Despite a fraction of the time commitment, run SIT induces similar body composition, VO(2max), and performance adaptations as ET, but with no effect on Q(max). These data suggest that adaptations with ET are of central origin primarily, whereas those with SIT are more peripheral

We assessed whether 10-s sprint interval training (SIT) bouts with 2 or 4 min recovery periods can improve aerobic and anaerobic performance. Subjects (n = 48) were assigned to one of four groups [exercise time (s):recovery time (min)]: (1) 30:4, (2) 10:4, (3) 10:2 or (4) control (no training). Training was cycling 3 week(-1) for 2 weeks (starting with 4 bouts session(-1), increasing 1 bout every 2 sessions, 6 total). Pre- and post-training measures included: VO(2max), 5-km time trial (TT), and a 30-s Wingate test. All groups were similar pre-training and the control group did not change over time. The 10-s groups trained at a higher intensity demonstrated by greater (P < 0.05) reproducibility of peak (10:4 = 96%; 10:2 = 95% vs. 30:4 = 89%), average (10:4 = 84%; 10:2 = 82% vs. 30:4 = 58%), and minimum power (10:4 = 73%; 10:2 = 69%; vs. 30:4 = 40%) within each session while the 30:4 group performed ~2X (P < 0.05) the total work session(-1) (83-124 kJ, 4-6 bouts) versus 10:4 (38-58 kJ); 10:2 (39-59 kJ). Training increased TT performance (P < 0.05) in the 30:4 (5.2%), 10:4 (3.5%), and 10:2 (3.0%) groups. VO(2max) increased in the 30:4 (9.3%) and 10:4 (9.2%), but not the 10:2 group. Wingate peak power kg(-1) increased (P < 0.05) in the 30:4 (9.5%), 10:4 (8.5%), and 10:2 (4.2%). Average Wingate power kg(-1) increased (P < 0.05) in the 30:4 (12.1%) and 10:4 (6.5%) groups. These data indicate that 10-s (with either 2 or 4 min recovery) and 30-s SIT bouts are effective for increasing anaerobic and aerobic performance.

Evidence indicates that skeletal muscle lipid droplet-associated proteins (PLINs) regulate lipolysis through protein-protein interactions on the lipid droplet surface. In adipocytes, PLIN1 is thought to regulate lipolysis by directly interacting with comparative gene identification-58 (CGI-58), an activator of adipose triglyceride lipase (ATGL). Upon lipolytic stimulation, PLIN1 is phosphorylated, releasing CGI-58 to fully activate ATGL and initiate triglyceride breakdown. The absence of PLIN1 in skeletal muscle leads us to believe that other PLIN family members undertake this role. Our purpose was to examine interactions between PLIN2, PLIN3, and PLIN5, with ATGL and its coactivator CGI-58 at rest and following contraction. Isolated rat solei were incubated for 30 min at rest or during 30 min of intermittent tetanic stimulation [150-ms volleys at 60 Hz with a train rate of 20 tetani/min (25°C)] to maximally stimulate intramuscular lipid breakdown. Results show that the interaction between ATGL and CGI-58 increased 128% following contraction (P ϭ 0.041). Further, ATGL interacts with PLIN2, PLIN3, and PLIN5 at rest and following contraction. The PLIN2-ATGL interaction decreased significantly by 21% following stimulation (P ϭ 0.013). Both PLIN3 and PLIN5 coprecipitated with CGI-58 at rest and following contraction, while there was no detectable interaction between PLIN2 and CGI-58 in either condition. Therefore, our findings indicate that in skeletal muscle, during contraction-induced muscle lipolysis, ATGL and CGI-58 strongly associate and that the PLIN proteins work together to regulate lipolysis, in part, by preventing ATGL and CGI-58 interactions at rest. adipocyte differentiation-related protein; adipophilin; OXPAT; MLDP; TIP47; ABHD5 FATTY ACIDS (FA) RELEASED from intramuscular triglycerides (IMTG) during lipolysis provide an important source of energy during muscle contraction. In skeletal muscle, IMTGs are packaged into lipid droplets that possess a unique coat of proteins associated with the surrounding phospholipid monolayer. This protein coat provides an interface for specific processes, such as transport, lipogenesis, and lipolysis (10, 34). Perilipins (PLINs) are the most recognized family of lipid droplet proteins and are the most likely to be involved in the regulation of lipogenesis and lipolysis in skeletal muscle (31).Our understanding of PLIN proteins in skeletal muscle is limited; however, studies in other tissues and in cell culture indicate that PLIN proteins are key regulators of lipid metabolism, as they appear to be directly involved with how cells and tissues store, mobilize, and utilize fatty acids (8,12,15,34,35,62). The PLIN family consists of five members, PLIN1

