A review of the injuries caused by occupational footwear.

BACKGROUND: Occupational footwear is intended to provide protection against the risks associated with work activities. The choice of footwear is complex due to the welfare, health and safety conditions of workers. AIMS: To identify the injuries and problems caused by occupational footwear through a systematic review of the existing literature. METHODS: A literature search was carried out in the Cumulative Index to Nursing and Allied Health Literature, Dialnet Plus, Pubmed, Scientific Electronic Library Online, Medline, Scopus and Web of Science databases over the period 2000-23, following the PRISMA Declaration guidelines. RESULTS: A total of 27 studies were included in the review. The results indicated that there is a wide variety of injuries caused by occupational footwear: from dermal injuries (e.g. calluses) and injuries to the nail apparatus to inflammatory pathologies such as plantar fasciitis or bursitis. In addition, inappropriate footwear can cause pain in the ankle and foot, knees, hips and lower back. Other results include the discomfort derived from the footwear itself. CONCLUSIONS: Inappropriate footwear can cause injuries to the foot and other related bone structures. Further studies are needed on the detection of foot injuries caused by occupational footwear and the levels of action at this level to improve the worker's health, the adaptability of the footwear to the wearer, and the worker's comfort and adherence to the footwear.

Muscle enzyme and fiber type-specific sarcomere protein increases in serum after inertial concentric-eccentric exercise.

Muscle damage induced by inertial exercise performed on a flywheel device was assessed through the serum evolution of muscle enzymes, interleukin 6, and fiber type-specific sarcomere proteins such as fast myosin (FM) and slow myosin (SM). We hypothesized that a model of muscle damage could be constructed by measuring the evolution of serum concentration of muscle proteins following inertial exercise, according to their molecular weight and the fiber compartment in which they are located. Moreover, by measuring FM and SM, the type of fibers that are affected could be assessed. Serum profiles were registered before and 24, 48, and 144 h after exercise in 10 healthy and recreationally active young men. Creatine kinase (CK) and CK-myocardial band isoenzyme increased in serum early (24 h) and returned to baseline values after 48 h. FM increased in serum late (48 h) and remained elevated 144 h post-exercise. The increase in serum muscle enzymes suggests increased membrane permeability of both fast and slow fibers, and the increase in FM reveals sarcomere disruption as well as increased membrane permeability of fast fibers. Consequently, FM could be adopted as a fiber type-specific biomarker of muscle damage.

Effect of the nucleotides CMP and UMP on exhaustion in exercise rats.

The aetiology of muscle fatigue has yet not been clearly established. Administration of two nucleotides, cytosine monophosphate (CMP) and uridine monophosphate (UMP), has been prescribed for the treatment of neuromuscular affections in humans. Patients treated with CMP/UMP recover from altered neurological functions and experience pain relief, thus the interest to investigate the possible effect of the drug on exhausting exercise. With such aim, we have determined, in exercised rats treated with CMP/UMP, exercise endurance, levels of lactate, glucose and glycogen, and the activity of several metabolic enzymes such as, creatine kinase (CK), lactate dehydrogenase (LDH), and aspartate aminotransferase (AST). Our results show that rats treated with CMP/UMP are able to endure longer periods of exercise (treadmill-run). Before exercise, muscle glucose level is significantly higher in treated rats, suggesting that the administration of CMP/UMP favours the entry of glucose in the muscle. Liver glycogen levels remains unaltered during exercise, suggesting that CMP/UMP may be implicated in maintaining the level of hepatic glycogen constant during exercise. Lactate dehydrogenase and aspartate aminotransferase activity is significantly lower in the liver of treated rats. These results suggest that administration of CMP/UMP enable rats to endure exercise by altering some metabolic parameters.

