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Biomedical subjects

C Offringa

Publications and source records attributed to C Offringa.

5 recordsLinked to original sources

Variability in fibre properties in paralysed human quadriceps muscles and effects of training.

A spinal cord injury usually leads to an increase in contractile speed and fatigability of the paralysed quadriceps muscles, which is probably due to an increased expression of fast myosin heavy chain (MHC) isoforms and reduced oxidative capacity. Sometimes, however, fatigue resistance is maintained in these muscles and also contractile speed is slower than expected. To obtain a better understanding of the diversity of these quadriceps muscles and to determine the effects of training on characteristics of paralysed muscles, fibre characteristics and whole muscle function were assessed in six subjects with spinal cord lesions before and after a 12-week period of daily low-frequency electrical stimulation. Relatively high levels of MHC type I were found in three subjects and this corresponded with a high degree of fusion in 10-Hz force responses (r=0.88). Fatigability was related to the activity of succinate dehydrogenase (SDH) (r=0.79). Furthermore, some differentiation between fibre types in terms of metabolic properties were present, with type I fibres expressing the highest levels of SDH and lowest levels of alpha-glycerophosphate dehydrogenase. After training, SDH activity increased by 76+/-26% but fibre diameter and MHC expression remained unchanged. The results indicate that expression of contractile proteins and metabolic properties seem to underlie the relatively normal functional muscle characteristics observed in some paralysed muscles. Furthermore, training-induced changes in fatigue resistance seem to arise, in part, from an improved oxidative capacity.

Adult↗

In situ rat fast skeletal muscle is more efficient at submaximal than at maximal activation levels.

The influence of stimulation frequency on efficiency (= total work output/high-energy phosphate consumption) was studied using in situ medial gastrocnemius muscle tendon complexes of the rat. The muscles performed 20 repeated concentric contractions (2/s) at 34 degrees C. During these repeated contractions, the muscle was stimulated via the severed sciatic nerve with either 60, 90, or 150 Hz. The muscle was freeze-clamped immediately after these contractions, and high-energy phosphate consumption was determined by measuring intramuscular chemical change relative to control muscles. The average values (+/-SD) of efficiency calculated for 60, 90, and 150 Hz were 18.5 +/- 1.5 (n = 7), 18.6 +/- 1.5 (n = 9), and 14.7 +/- 1.3 mJ/micromol phosphate (n = 9). The results indicate that the efficiency of the muscles that were submaximally activated (60 or 90 Hz) was higher (+26%, P < 0.05) than that of those maximally activated (150 Hz). Additional experiments showed that the low efficiency at maximal activation levels is unlikely to be the result of a higher energy turnover by the Ca2+ -ATPase relative to the total energy turnover. Therefore, alternative explanations are discussed.

Adenosine Triphosphate↗

Improved high-performance liquid chromatographic assay for the determination of "high-energy" phosphates in mammalian skeletal muscle. Application to a single-fibre study in man.

A sensitive and reproducible method for the determination of adenine nucleotides (ATP, IMP) and creatine compounds [creatine (Cr), phosphocreatine (PCr)] in freeze-dried single human muscle fibre fragments is presented. The method uses isocratic reversed-phase high-performance liquid chromatography of methanol extracts. Average retention times (min) of ATP, IMP and PCr, Cr from standard solutions were 10.6+/-0.42, 2.11+/-0.06 (n=6) and 10.5+/-0.31 and 1.19+/-0.02 (n=9), respectively. Detection limits in extracts from muscle fibre fragments were 2.0, 1.0, 3.0 and 2.0 mmol/kg dm, respectively. The assay was found successful for analysis of fibre-fragments weighing > or = 1 microg.

Adenine Nucleotides↗

[Not Available].

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Greece↗

[Not Available].

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History, Modern 1601-↗