This study aimed to compare and analyze the changes in the coagulation factors in fresh frozen plasma (FFP) prior to and following leukocyte filtration and irradiation. In total, 30 bags of FFP from healthy donors were processed: One-third of the FFP of each bag was left within the original bag (the A group), the other two-thirds of the FFP of each bag were passed through a disposable leukocyte filter, then divided equally into two parts. One of these was designated as the B group, and the other was designated the C group (subjected to 30 Gy irradiation). All samples were analyzed to evaluate 16 coagulation indicators. Analysis of variance revealed that there were statistically significant differences in the levels of fibrinogen (FbgC) and coagulation factor VIII (FVIII:C) among the groups (P=0.044 and P=0.015, respectively); the Dunnett’s t-test revealed that there was a statistically significant difference in the level of FbgC between the A and B groups (P=0.025), and there was a statistically significant difference in the level of FVIII:C between the A and C groups (P=0.009); while the remaining 14 coagulation parameters were not significantly different among the groups. Although the levels of FbgC and FVIII:C in the FFP were reduced following treatment, this would not affect the clinical effect of the FFP.
LMO7, an actin cytoskeleton‐associated protein, was identified to be able to interact with the spindle assembly checkpoint (SAC) protein MAD1 in our yeast two‐hybrid screening. LMO7a and LMO7b are known to be two major isoforms of LMO7 in human and rat cells. LMO7a contains CH, F‐box, PDZ and LIM domains whereas LMO7b does CH, PDZ and LIM domains. We find that LMO7 is a mitotic phosphoprotein and its expression is cell cycle‐regulated. Fluorescence microscopic analysis revealed that MAD1 and LMO7 colocalized to the spindle poles in metaphase. We observed that overexpression but not depletion of LMO7 could cause a defect in the SAC. Furthermore, overexpression of LMO7ΔLIM, a LMO7 mutant protein lacking LIM domain, did not cause a defect in the SAC. Strikingly, the LIM peptide fused to GFP, GFP‐LIM, could localize to the spindle poles, and its expression did not affect kinetochore localization of MAD1 but still could cause a defect in the SAC. These observations suggest that the LIM domain is the determinant for localization of LMO7 to the spindle poles and its role in the SAC. We further identified that YPEL1, a spindle pole‐associated protein, could interact with the LIM domain of LMO7. However, overexpression of YPEL1 could not relieve but instead exacerbate the defect in the SAC caused by overexpression of GFP‐LIM. The significance of LMO7‐YPEL1 interaction in the SAC is under investigation.
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