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Shelud’ko, Nikolay S.; Permjakova, T.; Tuturova, K.F.; Neverkina, O.; Дроздов, А. Л.

doi:10.1023/a:1010359718304

Cited by 24 publications

(14 citation statements)

References 33 publications

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“…The major component of large diameter molluscan thick filaments is paramyosin whose surface is covered with myosin [ 1 ], twitchin [ 2 , 3 ] and myorod [ 4 ]. Myorod is a protein that is specific to catch muscle [ 4 , 5 ], its content greatly exceeds the amount of twitchin while it is equally as abundant as myosin [ 6 , 7 ].…”

Section: Introductionmentioning

confidence: 99%

“…Myorod, a water-insoluble, heat-resistant protein consists of two polypeptides of 112 and 120 kDa [ 4 , 7 ], is an alternative product of the myosin heavy-chain gene. It contains a C-terminal rod part, which is identical to the rod portion of myosin, and a unique N-terminal domain [ 8 ].…”

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

“…Myorod, as well as myosin, is capable of polymerization in solutions of low and physiological ionic strength; however, the properties and structure of myorod filaments differ significantly from those of myosin [ 7 ]. In particular, solutions of myorod have unusually high viscosity, far lower aggregation capacity and resistance to MgATP, which differently than for myosin does not suppress polymerization of myorod [ 7 ]. Such differences are surprising because both proteins have identical C-terminal rod parts [ 8 ] and should therefore possess identical assembly competence domains (ACD), which are responsible for their polymerization [ 10 ].…”

Section: Introductionmentioning

confidence: 99%

“…Such differences are surprising because both proteins have identical C-terminal rod parts [ 8 ] and should therefore possess identical assembly competence domains (ACD), which are responsible for their polymerization [ 10 ]. As it turns out, the N-terminal domain of myorod may affect the properties of the C-terminal parts of the molecule and, in turn, its filament assembly [ 7 , 11 ].…”

Section: Introductionmentioning

confidence: 99%

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Catch Muscle Myorod Modulates ATPase Activity of Myosin in a Phosphorylation-Dependent Way

et al. 2015

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Myorod is expressed exclusively in molluscan catch muscle and localizes on the surface of thick filaments together with twitchin and myosin. Myorod is an alternatively spliced product of the myosin heavy-chain gene that contains the C-terminal rod part of myosin and a unique N-terminal domain. The unique domain is a target for phosphorylation by gizzard smooth myosin light chain kinase (smMLCK) and, perhaps, molluscan twitchin, which contains a MLCK-like domain. To elucidate the role of myorod and its phosphorylation in the catch muscle, the effect of chromatographically purified myorod on the actin-activated Mg2+-ATPase activity of myosin was studied. We found that phosphorylation at the N-terminus of myorod potentiated the actin-activated Mg2+-ATPase activity of mussel and rabbit myosins. This potentiation occurred only if myorod was phosphorylated and introduced into the ATPase assay as a co-filament with myosin. We suggest that myorod could be related to the catch state, a function specific to molluscan muscle.

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

Catch Muscle Myorod Modulates ATPase Activity of Myosin in a Phosphorylation-Dependent Way

et al. 2015

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Euopisthobranchs: Musculature

Lobo‐da‐Cunha,

Bartolomaeus,

Malaquias

2024

Microscopic Anatomy of Animals

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Muscular systems of euopisthobranchs comprise body muscles and the muscular tissue of internal organs. Body wall musculature is stronger in species without a shell or with a reduced shell. Most euopisthobranchs have a muscular ventral foot for benthic locomotion. However, in pteropods, the foot is highly modified into wing‐like parapodia used for swimming, and other euopisthobranchs also possess muscular parapodia. In euopisthobranchs the musculature is markedly developed around the buccal cavity, in the esophagus, and in the gizzard in species that have a gizzard. Muscle cells contain a contractile system made of thin and thick myofilaments. Thin myofilaments consist of actin associated with other proteins, and thick myofilaments are formed by a paramyosin core coated with myosin molecules. Electron‐dense bodies are points of attachment for thin myofilaments, which are also linked to the cell membrane. Smooth muscle fibers are the most common type of muscle cell in euopisthobranchs. In these cells, the electron‐dense bodies are scattered in the cytoplasm, and a striated pattern is not formed. Caveolae are very abundant in the cell membrane of these muscle fibers. As in other mollusks, transversely striated muscle fibers are not common in euopisthobranchs, being present in the heart and a few other muscles. In these cells, a transverse striation is created by the alignment of contractile units formed by thin and thick myofilaments that resemble the sarcomeres of vertebrates, but with discontinuous Z‐lines.

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Comparative characteristic of Mytilus muscle cells developed in vitro and in vivo

2003

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The mussel cells from premyogenic larval stages are capable of differentiation into smooth muscle cells in vitro. However, the behavior and protein composition of these cells are not completely identical to those of smooth muscle cells of adult mussels. In this study we compared some properties of mussel muscle cells forming from cells of trochophore (premyogenic larval stage) in vitro with those of muscle cells of veliger and adult mussel. We found a substantial difference between the contractile apparatus protein composition of veliger muscle and cultivated cells. Myorod, one of the molecular markers of the phenotype of mollusc smooth muscle cells (Shelud'ko et al., 1999, Comp Biochem Physiol 122:277-285), is not a constituent of the contractile apparatus of veliger muscle. At the same time the protein composition of contractile apparatus in cultivated cells was similar to that of adult Mytilus muscles. There were only few quantitative differences between them. The contractile activity of cultivated cells was changing in time. The kinetic parameters of first spontaneous contractions were similar to those of phasic contractions, while their period was close to that of tonic contractions. After 50-55 hrs cultivation the cells produced both phasic and tonic contractions, but the character of contractile activity of cultivated cells was regulated after six days of cultivation only. However, there were no muscle cells in vitro, whose contractile activity was similar to that of veliger muscle cells. So, we concluded that properties of muscle cells forming from premyogenic larval mussel cells in culture are similar to those of muscle cells of the adult mussel, but not of veliger.

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Cited by 24 publications

References 33 publications

Catch Muscle Myorod Modulates ATPase Activity of Myosin in a Phosphorylation-Dependent Way

Catch Muscle Myorod Modulates ATPase Activity of Myosin in a Phosphorylation-Dependent Way

Euopisthobranchs: Musculature

Comparative characteristic of Mytilus muscle cells developed in vitro and in vivo

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