Search PubMed⌕ Search

PubMed · 1834037

Torque development in isokinetic training.

Abstract

Twenty men were randomized into three groups that performed maximal isokinetic knee extensions five days a week for 12 weeks; a fourth group was a control group. The training protocol was different for the opposite lower extremity of each subject, such that subjects in group I trained at 36 degrees/sec with 20 or 60 repetitions, group II did 20 repetitions at 36 degrees/sec with one limb and 60 repetitions at 108 degrees/sec contralaterally, and group III trained at 108 degrees/sec with 20 or 60 repetitions. Group IV did no training. Bilateral pretraining and posttraining vastus lateralis muscle biopsies were done, and maximal torque-velocity tests (0 degrees to 234 degrees/sec at 18 degrees/sec steps) were performed every two weeks. The muscle biopsies were examined for muscle-fiber area and enzyme activity. Statistical analysis of the torque-velocity curves showed that subjects who trained at 36 degrees/sec made significant overall gains in torque and significantly greater torque gains than those training at 108 degrees/sec. Torque gains were not made uniformly during the 12 weeks of training; they occurred primarily during the initial 4 to 8 weeks. There were no significant increases in muscle-fiber areas in response to training, but there were increases in glycolytic and mitochondrial enzyme activities. These findings suggest that the critical variable for developing strength (maximal torque), at least within the context of isokinetic training, is the amount of torque developed during training.

Explore related subjects

Keep this discovery

Explore connections, maps & timelines

BibTeXRIS

P C Esselman, B J de Lateur, A D Alquist, K A Questad, R M Giaconi. 1991. Torque development in isokinetic training.. https://pubmed.ncbi.nlm.nih.gov/1834037/

Cite the original work for its findings. Save a collection to share your selection of sources.

KEEP EXPLORING

Related citations

Isolation and characterization of Plasmodium falciparum UAP56 homolog: evidence for the coupling of RNA binding and splicing activity by site-directed mutations.

UAP56 (U2AF65 associated protein) is a member of the DEAD-box helicase family. Helicases are essential enzymes generally involved in the metabolism of nucleic acids. The gene encoding a member of DEAD-box family was cloned and characterized from the human malaria parasite Plasmodium falciparum. PfU52 is homologous to UAP56 and contains the RNA-dependent ATPase, RNA helicase and RNA binding activities. Using the parasite extract we report that PfU52 is involved in splicing reaction. Site-directed mutagenesis studies indicate that the conserved residues glycine 181, isoleucine 182 and arginine 206 are involved in RNA binding and this activity is required for the enzymatic activities of PfU52. PfU52 is expressed in all the intraerythrocytic developmental stages of the parasite. In the present study we have reported the detailed characterization of PfU52 from P. falciparum and these results advance the knowledge regarding the function of UAP56 in general.

Adenosine Triphosphatases↗

Hormonal regulation of the Menkes and Wilson copper-transporting ATPases in human placental Jeg-3 cells.

Copper deficiency during pregnancy results in early embryonic death and foetal structural abnormalities including skeletal, pulmonary and cardiovascular defects. During pregnancy, copper is transported from the maternal circulation to the foetus by mechanisms which have not been clearly elucidated. Two copper-transporting ATPases, Menkes (ATP7A; MNK) and Wilson (ATP7B; WND), are expressed in the placenta and both are involved in placental copper transport, as copper accumulates in the placenta in both Menkes and Wilson disease. The regulatory mechanisms of MNK and WND and their exact role in the placenta are unknown. Using a differentiated polarized Jeg-3 cell culture model of placental trophoblasts, MNK and WND were shown to be expressed within these cells. Distinct roles for MNK and WND are suggested on the basis of their opposing responses to insulin. Insulin and oestrogen increased both MNK mRNA and protein levels, altered the localization of MNK towards the basolateral membrane in a copper-independent manner, and increased the transport of copper across this membrane. In contrast, levels of WND were decreased in response to insulin, and the protein was located in a tight perinuclear region, with a corresponding decrease in copper efflux across the apical membrane. These results are consistent with a model of copper transport in the placenta in which MNK delivers copper to the foetus and WND returns excess copper to the maternal circulation. Insulin and oestrogen stimulate copper transport to the foetus by increasing the expression of MNK and reducing the expression of WND. These data show for the first time that MNK and WND are differentially regulated by the hormones insulin and oestrogen in human placental cells.

Adenosine Triphosphatases↗

Green tea catechins inhibit bacterial DNA gyrase by interaction with its ATP binding site.

Catechins are the main ingredients of green tea extracts and have been shown to possess versatile biological activities, including antimicrobial. We determined that the catechins inhibit bacterial DNA gyrase by binding to the ATP binding site of the gyrase B subunit. In the group of four tested catechins, epigallocatechin gallate (EGCG) had the highest activity, followed by epicatechin gallate (ECG) and epigallocatechin (EGC). Specific binding to the N-terminal 24 kDa fragment of gyrase B was determined by fluorescence spectroscopy and confirmed using heteronuclear two-dimensional NMR spectroscopy of the EGCG-15N-labeled gyrase B fragment complex. Protein residues affected by binding to EGCG were identified through chemical shift perturbation. Molecular docking calculations suggest that the benzopyran ring of EGCG penetrates deeply into the active site while the galloyl moiety anchors it to the cleft through interactions with its hydroxyl groups, which explains the higher activity of EGCG and ECG.

Adenosine Triphosphatases↗