Obesity and type 2 diabetes are significant risk factors in the development of neurodegenerative diseases, such as Alzheimer's disease. A variety of cellular mechanisms, such as altered Akt and AMPK and increased inflammatory signaling, contribute to neurodegeneration. Exercise training can improve markers of neurodegeneration, but the underlying mechanisms remain unknown. The purpose of this study was to determine the effects of a single bout of exercise on markers of neurodegeneration and inflammation in brains from mice fed a high-fat diet. Male C57BL/6 mice were fed a low (LFD; 10% kcal from lard)- or a high-fat diet (HFD; 60% kcal from lard) for 7 wk. HFD mice underwent an acute bout of exercise (treadmill running: 15 m/min, 5% incline, 120 min) followed by a recovery period of 2 h. The HFD increased body mass and glucose intolerance (both P < 0.05). This was accompanied by an approximately twofold increase in the phosphorylation of Akt, ERK, and GSK in the cortex (P < 0.05). Following exercise, there was a decrease in beta-site amyloid precursor protein cleaving enzyme 1 (BACE1; P < 0.05) and activity (P < 0.001). This was accompanied by a reduction in AMPK phosphorylation, indicative of a decline in cellular stress (P < 0.05). Akt and ERK phosphorylation were decreased following exercise in HFD mice to a level similar to that of the LFD mice (P < 0.05). This study demonstrates that a single bout of exercise can reduce BACE1 content and activity independent of changes in adiposity. This effect is associated with reductions in Akt, ERK, and AMPK signaling in the cortex.

Introduction Brain-derived neurotrophic factor (BDNF) is an exercise-induced neurotropin mediating neuroprotection and synaptic plasticity. Although exercise intensity is implicated as a potentially important mediator of BNDF release after exercise, the optimal exercise stimulus (interval vs continuous) and intensity (submaximal vs supramaximal) for augmenting circulating BDNF levels remains unknown. Irisin, an exercise-driven myokine, may also contribute to neuroprotection by upregulating BDNF. Purpose To examine the response and recovery of plasma BDNF and irisin after acute exercise of differing intensities. Methods Eight males (23.1 ± 3.0 yr of age; V˙O2max 51.2 ± 4.4 mL·kg−1·min−1) completed four acute exercise sessions: 1) moderate-intensity continuous training (MICT, 65% V˙O2max); 2) vigorous-intensity continuous training (VICT, 85% V˙O2max); 3) sprint interval training (SIT, “all out”); and 4) no exercise (CTRL). Blood was collected preexercise as well as immediately, 30 min, and 90 min postexercise. Plasma BDNF and irisin were assessed with commercially available enzyme-linked immunosorbent assay kits. Results Plasma BDNF levels increased immediately after exercise in the SIT group (P < 0.0001) with plasma concentrations recovering 30 and 90 min postexercise. The BDNF levels after MICT were reduced 30 min postexercise compared with immediately postexercise (P = 0.0189), with no other changes across time points in MICT and VICT groups. Plasma BDNF area under the curve in SIT was significantly higher compared with CTRL, MICT, and VICT (P = 0.0020). No changes in plasma irisin across exercise groups and time points were found (P > 0.9999). Conclusions Plasma BDNF levels increased in an intensity-dependent manner with SIT eliciting the highest BDNF concentration immediately postexercise. These results identify SIT as a time-efficient exercise modality to promote brain health through BDNF release.