The purpose of the present study was to examine muscle use during double poling (DP) at two work intensities by use of PET. Eight male subjects performed two 20-min DP bouts on separate days. Work intensity was similar to 53 and 74% of peak oxygen uptake (V.O(2peak)), respectively. During exercise 188 +/- 8 MBq of [(18)F]fluorodeoxyglucose

([(18)F]FDG) was injected, and subsequent to exercise a full-body PET scan was conducted. Regions of interest Selleckchem AZD7762 (ROI) were defined within 15 relevant muscles, and a glucose uptake index (GUI) was determined for all ROIs. The muscles that span the shoulder and elbow joints, the abdominal muscles, and hip flexors displayed the greatest GUI during DP. Glucose uptake did not increase significantly from low to high intensity in most upper body muscles; however, an increased GUI (P < 0.05) was seen for the knee flexor (27%) and extensor muscles (16%), and for abdominal muscles (21%). The present data confirm previous findings that muscles of the upper limb are the primary working muscles in DP. The present data further suggest that when exercise intensity increases,

the muscles that span the lumbar spine, hip, and knee joints contribute increasingly. Finally, PET provides a promising alternative or supplement to existing methods to CT99021 inhibitor assess muscle activation in complex human movements.”
“Multidrug resistance-associated protein 4 (MRP4) check details is an organic anion efflux pump capable of transporting nucleoside, nucleotide analogs, and cyclic nucleotide. MRP4 could have an influence on the resistance and transport of the two oxazaphosphorines, cyclophosphamide (CP) and ifosfamide (IF). V/HepG2 (HepG2, hepatoma cells stably transfected with an empty vehicle plasmid) and MRP4/HepG2 (HepG2 cells stably expressing MRP4) were exposed to CP and IF in the absence or presence of various MRP4 inhibitors. HepG2 and HEK293 human kidney cells were also used to investigate the inducing potency of oxazaphosphorines on the MRP4 expression. In this study, insertion of MRP4 gene in HepG2 cells was found to confer significant resistance

to CP and IF in the 48-h drug-exposure assays. In the presence of various MRP4 inhibitors, the resistance to CP and IF was then partially reversed. These indicate that CP and IF are highly possible substrates of MRP4. In addition, CP and clofibrate (CFB), a reported MRP4 inducer, in vivo significantly increased the MRP4 expression at both protein level and mRNA level in HEK293 cells at higher concentrations, while IF significantly decreased the MRP4 expression at mRNA level at lower concentration and had no effect at higher concentrations. However, all tested compounds (CP, IF, and CFB) did not change the MRP4 protein expression in HepG2 cells. CP and CFB are cell-specific and concentration-dependent MRP4 inducers.