Effect of the nucleotides CMP and UMP on exhaustion in exercise rats

The aetiology of muscle fatigue has yet not been clearly established. Administrationof two nucleotides, cytosine monophosphate (CMP) and uridine monophosphate(UMP), has been prescribed for the treatment of neuromuscular affections inhumans. Patients treated with CMP/UMP recover from altered neurological functionsand experience pain relief, thus the interest to investigate the possible effect ofthe drug on exhausting exercise. With such aim, we have determined, in exercised ratstreated with CMP/UMP, exercise endurance, levels of lactate, glucose and glycogen,and the activity of several metabolic enzymes such as, creatine kinase (CK), lactatedehydrogenase (LDH), and aspartate aminotransferase (AST). Our results show thatrats treated with CMP/UMP are able to endure longer periods of exercise (treadmillrun).Before exercise, muscle glucose level is significantly higher in treated rats, suggestingthat the administration of CMP/UMP favours the entry of glucose in themuscle. Liver glycogen levels remains unaltered during exercise, suggesting thatCMP/UMP may be implicated in maintaining the level of hepatic glycogen constantduring exercise. Lactate dehydrogenase and aspartate aminotransferase activity is significantlylower in the liver of treated rats. These results suggest that administrationof CMP/UMP enable rats to endure exercise by altering some metabolic parameters (AU)

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The changes in the energy metabolism of human muscle induced by training.

The biochemical effects of training programmes have been studied with a kinetic model of central metabolism, using enzyme activities and metabolite concentrations measured at rest and after 30 s maximum-intensity exercise, collected before and after long and short periods of training, which differed only by the duration of the rest intervals. After short periods of training the glycolytic flux at rest was three times higher than it had been before training, whereas during exercise the flux and energy consumption remained the same as before training. Long periods of training had less effect on the glycolytic flux at rest, but increased it in response to exercise, increasing the contribution of oxidative phosphorylation.

Fast and slow myosins as markers of muscle injury.

OBJECTIVE: The diagnosis of muscular lesions suffered by athletes is usually made by clinical criteria combined with imaging of the lesion (ultrasonography and/or magnetic resonance) and blood tests to detect the presence of non-specific muscle markers. This study was undertaken to evaluate injury to fast and slow-twitch fibres using specific muscle markers for these fibres. METHODS: Blood samples were obtained from 51 non-sports people and 38 sportsmen with skeletal muscle injury. Western blood analysis was performed to determine fast and slow myosin and creatine kinase (CK) levels. Skeletal muscle damage was diagnosed by physical examination, ultrasonography and magnetic resonance and biochemical markers. RESULTS: The imaging tests were found to be excellent for detecting and confirming grade II and III lesions. However, grade I lesions were often unconfirmed by these techniques. Grade I lesions have higher levels of fast myosin than slow myosin with a very small increase in CK levels. Grade II and III lesions have high values of both fast and slow myosin. CONCLUSIONS: The evaluation of fast and slow myosin in the blood 48 h after the lesion occurs is a useful aid for the detection of type I lesions in particular, since fast myosin is an exclusive skeletal muscle marker. The correct diagnosis of grade I lesions can prevent progression of the injury in athletes undergoing continual training sessions and competitions, thus aiding sports physicians in their decision making.

Disturbances of the sarcoplasmic reticulum and transverse tubular system in 24-h electrostimulated fast-twitch skeletal muscle.

Chronic low-frequency stimulation of rabbit tibialis anterior muscle over a 24-h period induces a conspicuous loss of isometric tension that is unrelated to muscle energy metabolism (J.A. Cadefau, J. Parra, R. Cusso, G. Heine, D. Pette, Responses of fatigable and fatigue-resistant fibres of rabbit muscle to low-frequency stimulation, Pflugers Arch. 424 (1993) 529-537). To assess the involvement of sarcoplasmic reticulum and transverse tubular system in this force impairment, we isolated microsomal fractions from stimulated and control (contralateral, unstimulated) muscles on discontinuous sucrose gradients (27-32-34-38-45%, wt/wt). All the fractions were characterized in terms of calcium content, Ca2+/Mg2+-ATPase activity, and radioligand binding of [3H]-PN 200-110 and [3H]ryanodine, specific to dihydropyridine-sensitive calcium channels and ryanodine receptors, respectively. Gradient fractions of muscles stimulated for 24 h underwent acute changes in the pattern of protein bands. First, light fractions from longitudinal sarcoplasmic reticulum, enriched in Ca2+-ATPase activity, R1 and R2, were greatly reduced (67% and 51%, respectively); this reduction was reflected in protein yield of crude microsomal fractions prior to gradient loading (25%). Second, heavy fractions from the sarcoplasmic reticulum were modified, and part (52%) of the R3 fraction was shifted to the R4 fraction, which appeared as a thick, clotted band. Quantification of [3H]-PN 200-110 and [3H]-ryanodine binding revealed co-migration of terminal cisternae and t-tubules from R3 to R4, indicating the presence of triads. This density change may be associated with calcium overload of the sarcoplasmic reticulum, since total calcium rose three- to fourfold in stimulated muscle homogenates. These changes correlate well with ultrastructural damage to longitudinal sarcoplasmic reticulum and swelling of t-tubules revealed by electron microscopy. The ultrastructural changes observed here reflect exercise-induced damage of membrane systems that might severely compromise muscle function. Since this process is reversible, we suggest that it may be part of a physiological response to fatigue.

