用加铅挡块的方法直接测定体模散射因子Sp的探讨

目的：按Ｓｐ的定义，直接测量体模散射因子Ｓｐ。方法：在准直器开口不变的情况下，用加挡块的方法改变各射野在模体中的散射面积。分别测定各射野在模体中参考点处的吸收剂量率和加挡块和同一点的吸收剂量率，再根据Ｓｐ的定义、计算出Ｓｐ因子。结果：通过测量，直接得到各射野的体模散射因子Ｓｐ和总散射校正因子Ｓｃｐ，然后求出各射野的准直器散射修正因子Ｓｃ。结论：用本文加挡块的方法测定Ｓｐ因子，可以降低制作高能Ｘ线的     

Development of an in vitro test system for assessment of male,reproductive toxicity

There is a need for improved reproductive toxicology assays that do not require large numbers of animals but are sensitive and informative. Therefore, Staput velocity-sedimentation separation followed by culture of specific mouse testicular cells was used as such a system. The specificity of separation was assessed using immunocytochemistry to identify spermatids, spermatocytes and spermatogonia. The efficacy of the system to detect toxicity was then evaluated by analysing the effects of hydrogen peroxide (H₂O₂) by the terminal uridine-deoxynucleotide end-labelling (TUNEL) assay to show the rate of apoptosis induced among the different types of germ cells. We found that 2 h of treatment at both 1 and 10 μM induced increases of over ∼10-fold in the percentage of apoptotic cells (p ≤ 0.001), confirming that testicular germ cells are prone to apoptosis at very low concentrations of H₂O₂. It was also demonstrated for the first time for this compound that spermatogonia are significantly more susceptible than spermatocytes, which are more affected than spermatids. This reflects the proportion of actively dividing cells in these cell types, suggesting a mechanism for the differential sensitivity. The approach should thus form the basis of a useful test system for reproductive and genetic toxicology in the future.     

The SESA network links duplication of the yeast centrosome with the protein translation machinery

The yeast spindle pole body (SPB), the functional equivalent of mammalian centrosome, duplicates in G1/S phase of the cell cycle and then becomes inserted into the nuclear envelope. Here we describe a link between SPB duplication and targeted translation control. When insertion of the newly formed SPB into the nuclear envelope fails, the SESA network comprising the GYF domain protein Smy2, the translation inhibitor Eap1, the mRNA-binding protein Scp160 and the Asc1 protein, specifically inhibits initiation of translation of POM34 mRNA that encodes an integral membrane protein of the nuclear pore complex, while having no impact on other mRNAs. In response to SESA, POM34 mRNA accumulates in the cytoplasm and is not targeted to the ER for cotranslational translocation of the protein. Reduced level of Pom34 is sufficient to restore viability of mutants with defects in SPB duplication. We suggest that the SESA network provides a mechanism by which cells can regulate the translation of specific mRNAs. This regulation is used to coordinate competing events in the nuclear envelope.