evaluated by adding the tracer to culture media. To monitor hNIS expression in vivo, 9 to 12wk-old balb/c mice were injected with Tris buffer only, 2x108, 1x109 infectious particles （IP） of Rad-hNIS, or 1x109 IP of Rad-LacZ via tail vein （n=5-7 for each group）. Forty-eight hrs later, 3.7 MBq of TcO4 was injected intraperitoneally and whole body images were obtained for 1 hr. Then, mice were sacrificed for the biodistribution of TcO4 and the measurement of hNIS mRNA by RT-PCR. Results: hNIS protein was readily detected in the FRO cells infected with Rad-hNIS at 10 MOI. TcO4 uptake increased gradually as the cells were infected with increasing Rad-hNIS （96.5±51.4, 266.9±91.3, and 558.6±160.7-fold increase at MOI 5, 20, 100, respectively）. Sodium perchlorate inhibited the uptake completely. Scintigraphic and biodistribution studies clearly revealed high hepatic uptake of TcO4 （22.7□11.2 % injected dose/g） in mice injected with 1x109 IP of Rad-hNIS, which was significantly higher （p 0.01） than that in mice injected with Tris buffer （7.4 □0.5）, 2x108 IP of Rad-hNIS （8.5 □2.7）, or 1x109 IP of Rad-LacZ （5.8 □0.8）. Co-administration of sodium perchlorate inhibited the hepatic uptake of TcO4. hNIS mRNA was exclusively detected in the liver of Rad-hNIS groups, with much higher intensity in 1x109 Rad-hNIS group. Two mice injected wi