Differences between glycogen biogenesis in fast- and slow-twitch rabbit muscle.

Skeletal muscle glycogen is an essential energy substrate for muscular activity. The biochemical properties of the enzymes involved in de novo synthesis of glycogen were analysed in two types of rabbit skeletal muscle fiber (fast- and slow-twitch). Glycogen concentration was higher in fast-twitch muscle than in slow-twitch muscle, but the latter contained many more small intermediate-acceptor molecules that could act as glycogen synthase substrates. The enzymes involved in de novo synthesis of glycogen in fast-twitch muscle were strongly stimulated by Glc-6-P, but those in slow-twitch muscle were not.

Glycogen depletion and resynthesis during 14 days of chronic low-frequency stimulation of rabbit muscle.

Electro-stimulation alters muscle metabolism and the extent of this change depends on application intensity and duration. The effect of 14 days of chronic electro-stimulation on glycogen turnover and on the regulation of glycogen synthase in fast-twitch muscle was studied. The results showed that macro- and proglycogen degrade simultaneously during the first hour of stimulation. After 3 h, the muscle showed net synthesis, with an increase in the proglycogen fraction. The glycogen content peaked after 4 days of stimulation, macroglycogen being the predominant fraction at that time. Glycogen synthase was determined during electro-stimulation. The activity of this enzyme was measured at low UDPG concentration with either high or low Glu-6-P content. Western blots were performed against glycogen synthase over a range of stimulation periods. Activation of this enzyme was maximum before the net synthesis of glycogen, partial during net synthesis, and low during late synthesis. These observations suggest that the more active, dephosphorylated and very low phosphorylated forms of glycogen synthase may participate in the first steps of glycogen resynthesis before net synthesis is observed, while partially phosphorylated forms are most active during glycogen elongation.

Changes of skeletal muscle proteases activities during a chronic low-frequency stimulation period.

Modifications of muscular contractile patterns by chronic low-frequency stimulation induce structural, physiological, and biochemical transformations in fast-twitch fibers that cause them to act like slow-twitch muscle. During this transformation many changes in protein pattern appear and the proteolytic system may be involved in those changes. The activities of cathepsin L, B, H, D, the level of cystatin, as well as the calpain activity in rabbit fast-twitch muscle have been compared with those of slow-twitch muscle. The results show that fast-twitch muscle has lower cathepsin activities and higher calpain activities than slow-twitch muscle. Chronic low-frequency stimulation was applied for 24 days to fast-twitch muscles and changes in proteases and protease inhibitors (cystatin and calpastatin) were studied. After 7-14 days of stimulation, lysosomal cathepsin L, B, and D and cytoplasm calpain and proteosome activities increased several-fold. Involvement of the phagocyte cells in the protein fiber turnover was minimal. Although the turnover of contractile proteins during muscle electrostimulation takes place in synchrony with changes in the muscle proteolytic system, the stimulation period used did not attain the total transformation from fast- to slow-twitch muscle proteolytic pattern.

A short training programme for the rapid improvement of both aerobic and anaerobic metabolism.

