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Biomedical subjects

R Billeter

Publications and source records attributed to R Billeter.

43 records · Page 3Linked to original sources
PubMed1982

Anaerobic muscle enzyme changes after interval training.

In contrast to endurance training, little evidence is available concerning the effects of sprint-type training programs on the anaerobic metabolism of skeletal muscle. Four male subjects completed a mean of 16 training sessions consisting of eight 200-m runs at 90% of maximal speed, which were separated by 2-min rest periods. Before and after the 5-week training period, muscle biopsies were taken out of the lateral head of m. gastrocnemius and analyzed for the activities of phosphorylase, phosphofructokinase (PFK), glyceraldehyde phosphate dehydrogenase (GAPDH), lactate dehydrogenase (LDH), succinate dehydrogenase (SDH), and malate dehydrogenase (MDH). Following training there was a significant increase in the subjects' performance time in a treadmill test at a speed of 16 km/h speed and 15% grade. Significant increases were observed in the activities of phosphorylase, PFK, GAPDH, LDH, and MDH, whereas the 17.5% increase in SDH was not statistically significant. It is concluded that interval training with high intensity and a 1:4 work-rest ratio leads to increased activities of key enzymes involved in glycogenolysis and anaerobic glycolysis of skeletal muscle.

Adult↗
PubMed1981

Analysis of myosin light and heavy chain types in single human skeletal muscle fibers.

In this study, myosin types in human skeletal muscle fibers were investigated with electrophoretic techniques. Single fibers were dissected out of lyophilized surgical biopsies and typed by staining for myofibrillar ATPase after preincubation in acid or alkaline buffers. After 14C-labelling of the fiber proteins in vitro by reductive methylation, the myosin light chain pattern was analysed on two-dimensional gels and the myosin heavy chains were investigated by one-dimensional peptide mapping. Surprisingly, human type I fibers, which contained only the slow heavy chain, were found to contain variable amounts of fast myosin light chains in addition to the two slow light chains LC1s and LC2s. The majority of the type I fibers in normal human muscle showed the pattern LC1s, LC2s and LC1f. Further evidence for the existence in human muscle of a hybrid myosin composed of a slow heavy chain with fast and slow light chains comes from the analysis of purified human myosin in the native state by pyrophosphate gel electrophoresis. With this method, a single band corresponding to slow myosin was obtained; this slow myosin had the light chain composition LC1s, LC2s and LC1f. Type IIA and IIB fibers, on the other hand, revealed identical light chain patterns consisting of only the fast light chains LC1f, LC2f and LC3f but were found to have different myosin havy chains. On the basis of the results presented, we suggest that the histochemical ATPase normally used for fibre typing is determined by the myosin heavy chain type (and not by the light chains). Thus, in normal human muscle a number of 'hybrid' myosins were found to occur, namely two extreme forms of fast myosins which have the same light chains but different heavy chains (IIA and IIB) and a continuum of slow forms consisting of the same heavy chain and slow light chains with a variable fast light chain composition. This is consistent with the different physiological roles these fibers are thought to have in muscle contraction.

Adenosine Triphosphatases↗
PubMed1980

Myosin types in human skeletal muscle fibers.

By combining enzyme histochemistry for fiber typing with immunohistochemistry for slow and fast myosin a correlation between fiber type and myosin type was sought in human skeletal muscle. Fiber typing was done by staining for myofibrillar ATPases after preincubation at discriminating pH values. Myosin types were discriminated using type specific anti-rabbit myosin antibodies shown to cross-react with human myosin and were visualized by a protein A-peroxidase method. Type I fibers were shown to contain slow myosin only, type IIA and IIB fibers fast myosin only, and type IIC fibers both myosins in various proportions. When muscle biopsies from well-trained athletes were investigated essentially the same staining pattern was observed. However, rarely occurring type I fibers with high glycolytic activity were detected containing additional small amounts of fast myosin and occasional type IIA fibers had small amounts of slow myosin. Based on the observation of various fiber types in which slow and fast myosin coexist we propose a dynamic continuum of fibers encompassing all fiber types.

Adenosine Triphosphatases↗
PubMed1980

Muscle fiber types and morphometric analysis of skeletal msucle in six-year-old children.

Needle biopsies from the vastus lateralis of 13 six-year-old Swiss children were analyzed for muscle fiber type populations and morphometrical characteristics. No significant differences existed between the males and females for fiber type distribution, maximum oxygen consumption, or any of the ultra-structural parameters investigated. The vastus lateralis muscle consisted of 19.7% fast twitch glycolytic (FG) fibers, 21.5% fast twitch oxidative glycolytic (FOG) fibers, and 5,9,% slow twitch oxidative (SO) fibers. Maximum oxygen consumption averaged 45.2 ml/kg min-1 when the subjects were considered as a single group. Morphometrically, it was found that the mean volume density of the central mitochondria was 5.54%, the mitochondrial/myofibrillar volume ratio was 6.68%, and the intracellular lipid volume was 0.46%. There was a significant correlation (r=0.69) between the mitochondrial volume density and the distribution of SO fibers as determined histochemically. It was concluded that the fiber type distribution pattern and ultrastructure of skeletal muscle in six-year-old children was not different from normal adult tissue.

Age Factors↗
PubMed1979

Fast and slow myosin within single skeletal muscle fibres of adult rabbits.

There is good evidence for the coexistence of different myosin types both in developing muscles and in Purkinje cells from adult chicken hearts. In skeletal muscle fibres of adult animals, however, coexistence of fast (FM) and slow (SM) myosin has only been demonstrated after long-term electrical stimulation. The term 'promiscuity' has recently been coined to describe the coexistence of different myosin isoenzymes within a single fibre. Using novel, refined immunological methods we demonstrate here the presence of both FM and SM within single fibres of the musculus tibialis anterior of adult rabbits. Essentially identical results were also obtained with other muscles. Our findings imply that the genes coding for FM and SM can be expressed simultaneously within the same cell throughout an animal's entire life, and not only during development or after artificial electrical stimulation.

Animals↗