Relation Between Iliopsoas Cross-sectional Area and Kicked Ball Speed in Soccer Players.

This study aimed to investigate the relationship between the maximal anatomical cross-sectional area (ACSA) of the iliopsoas muscle and ball speed in side-foot and instep kicks. The ACSA of the psoas major and iliacus was measured in 29 male collegiate soccer players by using magnetic resonance imaging. They performed maximal side-foot and instep kicks to a stationary ball. The kicked ball speed was measured with a high-speed camera. Ball speed in the side-foot and instep kicks was significantly correlated with body height (side-foot kick: r=0.650, P<0.001; instep kick: r=0.583, P<0.001). After adjustment for body height, the maximal ACSA of the psoas major was significantly correlated with ball speed in the side-foot kick (r=0.441, P=0.017), but not in the instep kick. The maximal ACSA of the iliacus was not correlated with ball speed in side-foot or instep kicks, even after adjustment for body height. Our results suggest that: 1) body height is a significant determinant of the ball speed in side-foot and instep kicks, and 2) for a given body height, the maximal ACSA of the dominant psoas major is a factor that affects the ball speed in side-foot kick.

Solution structure of a DNA mimicking motif of an RNA aptamer against transcription factor AML1 Runt domain.

AML1/RUNX1 is an essential transcription factor involved in the differentiation of hematopoietic cells. AML1 binds to the Runt-binding double-stranded DNA element (RDE) of target genes through its N-terminal Runt domain. In a previous study, we obtained RNA aptamers against the AML1 Runt domain by systematic evolution of ligands by exponential enrichment and revealed that RNA aptamers exhibit higher affinity for the Runt domain than that for RDE and possess the 5'-GCGMGNN-3' and 5'-N'N'CCAC-3' conserved motif (M: A or C; N and N' form Watson-Crick base pairs) that is important for Runt domain binding. In this study, to understand the structural basis of recognition of the Runt domain by the aptamer motif, the solution structure of a 22-mer RNA was determined using nuclear magnetic resonance. The motif contains the AH(+)-C mismatch and base triple and adopts an unusual backbone structure. Structural analysis of the aptamer motif indicated that the aptamer binds to the Runt domain by mimicking the RDE sequence and structure. Our data should enhance the understanding of the structural basis of DNA mimicry by RNA molecules.