Paramyosin and the filaments of molluscan “catch” muscles

Cohen, Carolyn; Szent‐Györgyi, Albert; Kendrick‐Jones, John

doi:10.1016/0022-2836(71)90461-x

Cited by 165 publications

(56 citation statements)

References 26 publications

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“…Characteristic coiled-coil helical structure with repeated sequences of hydrophilic and charged amino acids, which is a typical structural property of paramyosins [1], was found throughout the CsPmy sequence. The CsPmy was found to be expressed in various developmental stages from metacercariae to adults.…”

Section: Discussionmentioning

confidence: 99%

“…The protein mainly localizes in muscles, acting as a key component in the formation of large filaments in mollusca [1] and likely playing an important role in specialized contractile activities [1][2][3]. Paramyosin has been also identified in numerous helminth parasites, including Schistosoma mansoni [4][5][6], Schistosoma japonicum [7][8][9], Fasciola hepatica [10], Paragonimus westermani [11], Taenia solium [12,13], Echinococcus granulosus [14], and Onchocerca volvulus [15].…”

Section: Introductionmentioning

confidence: 99%

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Molecular Cloning and Characterization of a Paramyosin from Clonorchis sinensis

Park

Kang

et al. 2009

Korean J Parasitol

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Paramyosin is a myofibrillar protein present in helminth parasites and plays multifunctional roles in host-parasite interactions. In this study, we identified the gene encoding paramyosin of Clonorchis sinensis (CsPmy) and characterized biochemical and immunological properties of its recombinant protein. CsPmy showed a high level of sequence identity with paramyosin from other helminth parasites. Recombinant CsPmy (rCsPmy) expressed in bacteria had an approximate molecular weight of 100 kDa and bound both human collagen and complement 9. The protein was constitutively expressed in various developmental stages of the parasite. Imunofluorescence analysis revealed that CsPmy was mainly localized in the tegument, subtegumental muscles, and the muscle layer surrounding the intestine of the parasite. The rCsPmy showed high levels of positive reactions (74.6%, 56/75) against sera from patients with clonorchiasis. Immunization of experimental rats with rCsPmy evoked high levels of IgG production. These results collectively suggest that CsPmy is a multifunctional protein that not only contributes to the muscle layer structure but also to non-muscular functions in host-parasite interactions. Successful induction of host IgG production also suggests that CsPmy can be applied as a diagnostic antigen and/or vaccine candidate for clonorchiasis.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Molecular Cloning and Characterization of a Paramyosin from Clonorchis sinensis

Park

Kang

et al. 2009

Korean J Parasitol

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“…Although not present in all synthetic filaments {Camatini, 1976 24200 /id; Castellani, 1978 32320 /id;Hodge, 1952 24202 /id;Locker, 1957 29855 /id;Obinata, 1975 30188 /id}, in many species these filaments have either 72.5 nm periodicity (Limulus: Ikemoto and Kawaguti, 1967;amphioxus: Castellani-Ceresa and Lanzavecchia, 1982;sea urchin: Fukushima and Murakami, 1985;mollusc: Hanson et al, 1957;Tien-Chin et al, 1965;Kendrick-Jones et al, 1969;Cohen et al, 1971;Fukushima and Murakami, 1985;crustacea: Tien-Chin et al, 1965), or a checkerboard pattern (annelid: Weisel, 1975;mollusc: Cohen et al, 1971;Weisel, 1975), which agrees well with the observations on real large diameter thick filaments.…”

Section: 21mentioning

confidence: 99%

“…These data and the known length of the paramyosin molecule were then used to explain the multiple types of paramyosin filament staining patterns as arising from variations in a common molecular structure (Kendrick-Jones et al, 1969;Cohen et al, 1971;Cohen, 1998). The fundamental building block of this model is that the paramyosin dimers bind with partial overlaps that result in gaps between axially adjacent molecules ( Fig.…”

Section: 21mentioning

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

124

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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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“…In molluscs, paramyosin may play a role in the specialized function described as catch, in which some muscle types can generate strong isometric contractions for long periods of time, using very little energy (Twarog, 1976;Szent-Gy6rgyi et al ., 1971;Cohen et al ., 1971) . However, paramyosin is present in other invertebrate muscles which do not display catch-like characteristics (Bullard et al, 1973;Waterston et al ., 1974;Levine et al ., 1983 ;Hinkel-Aust et al ., 1990) .…”

mentioning

confidence: 99%

Analysis of Drosophila paramyosin: identification of a novel isoform which is restricted to a subset of adult muscles.

Becker

O'Donnell

Heitz

et al. 1992

The Journal of Cell Biology

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Abstract. In this report we show that Drosophila melanogaster muscles contain the standard form of the thick filament protein paramyosin, as well as a novel paramyosin isoform, which we call miniparamyosin . We have isolated Drosophila paramyosin using previously established methods. This protein is =105 kD and cross-reacts with polyclonal antibodies made against Caenorhabditis elegans or Heliocopris dilloni paramyosin. The Heliocopris antibody also cross-reacts with a

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Paramyosin and the filaments of molluscan “catch” muscles

Cited by 165 publications

References 26 publications

Molecular Cloning and Characterization of a Paramyosin from Clonorchis sinensis

Molecular Cloning and Characterization of a Paramyosin from Clonorchis sinensis

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

Analysis of Drosophila paramyosin: identification of a novel isoform which is restricted to a subset of adult muscles.

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