The aim of this study was to evaluate the changes in aerobic and anaerobic metabolism produced by a newly devised short training programme. Five young male volunteers trained daily for 2 weeks on a cycle ergometer. Sessions consisted of 15-s all-out repetitions with 45-s rest periods, plus 30-s all-out repetitions with 12-min rest periods. The number of repetitions was gradually increased up to a maximum of seven. Biopsy samples of the vastus lateralis muscle were taken before and after training. Performance changes were evaluated by two tests, a 30-s all-out test and a maximal progressive test. Significant increases in phosphocreatine (31%) and glycogen (32%) were found at the end of training. In addition, a significant increase was observed in the muscle activity of creatine kinase (44%), phosphofructokinase (106%), lactate dehydrogenase (45%), 3-hydroxy-acyl-CoA dehydrogenase (60%) and citrate synthase (38%). After training, performance of the 30-s all-out test did not increase significantly, while in the maximal progressive test, the maximum oxygen consumption increased from mean (SD) 57.3 (2.6) ml x min(-1) x kg(-1) to 63.8 (3.0) ml min(-1) x kg(-1), and the maximum load from 300 (11) W to 330 (21) W; all changes were significant. In conclusion, this new protocol, which utilises short durations, high loads and long recovery periods, seems to be an effective programme for improving the enzymatic activities of the energetic pathways in a short period of time.

Ethanol inhibits skeletal muscle cell proliferation and delays its differentiation in cell culture.

Chronic ingestion of ethanol (EtOH) produces physiological and morphological alterations in skeletal muscle. The effects of EtOH on skeletal muscle have been studied in experimental animals or on biopsies from alcoholic patients. However, alterations in skeletal muscle from alcoholic patients could be secondary to the effects of EtOH on the nervous system. In this study, by assaying the action of EtOH on primary skeletal muscle cell cultures, we provide evidence of its direct effect on skeletal muscle proliferation and differentiation. The results indicate that EtOH: (1) significantly inhibits skeletal muscle cell proliferation at the beginning of the proliferation phase; (2) delays skeletal muscle differentiation, shown by the significant changes in the evolution of the percentage of the creatine kinase isozymes; (3) has no significant effect on skeletal muscle DNA or protein content during the proliferation phase.

The distribution of rest periods affects performance and adaptations of energy metabolism induced by high-intensity training in human muscle.

The effect of the distribution of rest periods on the efficacy of interval sprint training is analysed. Ten male subjects, divided at random into two groups, performed distinct incremental sprint training protocols, in which the muscle load was the same (14 sessions), but the distribution of rest periods was varied. The 'short programme' group (SP) trained every day for 2 weeks, while the 'long programme' group (LP) trained over a 6-week period with a 2-day rest period following each training session. The volunteers performed a 30-s supramaximal cycling test on a cycle ergometer before and after training. Muscle biopsies were obtained from the vastus lateralis before and after each test to examine metabolites and enzyme activities. Both training programmes led to a marked increase (all significant, P < 0.05) in enzymatic activities related to glycolysis (phosphofructokinase - SP 107%, LP 68% and aldolase - SP 46%, LP 28%) and aerobic metabolism (citrate synthase - SP 38%, LP 28.4% and 3-hydroxyacyl-CoA dehydrogenase - SP 60%, LP 38.7%). However, the activity of creatine kinase (44%), pyruvate kinase (35%) and lactate dehydrogenase (45%) rose significantly (P < 0.05) only in SP. At the end of the training programme, SP had suffered a significant decrease in anaerobic ATP consumption per gram muscle (P < 0.05) and glycogen degradation (P < 0.05) during the post-training test, and failed to improve performance. In contrast, LP showed a marked improvement in performance (P < 0.05) although without a significant increase in anaerobic ATP consumption, glycolysis or glycogenolysis rate. These results indicate that high-intensity cycling training in 14 sessions improves enzyme activities of anaerobic and aerobic metabolism. These changes are affected by the distribution of rest periods, hence shorter rest periods produce larger increase in pyruvate kinase, creatine kinase and lactate dehydrogenase. However, performance did not improve in a short training programme that did not include days for recovery, which suggests that muscle fibres suffer fatigue or injury.

