title: M-band: a safeguard for sarcomere stability?
abstract: The sarcomere of striated muscle is a very efficient machine transforming chemical energy into movement. However, a wrong distribution of the generated forces may lead to self-destruction of the engine itself. A well-known example for this is eccentric contraction (elongation of the sarcomere in the activated state), which damages sarcomeric structure and leads to a reduced muscle performance. The goal of this review is to discuss the involvement of different cytoskeletal systems, in particular the M-band filaments, in the mechanisms that provide stability during sarcomeric contraction. The M-band is the transverse structure in the center of the sarcomeric A-band, which is responsible both for the regular packing of thick filaments and for the uniform distribution of the tension over the myosin filament lattice in the activated sarcomere. Although some proteins from the Ig-superfamily, like myomesin and M-protein, are the major candidates for the role of M-band bridges, the exact molecular organisation of the M-band is not clear. However, the protein composition of the M-band seems to modulate the mechanical characteristics of the thick filament lattice, in particular its stiffness, adjusting it to the specific demands in different muscle types. The special M-band design in slow fibers might be part of structural adaptations, favouring sarcomere stability for a continuous contractile activity over a broad working range. In conclusion, we discuss why the interference with M-band structure might have fatal consequences for the integrity of the working sarcomere.
authors: Institute of Cell Biology, ETH-Zurich Hoenggerberg, CH-8093 Zurich, Switzerland.
authors: Irina
authors: I
authors: Agarkova
authors: Elisabeth
authors: E
authors: Ehler
authors: Stephan
authors: S
authors: Lange
authors: Roman
authors: R
authors: Schoenauer
authors: Jean-Claude
authors: JC
authors: Perriard
mesh_terms: D000818:Animals; D064211:Connectin; D003599:Cytoskeleton / Q000502:physiology; D004548:Elasticity; D006801:Humans; D008954:Models, Biological; D009119:Muscle Contraction / Q000502:physiology; D018656:Muscle Fibers, Fast-Twitch / Q000737:chemistry / Q000502:physiology; D018657:Muscle Fibers, Slow-Twitch / Q000737:chemistry / Q000502:physiology; D009124:Muscle Proteins / Q000502:physiology*; D018482:Muscle, Skeletal / Q000502:physiology*; D009210:Myofibrils / Q000502:physiology; D020033:Protein Isoforms / Q000502:physiology; D011494:Protein Kinases / Q000502:physiology; D012518:Sarcomeres / Q000502:physiology*; D015398:Signal Transduction; D013314:Stress, Mechanical
chemical_list: D064211:Connectin; D009124:Muscle Proteins; D020033:Protein Isoforms; C577285:TTN protein, human; D011494:Protein Kinases