Now showing 1 - 5 of 5
- PublicationMetadata onlyResistance training does not increase myocellular garbage dumps: A pilot study on lipofuscin in skeletal muscle fibers of resistance trained young menLipofuscin (LF) is an intracellular aggregate associated with proteostatic impairments, especially prevalent in nondividing skeletal muscle fibers. Reactive oxygen species (ROS) drive LF-formation. Resistance training (RT) improves muscle performance but also increases ROS production, potentially promoting LF-formation. Thus, we aimed to investigate if RT of a mesocycle duration increases LF-formation in type-I and II muscle fibers and whether RT increases the antioxidant capacity (AOC) in terms of SOD1 and SOD2 content. An intervention group (IG) performed 14 eccentrically accented RT-sessions within 7 weeks. Vastus lateralis muscle biopsies were collected before and after the intervention from IG as well as from a control group (CG) which refrained from RT for the same duration. LF was predominantly found near nuclei, followed by membrane-near and a minor amount in the fiber core, with corresponding spot sizes. Overall, LF-content was higher in type-I than type-II fibers (p < 0.05). There was no increase in LF-content in type-I or IIA fibers, neither for the IG following RT nor for the CG. The same is valid for SOD1/2. We conclude that, in healthy subjects, RT can be safely performed, without adverse effects on increased LF-formation.
- PublicationMetadata onlyCoordinated alpha-crystallin B phosphorylation and desmin expression indicate adaptation and deadaptation to resistance exercise-induced loading in human skeletal muscleSkeletal muscle is a target of contraction-induced loading (CiL), leading to protein unfolding or cellular perturbations, respectively. While cytoskeletal desmin is responsible for ongoing structural stabilization, in the immediate response to CiL, alpha-crystallin B (CRYAB) is phosphorylated at serine 59 (pCRYABS59) by P38, acutely protecting the cytoskeleton. To reveal adaptation and deadaptation of these myofibrillar subsystems to CiL, we examined CRYAB, P38, and desmin regulation following resistance exercise at diverse time points of a chronic training period. Mechanosensitive JNK phosphorylation (pJNKT183/Y185) was determined to indicate the presence of mechanical components in CiL. Within 6 wk, subjects performed 13 resistance exercise bouts at the 8-12 repetition maximum, followed by 10 days detraining and a final 14th bout. Biopsies were taken at baseline and after the 1st, 3rd, 7th, 10th, 13th, and 14th bout. To assess whether potential desensitization to CiL can be mitigated, one group trained with progressive and a second with constant loading. As no group differences were found, all subjects were combined for statistics. Total and phosphorylated P38 was not regulated over the time course. pCRYABS59 and pJNKT183/Y185 strongly increased following the unaccustomed first bout. This exercise-induced pCRYABS59/pJNKT183/Y185 increase disappeared with the 10th until 13th bout. As response to the detraining period, the 14th bout led to a renewed increase in pCRYABS59. Desmin content followed pCRYABS59 inversely, i.e., was up- when pCRYABS59 was downregulated and vice versa. In conclusion, the pCRYABS59 response indicates increase and decrease in resistance to CiL, in which a reinforced desmin network could play an essential role by structurally stabilizing the cells.
- PublicationMetadata onlyPhosphorylation of αB-crystallin and its cytoskeleton association differs in skeletal myofiber types depending on resistance exercise intensity and volumeαB-crystallin (CRYAB) is an important actor in the immediate cell stabilizing response following mechanical stress in skeletal muscle. Yet, only little is known regarding myofiber type-specific stress responses of CRYAB. We investigated whether the phosphorylation of CRYAB at serine 59 (pCRYABSer59) and its cytoskeleton association are influenced by varying load-intensity and -volume in a fiber type-specific manner. Male subjects were assigned to 1, 5, and 10 sets of different acute resistance exercise protocols: hypertrophy (HYP), maximum strength (MAX), strength endurance (SE), low intensity (LI), and three sets of maximum eccentric resistance exercise (ECC). Skeletal muscle biopsies were taken at baseline and 30 min after exercise. Western blot revealed an increase in pCRYABSer59 only following 5 and 10 sets in groups HYP, MAX, SE, and LI as well as following 3 sets in the ECC group. In type I fibers, immunohistochemistry determined increased pCRYABSer59 in all groups. In type II fibers, pCRYABSer59 only increased in MAX and ECC groups, with the increase in type II fibers exceeding that of type I fibers in ECC. Association of CRYAB and pCRYABSer59 with the cytoskeleton reflected the fiber type-specific phosphorylation pattern. Phosphorylation of CRYAB and its association with the cytoskeleton in type I and II myofibers is highly specific in terms of loading intensity and volume. Most likely, this is based on specific recruitment patterns of the different myofiber entities due to the different resistance exercise loadings. We conclude that pCRYABSer59 indicates contraction-induced mechanical stress exposure of single myofibers in consequence of resistance exercise. NEW & NOTEWORTHY We determined that the phosphorylation of αB-crystallin at serine 59 (pCRYABSer59) after resistance exercise differs between myofiber types in a load- and intensity-dependent manner. The determination of pCRYABSer59 could serve as a marker indirectly indicating contractile involvement and applied mechanical stress on individual fibers. By that, it is possible to retrospectively assess the impact of resistance exercise loading on skeletal muscle fiber entities.
- PublicationMetadata onlyResistance exercise-induced muscle fatigue is not accompanied by increased phosphorylation of ryanodine receptor 1 at serine 2843
- PublicationMetadata onlyResistance exercise-induced muscle fatigue is not accompanied by increased phosphorylation of ryanodine receptor 1 at serine 2843Skeletal muscle fatigue has been shown to be associated with hyperphosphorylation of the ryanodine receptor 1 at serine 2843 (pRyR1Ser2843), due to chronic overloading exercise. We investigated whether pRyR1Ser2843, is a mechanism relevant for muscle fatigue also under acute, in contrast to chronic, muscle loading. 24 male subjects (age: 24,8±3,8; height: 182,8±7,2 cm; weight: 82,5±9,9 kg) were evenly (n = 6) assigned to the following four different resistance exercise (RE) groups: hypertrophy- (HYP), strength endurance- (SE), maximum power- (MAX) at the subjects' 10, 25 and 3 repetition maximum, respectively, and low intensity (LI) RE with 70% of the 10 repetition maximum. Each group completed three different RE volumes (1 set, 5, and 10 sets). Muscle biopsies from the vastus lateralis were taken before and after exercise, analyzed for pRyR1Ser2843 and examined for association with RE-induced muscle fatigue which was determined as reduction in maximum isometric force (isoFmax) in the quadriceps femoris muscle also before and after exercise.The degree of RE-induced muscle fatigue was specific in terms of set volume as well as of RE mode. isoFmax was not reduced in any group after one set of RE. Five sets led to a significant reduction of isoFmax in HYP and SE but not in LI and MAX (p<0,05). Ten sets of RE, as compared to five sets, exclusively induced further muscle fatigue in LI. In terms of RE mode differences, isoFmax reduction was generally higher in HYP and SE than in MAX and Li after five and ten sets of RE (p<0,05). However, pRyR1Ser2843 did not show any significant regulation, regardless of exercise condition. We conclude that despite its relevance in reducing muscle contractility in chronic overloading, pRyR1Ser2843 does not reflect the degree of muscle fatigue exerted by acute hypertrophy-, strength endurance-, maximum power and low intensity-oriented exercise.