GLUT1 glucose transporter gene transcription is repressed by Sp3. Evidence for a regulatory role of Sp3 during myogenesis.

GLUT1 glucose transporters are highly expressed in proliferating and transformed cells as well as in tissues during fetal life. However, the mechanisms that regulate GLUT1 gene expression remain largely unknown. Here, we demonstrate that Sp3 proteins bind to the GLUT1 proximal promoter gene and inhibit transcriptional activity in muscle and non-muscle cells. Two different Sp3 translational products (110 and 74 kDa) derived from differential translational initiation were detected in nuclear extracts from myoblast cells, and both Sp3 protein species inhibited GLUT1 gene transcriptional activity. The inhibitory effect of Sp3 was dominant over the stimulatory effect of Sp1 on transcriptional activity of GLUT1 gene. Furthermore, abolition of Sp3 binding to the proximal promoter of GLUT1 gene completely blocked the response to Sp3. We provide evidence that the expression of Sp3 protein is subject to regulation in muscle cells and that this is likely to control GLUT1. Thus, Sp3 protein was up-regulated in the absence of changes in Sp1 early after the induction of IGF-II-dependent myogenesis. Furthermore, forced over-expression of MyoD caused an enhancement in the cellular Sp3/Sp1 ratio which was concomitant to a reduced GLUT1 expression. Later during myogenesis, Sp3 expression was substantial whereas Sp1 was markedly down-regulated. In summary, we provide direct evidence that the transcription factor Sp3 represses gene expression in non-muscle and muscle cells and this is likely to operate in fetal heart by binding to the GLUT1 gene promoter. This is the first description of a repressor of GLUT1 gene transcription. Furthermore, we propose that variations in the ratio of Sp3 versus Sp1 regulate GLUT1 promoter activity and this is crucial in the down-regulation of GLUT1 associated to myogenesis.

Contractile activity modifies Fru-2,6-P(2) metabolism in rabbit fast twitch skeletal muscle.

Modification of muscular contractile patterns by denervation and chronic low frequency stimulation induces structural, physiological, and biochemical alterations in fast twitch skeletal muscles. Fructose 2,6-bisphosphate is a potent activator of 6-phosphofructo-1-kinase, a key regulatory enzyme of glycolysis in animal tissues. The concentration of Fru-2,6-P(2) depends on the activity of the bifunctional enzyme, 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase (PFK-2/FBPase-2), which catalyzes the synthesis and degradation of this metabolite. This enzyme has several isoforms, the relative abundance of which depends on the tissue metabolic properties. Skeletal muscle expresses two of these isoforms; it mainly contains the muscle isozyme (M-type) and a small amount of the liver isozyme (L-type), whose expression is under hormonal control. Moreover, contractile activity regulates expression of muscular proteins related with glucose metabolism. Fast twitch rabbit skeletal muscle denervation or chronic low frequency stimulation can provide information about the regulation of this enzyme. Our results show an increase in Fru-2,6-P(2) concentration after 2 days of denervation or stimulation. In denervated muscle, this increase is mediated by a rise in liver PFK-2/FBPase-2 isozyme, while in stimulated muscle it is mediated by a rise in muscle PFK-2/FBPase-2 isozyme. In conclusion, our results show that contractile activity could alter the expression of PFK-2/FBPase-2.

Effect of chronic electrostimulation of rabbit skeletal muscle on calmodulin level and protein kinase activity.

(a) Chronic electrostimulation of fast-twitch skeletal muscles makes them resemble slow-twitch muscles. The involvement of second-messenger cascades in this muscle reprogramming is not well understood. The goal of this study was to examine protein kinase activities and calmodulin levels as a function of the duration of electrostimulation. (b) Fast-twitch rabbit muscle was subjected to continuous low-frequency electrostimulation for 2 weeks. The extensor digitorum longus was taken and examined for calmodulin concentration and cAMP-dependent (PKA). Ca(2+)-phospholipid-dependent (PKC) and Ca(2+)-calmodulin-dependent (CaM kinase or PKB) protein kinase activities. (c) Electrostimulation for 14 days led to a significant increase in total calmodulin level and PKB activity, both rising in the cytosolic fraction. Protein kinase C translocated to the membrane fraction, although total activity did not change. (d) These changes could be related with electrostimulation-induced changes in excitation-contraction coupling.

