The Ku Level


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Students are eligible to take the national certification exam after completion of all program requirements. Student outcomes are measured by these 10 key questions. An oral exam of these questions is given at the end of the first year of study and again as a graduation requirement at the end of the third year. Back to top. Graduation Rates Below are figures for the three most recent calendar years , , for graduates from KU's entry-level master's degree program in occupational therapy. One practical means of demonstrating a program's quality is the success rate of a program's graduates when they take the National Certification exam.

Department Home. Overview Why choose KU? Note: these figures apply to the master's degree program only.

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Last modified: Apr 08, Graduate tuition - Kansas resident. To study whether total levels of Ku change in replicatively senescent cells we used two lines of primary human fibroblasts: embryonic lung fibroblasts IMR and neonatal foreskin fibroblasts HCA2. Each Ku subunit was detected with two different antibodies polyclonal and monoclonal to confirm that the observed reduction in Ku is not caused by conformational change and the use of conformation-specific antibody. In summary, Ku protein levels decline in senescent fibroblasts.


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The observed effect was consistent in two fibroblast cell lines of different tissue origin and affected both subunits of Ku. Ku levels in young and senescent cells. Y, young cells; S, senescent cells. B The Western blots were quantified using ImageQuant software. Black bars represent young cells; white bars represent senescent cells. The experiments were repeated four times, and error bars show standard deviations.

Ku is found in the nucleus, cytoplasm and membrane, therefore we aimed to test which subcellular fraction of Ku was reduced in senescent cells. Young and senescent IMR and HCA2 fibroblasts were grown as described above, harvested and immediately subjected to fractionation. The fractionation procedure was based on differential solubility of cellular compartments in four sequentially applied extraction buffers. The first extraction buffer releases cytosolic proteins, the second buffer solubilizes membranes and organelles, nuclear proteins are released with the third buffer, and cytoskeleton is solubilized with the fourth buffer.

The advantage of this fractionation method is that all the fractions are being extracted from a single cell sample and no protein material is discarded. Therefore, the proteins in the fractions are present in the same proportion as they are found within cells.

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Following fractionation the amount of protein in each fraction and its proportion to the total protein in all four fractions was calculated. The fractions were loaded on a gel according to the proportion of total cellular protein they represent. Such loading shows the distribution of a given protein between subcellular fractions, keeping the same ratio between the different fractions as they are present within the cell. Hybridization with the antibodies to the marker proteins shows that the fractionation procedure was very efficient, and there was virtually no cross-contamination between the fractions.

Subcellular distribution of Ku70 and Ku80 in young and senescent cells. A Western blot analysis of Ku in subcellullar fractions. The fractions were loaded according to the percent of total cellular protein represented by each fraction. The fractions were plotted according to the percent of total cellular protein represented by each fraction. Experiments were repeated four times, and error bars show standard deviations.

Ku70 and Ku80 were localized predominantly in the cytoplasm and the nucleus in young cells Figure 2.

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In senescent cells Ku was localized in the nucleus, and almost disappeared from the cytoplasmic fraction Figure 2. We then used immunohistochemistry to confirm Ku localization results obtained by cell fractionation. In young cells Ku was distributed evenly throughout the nucleus and cytoplasm, while in senescent cells Ku was localized in the nucleus. Thus, we show by both cell fractionation and immunohistochemical techniques that Ku is localized in the nucleus and cytoplasm in the young cells, and changes its localization to nuclear in senescent cells. Immunohistochemical analysis of Ku localization in young and senescent human fibroblasts.

A Untreated young and senescent cells. C Young cells 24 hours after UVC treatment. Replicatively senescent cells enter irreversible G0 growth arrest. We therefore tested whether the changes in Ku levels and intracellular distribution we observed in senescent cells would be found in the young growth-arrested cells.

Normal human fibroblasts enter G1 arrest when cells reach confluence and remain viable on a plate, with regular media changes, for extended periods of time. The levels of Ku70 and Ku80 remained unchanged in the G1 arrested cells. We then tested whether intracellular distribution of Ku in G1-arrested cells. Young cells were kept at confluence for 48 hours or for 7 days and Ku localization was assayed by cell fractionation Figure 4B.

