Criterion validity and reliability of the International Physical Activity Questionnaire - Hungarian short form against the RM42 accelerometer.

BACKGROUND: Physical inactivity is a global phenomenon in European welfare countries. Proper monitoring is essential to measure the physical activity level of the population. METHODS: In the Hungarian cohort of the European Physical Activity and Sport Monitoring System (EUPASMOS) project, our participants (N = 598) completed sociodemographic questions and the International Physical Activity Questionnaire - short form (IPAQ-SF) survey. The validity and reliability of the subjective measurement tool were examined, IPAQ-SF outcomes were contrasted against triaxial RM42 accelerometer wore for 7 consecutive days. RESULTS: The IPAQ-SF showed moderate internal consistency (Cronbach Alpha = 0.647). The concurrent validity of the IPAQ-SF to triaxial accelerometer indicated a significant weak-to-moderate correlation (R = 0.111-0.338, p = 0.042; p < 0.001). The test-retest reliability showed a significant correlation between two measurements (R = 0.788-0.981, p < 0.001). CONCLUSION: The Hungarian version of the IPAQ-SF had excellent test-retest reliability, but low-to-fair concurrent validity for moderate and vigorous physical activity, walking and sitting time, as compared to the objective criterion measure among Hungarian adults.

Nuclear translocation of the tumor marker pyruvate kinase M2 induces programmed cell death.

Cancer cells often fail to respond to stimuli that normally activate their intrinsic apoptotic machinery. Moreover, they are able to adapt to hypoxia by changing their glycolytic rate. Pyruvate kinase (PK) is a rate-limiting enzyme in glycolysis that is converted to a less active dimer form of PKM2 isoenzyme during oncogenesis. Here, we show that both somatostatin and the structural analogue TT-232 interact with the PKM subtype. We further show that the PKM2 is translocated to the nucleus in response to TT-232 and different apoptotic agents. Nuclear translocation of PKM2 is sufficient to induce cell death that is caspase independent, isoform specific, and independent of its enzymatic activity. These results show that the tumor marker PKM2 plays a general role in caspase-independent cell death of tumor cells and thereby defines this glycolytic enzyme as a novel target for cancer therapy development.