Are muscle fibres of body builders intrinsically weaker? A comparison with single fibres of aged‐matched controls

Author(s):  
Elena Monti ◽  
Luana Toniolo ◽  
Lorenzo Marcucci ◽  
Michela Bondì ◽  
Ivan Martellato ◽  
...  
Keyword(s):  
2005 ◽  
Vol 1 (3) ◽  
pp. 342-345 ◽  
Author(s):  
Dilson E Rassier ◽  
Eun-Jeong Lee ◽  
Walter Herzog

In this study, we investigated the effects of activation and stretch on the passive force–sarcomere length relationship in skeletal muscle. Single fibres from the lumbrical muscle of frogs were placed at varying sarcomere lengths on the descending limb of the force–sarcomere length relationship, and tetanic contractions, active stretches and passive stretches (amplitudes of ca 10% of fibre length at a speed of 40% fibre length/s) were performed. The passive forces following stretch of an activated fibre were higher than the forces measured after isometric contractions or after stretches of a passive fibre at the corresponding sarcomere length. This effect was more pronounced at increased sarcomere lengths, and the passive force–sarcomere length relationship following active stretch was shifted upwards on the force axis compared with the corresponding relationship obtained following isometric contractions or passive stretches. These results provide strong evidence for an increase in passive force that is mediated by a length-dependent combination of stretch and activation, while activation or stretch alone does not produce this effect. Based on these results and recently published findings of the effects of Ca 2+ on titin stiffness, we propose that the observed increase in passive force is caused by the molecular spring titin.


Infra-red absorption spectroscopy of muscle has already been carried out, using the Burch reflecting microscope (Barer, Cole & Thompson 1949: Barer, Thompson & Williams unpublished). There are considerable difficulties involved in this type of work. In the first place it is rather doubtful whether such measurements will ever be possible on living muscle owing to the presence of water, which possesses intense absorption bands in some of the most useful regions of the infra-red spectrum. It may be possible to overcome this difficulty to some extent by using heavy water which has a different absorption spectrum. It is in principle possible to obtain information similar to that given by infra-red spectroscopy, even in the presence of water, by means of Raman spectroscopy, but the technical difficulties involved, particularly fight scattering by colloids, would seem to preclude this method of attack so far as muscle is concerned. Our infra-red measurements have hitherto been confined to dried material. The results indicate that there is little prospect of working with whole muscles, as even single isolated striated fibres of the frog, rabbit and crab were usually too thick. However, it was possible to obtain good spectra in the chemically important region from 3 to 14/ µ on exceptionally thin single fibres or on artificially compressed fibres. An attempt was made to detect dichroism by means of polarized infra-red radiation, but to our surprise none was observed throughout the 3 to 14 µ range, even though the material used showed strong birefringence in the visible region. Hr Stocken and I have recently examined certain molecular models of muscle, in the fight of the work of Ambrose, Elliott & Temple (1949) on myosin, and it now appears possible that infra-red dichroism of muscle might be expected to manifest itself only under rather special conditions. We hope to put these theoretical deductions to experimental test. As regards measurements on muscle in the ultra-violet region, the position is much more promising. It is quite possible to determine the absorption spectrum of the A or I band in living single fibres. The entire spectrum from about 230 m µ in the ultra-violet to over 600 m µ , in the visible can be recorded simultaneously, using the reflecting microscope. This technique can also be used with polarized ultra-violet fight, in order to detect variation of dichroism in crystals at different wave-lengths (Barer, Jope & Perutz unpublished), and I intend to apply it to the study of dichroism in muscle fibres. Another new possibility is the observation of birefringence, as well as dichroism, in the ultra-violet. I have recently carried out experiments with a view to developing a new type of ultra-violet polarizer and it should now be possible to use the reflecting microscope as an ultra-violet polarizing microscope.


