Striated muscle twitchin of bivalves has "catchability", the ability to bind thick filaments tightly to thin filaments, representing the catch state.
Catch muscles are found in some invertebrates which can maintain high passive tension with little energy expenditure for long periods after their active contraction. Twitchin in the catch muscles has the ability to facilitate the tight binding of thick filaments to thin filaments, which is the structural basis of the catch tension. We defined this ability as catchability and assessed the catchability of twitchins purified from striated muscles of an oyster (Crassostrea gigas) and a scallop (Mimachlamys nobilis), by using an in vitro catch assay where the binding of filaments could be directly visualized under a light microscope. We found that both twitchins had catchability, even though these muscles are not considered to be catch muscles in physiological experiments. In addition, these muscles contained water-soluble factors regulating the binding of the catch, probably protein kinase A and protein phosphatase 2B. These findings suggest that not only bivalve smooth muscles but also striated muscles have a system that regulates their relaxation rate through the catchability of twitchin, at least at the molecular level.
Tsutsui
Yasutaka
Y
Graduate School of Life Science, University of Hyogo, Hyogo 678-1297, Japan.
Yoshio
Maki
M
Oiwa
Kazuhiro
K
Yamada
Akira
A
D000818:Animals; D049872:Bivalvia / Q000737:chemistry / Q000502:physiology*; D003599:Cytoskeleton / Q000737:chemistry*; D009119:Muscle Contraction; D009124:Muscle Proteins / Q000502:physiology*; D018482:Muscle, Skeletal / Q000737:chemistry / Q000502:physiology*; D009130:Muscle, Smooth / Q000737:chemistry / Q000502:physiology; D009218:Myosins / Q000737:chemistry
D009124:Muscle Proteins; D009218:Myosins