After extended period of arrest the distribution of Ku has changed to acquire a unique distribution where similar levels of Ku were localized in the nucleus, membrane, and cytoplasm. This distribution differs from both young and senescent cells. This result shows that the reduction of Ku levels and the changes of intracellular distribution of Ku in senescent cells are characteristic of senescent cells and not the result of the growth-arrest alone.

Ku levels and intracellular localization in young arrested cells. The total levels of Ku were analyzed by Western blot in whole cell extracts. B Cells were kept at confluence for 48 hours or for 7 days and subcellular distribution of Ku was analyzed by cell fractionation as in Figure 2. We hypothesized that nuclear translocation of Ku in senescent cells is caused by accumulation of DNA breaks and short telomeres that require Ku binding.


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  • To test this hypothesis we subjected young cells to DNA damage and examined the changes in Ku distribution. The cells were harvested 1 h, 5 h, and 24 hours after treatment and subjected to subcellular fractionation as described above, and subcellular fractions and whole cell extracts were analyzed by Western blot.

    Total levels of Ku70 and Ku80 did not change upon treatment data not shown , while marked changes were observed in subcellular distribution of Ku. It is possible that in the young cells cytoplasmic fraction of Ku serves as a reserve that is recruited to the nucleus upon DNA damage. Quantification was done using ImageQuant software.

    Bar's shading represent different time points after irradiation: black bars, 0 time point; dark grey bars, 1 hour after irradiation; light grey bars, 5 hours after irradiation; and white bars, 24 hours after irradiation. The experiments were repeated twice for each cell line and standard deviations are shown.

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    In the young cells subjected to UVC-irradiation both Ku70 and Ku80 moved out of the nucleus into the cytoplasm. The high UVC dose resulted in all Ku being exported into the cytoplasm.

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    The reduction in nuclear Ku was detectable as early as 1 hour after irradiation and almost no Ku was detectable in the nucleus by 24 h post treatment Figure 6. In senescent cells Ku response to UVC was greatly attenuated, with only a small fraction of Ku moving out of the nucleus at either high or low UVC doses. In summary this set of experiments shows that in the young cells Ku changes intracellular distribution after DNA damage.

    This response is impaired in senescent cells, where Ku may be permanently bound to existing DNA lesions in the nucleus and unable to participate in new transactions. The fractions were loaded according to the percent of the total cellular protein represented by each fraction. In this study we examined the levels and intracellular localization of Ku70 and Ku80 proteins during cellular senescence. We show that the levels of both Ku70 and Ku80 in whole cell extracts drop approximately two fold in senescent cells.

    This effect was observed in two normal human fibroblast cell lines of different tissue origin. Ku70 has recently been proposed to be a new biomarker of aging [ 36 ], as reduced Ku levels were also reported in tissues of old rats [ 37 ] and humans [ 36 ]. We have previously shown that NHEJ in senescent cells is less efficient and more error-prone [ 19 ]. The analysis of intracellular distribution of Ku by cell fractionation and immunofluorescence revealed marked differences between young and senescent cells.

    In the young cells Ku is present in the nucleus, cytoplasm, and a small fraction of Ku is localized to the membrane and organelles, while in senescent cells Ku is confined to the nucleus, and a very small amount is found in the membrane fraction.

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    UVC treatment of young cells induced translocation of Ku out of the nucleus into the cytoplasm. The differences in Ku dynamics between young and senescent cells are summarized in Figure 7. Senescence-related changes in Ku distribution and response to DNA damage. In the young cells Ku open circles is present predominantly in the nucleus and cytoplasm.

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    In response to UVC Ku moves out of the nucleus. In senescent cells the majority of Ku protein is localized in the nucleus, presumably in a DNA-bound form crossed circles. Our results suggest that Ku is regulated through its transport in and out of the nucleus. How exactly this happens and what factors and signaling pathways are involved in Ku shuttling remains to be determined.

    We hypothesize that the cytoplasm of young cells contains Ku that serves as a reserve that is recruited to the nucleus upon DNA damage. Senescent cells, in contrast, lack this reserve, so no additional Ku can be brought into the nucleus to repair DNA damage. Furthermore, Ku is unable to move out of the nucleus in senescent cells in response to UVC, which suggests that it is present in a bound form, possibly permanently bound to DNA breaks.


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