1999 ◽  
Vol 97 (4) ◽  
pp. 449-455 ◽  
Author(s):  
Hans DEGENS ◽  
Mattias SOOP ◽  
Peter HÖÖK ◽  
Olle LJUNGQVIST ◽  
Lars LARSSON

Surgery and accidental trauma are associated with a transient period of insulin resistance, substrate catabolism and muscle weakness. In the present study, we evaluated the changes in the force-generating capacity of chemically skinned single muscle fibres following abdominal surgery. Biopsies of the m. vastus lateralis were obtained in three patients 1 day before and 3 or 6 days after surgery. Part of the biopsy was frozen for histochemical analysis of the fibre cross-sectional area (FCSA) and myofibrillar protein content, and another part was used for single-fibre contractile measurements. All patients developed insulin resistance following surgery. The maximum velocity of unloaded shortening of single muscle fibres did not change following surgery. The FCSA did not decrease after surgery, as determined either from histochemical sections or from single fibres measured at a fixed sarcomere length of 2.76±0.09 μm (mean±S.D.). Further, the force-generating capacity of the single fibres, measured as maximal Ca2+-activated force (P0) or as P0 normalized to FCSA (specific tension), remained unchanged, as did the myofibrillar protein content of the muscle. In conclusion, the muscle weakness associated with post-operative insulin resistance is not related to a decreased specific tension or a loss of myofibrillar proteins. Other potential cellular mechanisms underlying post-operative weakness are discussed.


1980 ◽  
Vol 209 (1177) ◽  
pp. 563-568 ◽  

Satellite cells were visualized in living muscle fibres of the frog. Single fibres or bundles consisting of a few fibres were isolated after treatment with collagenase, and viewed under the light microscope. Subsequent electron microscopy of identified cells confirmed that they were satellite muscle cells. Under the light microscope, satellite cells appear as fusiform cells, tapering into long fine processes usually orientated parallel to the muscle fibre axis. Horseradish peroxidase injected into the muscle fibre was not transferred to the satellite cells.


1988 ◽  
Vol 250 (1) ◽  
pp. 307-308 ◽  
Author(s):  
D Biral ◽  
R Betto ◽  
D Danieli-Betto ◽  
G Salviati

Electrophoretic analysis in the presence of 33% glycerol of purified myosin from normal human muscle shows three distinct protein bands which are identified as type 1, 2B, and 2A myosin heavy chain (MHC) isoforms by affinity-purified polyclonal antibodies. Analysis of MHC of single human muscle fibres shows that human muscles contain a large population of fibres showing the coexistence of type 2A and 2B MHC.


2018 ◽  
Vol 1 (5) ◽  
Author(s):  
Sebastian Edman ◽  
Karin Söderlund ◽  
Eva Blomstrand

Objective Human muscle consists of a mixture of fibres with different contractile and metabolic properties, type I (slow-twitch) and type II (fast-twitch) fibres. Little is known about the effect of anabolic stimuli, in particular nutrition, on the molecular response in the different fibre types. Here, we examine the effect of resistance exercise and essential amino acid (EAA) supplementation on mTOR signalling in individual type I and type II human muscle fibres. Methods Five strength-trained male subjects performed two sessions of leg press exercise (10 x 10 repetition at 62-85 % of 1RM). During exercise and recovery, the subjects ingested an aqueous solution with EAA (290 mg/kg) or flavoured water (placebo). Muscle biopsies were taken from the vastus lateralis before and 90 min after exercise. The biopsies were freeze-dried and single fibres dissected out and weighed (range 0.9 – 8 ug). The fibres were individually homogenized and analysed for proteins in the mTOR pathway using Western blot. Membranes were repeatedly stripped and fibres were identified as type I or type II following incubation with antibodies against the different myosin isoforms. Results Exercise led to a significant increase in mTOR and p70S6k1 phosphorylation and a fall in eEF2 phosphorylation, similar in both fibre types. There was a large variation between individual fibres; some fibres were highly activated whereas others were not activated at all despite the heavy exercise performed. Intake of EAA caused a 2- to 6-fold higher increase in mTOR and p70S6k1 phosphorylation in both type I and type II fibres as compared to intake of placebo, with no difference between the fibre types. The phosphorylation of eEF2 was not affected by intake of EAA. The total expression of p70S6k1 and eEF2 was 145% and 155% higher in type II than in type I fibres (P<0.05), respectively, whereas no difference between the fibre types was observed for mTOR protein. Conclusions The response to heavy resistance exercise regarding mTOR signalling was similar in type I and type II fibres in trained subjects, but with a large variation between single fibres of both types. Furthermore, ingestion of EAA enhanced the effect of resistance exercise on phosphorylation of mTOR and p70S6k1 in both fibre types.  


