Functional investigations of exercising muscle: a noninvasive magnetic resonance spectroscopy-magnetic resonance imaging approach

Muscle fatigue, which is defined as the decline in muscle performance during exercise, may occur at different sites along the pathway from the central nervous system through to the intramuscular contractile machinery. Historically, both impairment of neuromuscular transmission and peripheral alterations within the muscle have been proposed as causative factors of fatigue development. However, according to more recent studies, muscle energetics play a key role in this process. Intramyoplasmic accumulation of inorganic phosphate (P_i) and limitation in ATP availability have been frequently evoked as the main mechanisms leading to fatigue. Although attractive, these hypotheses have been elaborated on the basis of experimental results obtained in vitro, and their physiological relevance has never been clearly demonstrated in vivo. In that context, noninvasive methods such as 31-phosphorus magnetic resonance spectroscopy and surface electromyography have been employed to understand both metabolic and electrical aspects of muscle fatigue under physiological conditions. Mapping of muscles activated during exercise is another interesting issue which can be addressed using magnetic resonance imaging (MRI). Exercise-induced T2 changes have been used in order to locate activated muscles and also as a quantitative index of exercise intensity. The main results related to both issues, i.e. the metabolic and electrical aspects of fatigue and the MRI functional investigation of exercising muscle, are discussed in the present review.Received 4 September 2003; received after revision 4 December 2003; accepted 22 December 2003     

Level of polysomes in cells of Escherichia coli treated with sublethal doses of aminoglycosides

Polysome level was measured in Escherichia coli cells grown in the presence of sublethal doses of four different aminoglycosides which all induce mistranslation: streptomycin, neomycin, kanamycin and gentamycin. No significant variation was noticed as referred to the level of polysomes in normally growing cells. This observation indicates that the erroneous incorporation of amino acids into polypeptide chains does not necessarily result in the release of ribosomes from messenger RNA molecules.     

Protein kinase activity in Escherichia coli]

When growing E. coli in a minimal medium, at least four proteins from the soluble fraction and one ribosome-associated protein are found phosphorylated at the level of their threonine and serine residues.