Although heat-shock factor (HSF) 1 is a known transcriptional factor of heat-shock proteins, other pathways like production of aneuploidy and increased protein stability of cyclin B1 have been proposed. In the present study, the regulatory domain of HSF1 (amino-acid sequence 212-380) was found to interact directly with the amino-acid sequence 106-171 of Cdc20. The association between HSF1 and Cdc20 inhibited the interaction between Cdc27 and Cdc20, the phosphorylation of Cdc27 and the ubiquitination activity of anaphase-promoting complex (APC). The overexpression of HSF1 inhibited mitotic exit and the degradations of cyclin B1 and securin, which resulted in production of aneuploidy and multinucleated cells, but regulatory domain-deficient HSF1 did not. Moreover, HSF1-overexpressing cells showed elevated levels of micronuclei and genomic alteration. The depletion of HSF1 from cells highly expressing HSF1 reduced nocodazole-mediated aneuploidy in cells. These findings suggest a novel function of HSF1 frequently overexpressed in cancer cells, to inhibit APC/C activity by interacting with Cdc20, and to result in aneuploidy development and genomic instability.

This paper reports experimental and analytical studies on the capture efficiency of a superconducting high-gradient magnetic separation (HGMS) system, employing ferromagnetic filters with various wire diameters and packing fractions. The magnetization force was inversely proportional to wire diameter because the magnetic field gradient increased with decreasing wire diameter. In addition, the capture efficiency of the HGMS system was increased with decreasing wire diameter and increasing packing fraction. The experimental results from the filtration tests via the superconducting HGMS system were in reasonably good agreement with the capture efficiency using the magnetization force obtained by magnetic field analysis.