1982 ◽  
Vol 203 (1) ◽  
pp. 179-184 ◽  
Author(s):  
O A Young

Young & Davey (1981) (Biochem. J. 195, 317-327) identified numbers of polymorphs of myofibrillar proteins by sodium dodecyl sulphate/polyacrylamide gel electrophoresis of single muscle fibres isolated from three bovine muscles. Fibres were classed according to the distribution of polymorphs. The study has now been extended to eight diverse bovine muscles. The previous distinction made between fast and slow fibres is valid without exception in the extended study. Within these classes, variations in myofibrillar expression are examined within and between fibres, muscles and animals. Two slow muscles are contrasted; masseter is homogeneous in fibre type, whereas diaphragm is subtly heterogeneous, possibly arising from greater physiological demands. Of the myofibrillar polymorphs, attention is concentrated on two variants of fast-muscle myosin heavy chain. Both are present in all fast and mixed muscles examined, except sternomandibularis, and each is respectively associated with certain unidentified proteins. Within a muscle the fast-muscle myosin light-chain expression is the same irrespective of the heavy-chain variant. Histochemical techniques demonstrated that the variants are respectively associated with types IIA and IIB as defined by other investigators.


1982 ◽  
Vol 207 (2) ◽  
pp. 261-272 ◽  
Author(s):  
G Salviati ◽  
R Betto ◽  
D Danieli Betto

Rabbit predominantly fast-twitch-fibre and predominantly slow-twitch-fibre skeletal muscles of the hind limbs, the psoas, the diaphragm and the masseter muscles were fibre-typed by one-dimensional polyacrylamide-gel electrophoresis of the myofibrillar proteins of chemically skinned single fibres. Investigation of the distribution of fast-twitch-fibre and slow-twitch-fibre isoforms of myosin light chains and the type of myosin heavy chains, based on peptide ‘maps’ published in Cleveland. Fischer, Kirschner & Laemmli [(1977) J. Biol. Chem. 252, 1102-1106], allowed a classification of muscle fibres into four classes, corresponding to histochemical types I, IIA, IIB and IIC. Type I fibres with a pure slow-twitch-type of myosin were found to be characterized by a unique set of isoforms of troponins I, C and T, in agreement with the immunological data of Dhoot & Perry [(1979) Nature (London) 278, 714-718], by predominance of the beta-tropomyosin subunit and by the presence of a small amount of an additional tropomyosin subunit, apparently dissimilar from fast-twitch-fibre alpha-tropomyosin subunit. The myofibrillar composition of type IIB fast-twitch white fibres was the mirror image of that found for slow-twitch fibres in that the fast-twitch-fibre isoforms only of the troponin subunits were present and the alpha-tropomyosin subunit predominated. Type IIA fast-twitch red fibres showed a troponin subunit composition identical with that of type IIB fast-twitch white fibres. On the other hand, a unique type of myosin heavy chains was found to be associated with type IIA fibres. Furthermore, the myosin light-chain composition of these fibres was invariably characterized by a small amount of LC3F light chain and by a pattern that was either a pure fast-twitch-fibre light-chain pattern or a hybrid LC1F/LC2F/LC3F/LC1Sb light-chain pattern. By these criteria type IIA fibres could be distinguished from type IIC intermediate fibres, which showed coexistence of fast-twitch-fibre and slow-twitch-fibre forms of myosin light chains and of troponin subunits.


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