Preparation of myosin A from body wall musculature of Ascaris lumbricoides

Yamaguchi, Masahiro; Nakamura, Takeshi; Okumura, Hiroshi; Sekine, Toshimori

doi:10.1016/0005-2795(73)90226-2

Cited by 6 publications

(1 citation statement)

References 18 publications

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“…Parallel regulatory pathways via both direct Ca ++ thick filament binding (Lehman and Szent-Györgyi, 1975; and myosin light chain phosphorylation (Martin et al, 1986) are also present. Ascaris actomyosin is active at low (relative to rabbit skeletal actomyosin) ATP concentrations (Yamaguchi et al, 1973). Villafranca et al, 1959Villafranca et al, , 1968Stanley, 1970) and requires Mg ++ and Ca ++ for activation (de Villafranca and Naumann, 1964;de Villafranca, 1967;de Villafranca and Campbell, 1969;de Villafranca and Waksmonski, 1970).…”

Section: Ecdysozoa Nematoda-mentioning

confidence: 99%

Invertebrate muscles: Thin and thick filament structure; molecular basis of contraction and its regulation, catch and asynchronous muscle

Hooper

Hobbs

Thuma

2008

Progress in Neurobiology

131

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This is the second in a series of canonical reviews on invertebrate muscle. We cover here thin and thick filament structure, the molecular basis of force generation and its regulation, and two special properties of some invertebrate muscle, catch and asynchronous muscle. Invertebrate thin filaments resemble vertebrate thin filaments, although helix structure and tropomyosin arrangement show small differences. Invertebrate thick filaments, alternatively, are very different from vertebrate striated thick filaments and show great variation within invertebrates. Part of this diversity stems from variation in paramyosin content, which is greatly increased in very large diameter invertebrate thick filaments. Other of it arises from relatively small changes in filament backbone structure, which results in filaments with grossly similar myosin head placements (rotating crowns of heads every 14.5 nm) but large changes in detail (distances between heads in azimuthal registration varying from three to thousands of crowns). The lever arm basis of force generation is common to both vetebrates and invertebrates, and in some invertebrates this process is understood on the near atomic level. Invertebrate actomyosin is both thin (tropomyosin:troponin) and thick (primarily via direct Ca ++ binding to myosin) filament regulated, and most invertebrate muscles are dually regulated. These mechanisms are well understood on the molecular level, but the behavioral utility of dual regulation is less so. The phosphorylation state of the thick filament associated giant protein, twitchin, has been recently shown to be the molecular basis of catch. The molecular basis of the stretch activation underlying asynchronous muscle activity, however, remains unresolved.

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