Effect of summer intermission on skeletal muscle of adolescent soccer players.

BACKGROUND: To study the effect of some weeks of rest on three groups of adolescent soccer players, who had undergone systematic training for eleven months. EXPERIMENTAL DESIGN: Retrospective and comparative investigation; duration 4-8 weeks. SETTING: young amateur players from a Spanish football club were examined at the beginning and at the end of the summer rest period. PARTICIPANTS: 37 young soccer players aged 14, 15 and 16 years old. They were members of three football teams. INTERVENTIONS: during the rest period they were free from any training program. MEASURES: biopsies of M. vastus lateralis were taken immediately after training and after the summer holidays. The type, percentage and diameter of the fibers, as well as the enzymes of glycogen metabolism (glycogen synthase and glycogen phosphorylase), glycolysis (phosphofructokinase and lactate dehydrogenase), oxidative metabolism (succinate dehydrogenase and citrate synthase) and creatine kinase and transaminase (aspartate and alanine aminotransferase) were studied. RESULTS: Detraining had an adaptation effect, decreasing the cross-sectional area of type I and type II fibers, and decreasing the activities of creatine kinase, citrate synthase, phosphofructokinase, lactate dehydrogenase and aspartate aminotransferase. CONCLUSIONS: The results can help trainers to plan the length of the rest period between training.

Enhanced catalytic activity of hexokinase by work-induced mitochondrial binding in fast-twitch muscle of rat.

Using a teased muscle fiber preparation, we determined the activity of mitochondrially bound hexokinase in rat fast-twitch muscle under control conditions and after low-frequency stimulation periods for up to 2 h. As compared to soluble hexokinase, mitochondrial binding led to stimulation of glucose 6-phosphate production. Low-frequency stimulation greatly enhanced glucose 6-phosphate formation which was 100% and 250% elevated after 1 and 2 h, respectively. These observations point to a mechanism which rapidly increases the catalytic activity of hexokinase through binding to the mitochondrial surface.

Myofibril-bound muscle phosphofructokinase is less sensitive to inhibition by ATP than the free enzyme, but retains its sensitivity to stimulation by bisphosphorylated hexoses.

Phosphofructokinase activity is modulated by allosteric effectors and macromolecular interactions (e.g. binding to myofibrillar components). The aim of this study was to determine the effects of ATP and bisphosphorylated sugars upon phosphofructokinase in the presence of myofibrils. Myofibrils were prepared from resting and electrically stimulated rat muscle. Dephosphorylation of myofibrils was performed with alkaline phosphatase acid. Purified rabbit skeletal muscle phosphofructokinase was used for all experiments. Myofibrils from resting muscle showed a higher capacity to bind phosphofructokinase and a lower phosphate content than myofibrils from stimulated muscle. Dephosphorylation of myofibrils did not increase their binding capacity. Myofibrils greatly counteracted the inhibition of phosphofructokinase by high concentrations of ATP, without affecting maximum activity. In the presence of myofibrils, both glucose 1,6-bisphosphate and fructose 2,6-bisphosphate additionally activated muscle phosphofructokinase. We suggest that the binding of phosphofructokinase to myofibrils in combination with increasing glucose 1,6-bisphosphate concentration could be important in the enhancement of the glycolytic flux that takes place during muscle contraction.

Effect of chronic alcoholism on human muscle glycogen and glucose metabolism.

To determine the effect of alcohol on carbohydrate metabolism, 48 human muscle biopsies from chronic alcoholics were studied. The level of glycogen and the activities of the enzymes catalyzing glycogen and glucose metabolism were analyzed. Chronic alcohol intake produced an increase in glycogen concentration and a decrease in pyruvate kinase activity before the first signs of myopathy appeared. When myopathy was present, glycogen decreased. These changes may contribute to the decline in skeletal muscle performance in these patients.