title: M-band structure, M-bridge interactions and contraction speed in vertebrate cardiac muscles.
abstract: Cardiac muscle M-band structures in several mammals (guinea pig, rabbit, rat and cow) and also from three teleosts (plaice, carp and roach), have been studied using electron microscopy and image processing. Axial structure seen in negatively stained isolated myofibrils or negatively stained cryo-sections shows the presence of five strong M-bridge lines (M6, M4, M1, M4' and M6') except in the case of the teleost M-bands in which the central M-line (M1) is absent, giving a four-line M-band. The M4 (M4') lines are consistently strong in all muscles, supporting the suggestion that bridges at this position are important for the structural integrity of the A-band myosin filament lattice. Across the vertebrate kingdom, cardiac M-band ultrastructure appears to correlate roughly with heartbeat frequency, just as in skeletal muscles it correlates with contraction speed, reinforcing the suggestion that some M-band components may have a significant physiological role. Apart from rat heart, which is relatively fast and has a conventional five-line M-band with M1 and M4 approximately equal, the rabbit, guinea pig and beef heart M-bands from a new 1 + 4 class; M1 is relatively very much stronger than M4. Transverse sections of the teleost (roach) cardiac A-band show a simple lattice arrangement of myosin filaments, just as teleost skeletal muscles. Almost all other vertebrate striated muscles, including mammalian heart muscles, have a statistical superlattice structure. The high degree of filament lattice order in teleost cardiac muscles indicates their potential usefulness for ultrastructural studies. It is shown that, in four-line M-bands in which the central (M1) M-bridges are missing, interactions at M4 (M4') are sufficient to define the different myosin filament orientations in simple lattice and superlattice A-bands. However the presence of M1 bridges may improve the axial order of the A-band.
authors.affiliation: Biophysics Section, Blackett Laboratory, Imperial College, London, UK.
authors.forename: H T
authors.initials: HT
authors.lastname: Pask
authors.forename: K L
authors.initials: KL
authors.lastname: Jones
authors.forename: P K
authors.initials: PK
authors.lastname: Luther
authors.forename: J M
authors.initials: JM
authors.lastname: Squire
mesh_terms: D008841:Actin Cytoskeleton / Q000648:ultrastructure; D000818:Animals; D002417:Cattle; D005399:Fishes; D006168:Guinea Pigs; D006339:Heart Rate; D009200:Myocardial Contraction; D009206:Myocardium / Q000648:ultrastructure*; D011817:Rabbits; D051381:Rats; D012518:Sarcomeres / Q000648:ultrastructure*; D013045:Species Specificity; D014714:Vertebrates / Q000033:anatomy & histology* / Q000502:physiology