White muscle differentiation in the eel (Anguilla anguilla L.): changes in the myosin isoforms pattern and ATPase profile during post-metamorphic development

Chanoine, Christophe; Guyot-Lenfant, Michèle; Attari, Ahmed El; Saadi, Assia; Gallien, Claude-Louis

doi:10.1111/j.1432-0436.1992.tb00770.x

Cited by 13 publications

(4 citation statements)

References 36 publications

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“…The peptide maps obtained here with H. longifilis muscle preparations show that distinct myosin heavy-chain isoforms are synthesised in the white muscle of larvae, juveniles fishes and adults. Similar observations have been made on other teleost (Martinez et al 1991(Martinez et al , 1993Chanoine et al 1992;Focant et al 1992;Brooks and Johnston 1993;Crockford and Johnston 1993;Johnston et al 1997;James et al 1998). One-and two-dimensional PAGE did not reveal any qualitative or quantitative difference in the alkali light chains LC1 and LC3 during development.…”

Section: Myosinsupporting

confidence: 87%

“…They observed qualitative and/or quantitative differences in expression of the alkali light chains LC1 and LC3 and in the relative proportions of the two tropomyosin subunits. Polymorphism of myosin isoforms has also been demonstrated during growth of the eel, Anguilla anguilla (L. 1758) (Chanoine et al 1992). Changes in the composition of all myofibrillar proteins have been investigated in the myotomal muscle of the Atlantic herring, Clupea harengus L. 1758 reared at temperatures ranging from 5 • C to 15 • C. It was concluded that although the main muscle-fibre type in larvae shares some myofibrillar proteins with adult white muscle, it also contains characteristic isoforms of myosin heavy chains, myosin light chain LC2, troponin-I, and troponin-T and thus represents a distinct fibre type (Crockford and Johnston 1993).…”

Section: Introductionmentioning

confidence: 99%

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Huriaux

Vandewalle

Baras

et al. 1999

Fish Physiology and Biochemistry

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Developmental changes in myofibrillar protein composition were investigated in the myotomal muscle of the African catfish, Heterobranchus longifilis (Clariidae), by several electrophoretic techniques. The main muscle fibres of larvae and the fast-white muscle fibres of juvenile and adult fish were found to express distinct myosin heavy chain and myosin light chain 2 (LC2) isoforms. Three myosin LC2 chains were successively detected, differing by their isoelectric points. In contrast, the alkali light chains remained qualitatively and quantitatively unchanged during fish growth. Actin, α-tropomyosin, and troponin-C (TN-C) were also similar in larval, juvenile, and adult white muscle, but an additional larval tropomyosin isoform was found in the first developmental stages. Two isoforms of troponin-T (TN-T) and troponin-I (TN-I) were synthesised in the course of fish growth. Transition from the larval to the adult isoform was much faster for TN-T than for TN-I. Slow-red muscle myofibrils from adult H. longifilis showed no common component (except actin) with larval, juvenile, or adult fast-white muscle myofibrils. Red myofibrils displayed a single TN-T and a single TN-I isoform, but two isoforms of TN-C. The myofibrillar protein isoforms synthesised at any given developmental stage almost certainly reflect changes in the functional requirements of swimming muscles in the course of fish development.

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Section: Myosinsupporting

confidence: 87%

Section: Introductionmentioning

confidence: 99%

Untitled

Huriaux

Vandewalle

Baras

et al. 1999

Fish Physiology and Biochemistry

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“…During larval developAt hatch the larval stages of many fish species contain a single superficial layer of small-diameter muscle fibres that express fast muscle myosin light chains (LC) (Johnston and Horne 1994) and have a myosin heavy-chain composition distinct from that of adult red and white muscle fibres (Mascerello et al 1995). During ontogeny there is sequential expression of different myosin heavy chains in fish (Chanoine et al 1992;Crockford and Johnston 1993;Martinez et al 1991). The myosin LC isoform compositions of the white muscle of embryonic and 5-year-old Arctic charr (Salvelinus alpinus) were shown to be similar (Martinez et al 1991), whereas the myosin LC3:LCl ratio increased with development ment in other species the myofibrillar protein composition and metabolic characteristics of the embryonic superficial and inner muscle fibres gradually come to resemble those of adult red and white muscle fibres, respectively (Dicentrarchus labrax, Scapolo et al 1988; Rutilus rutilus, El-Fiky et al 1987), and pink and tonic muscle fibres are formed (Scophthalmus maximus, Gibson and Johnston 1995 ; Sparus a u r a t a , Mascerello et al 1995).…”

Section: Introductionmentioning

confidence: 97%

Temperature and family effects on muscle cellularity at hatch and first feeding in Atlantic salmon (Salmo salarL.)

Johnston¹

1997

Can. J. Zool.

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Muscle cellularity was investigated in alevins from five families of Atlantic salmon (Salmo salar L.) reared at variable ambient temperatures averaging 4.3"C and in water heated to ca. 8°C. At hatch, fish reared at 8°C had fewer muscle fibres and myonuclei per myotome and lower mean fibre cross-sectional areas than fish reared at ambient temperature. The total cross-sectional area of white muscle was 40% less in the group reared at 8°C than in the group reared at ambient temperature. Muscle cellularity and response to temperature varied among families and there was evidence of interactions with temperature and developmental stage. The number of red and white muscle fibres approximately doubled between hatch and first feeding. At hatch, red muscle fibres stained with an antibody to fast myosin light chains, but expression was gradually switched off as development proceeded. Following hatch, alevins reared at 8°C were more effective in translating yolk into muscle than those reared at ambient temperature, so towards the end of yolk resorption there were no significant differences in fibre number or cross-sectional area.RCsumC : La cellularitk musculaire a kt6 ktudike chez les alevins de cinq familles de Saumons de I'Atlantique (Salmo salar L.) klevkes a des temperatures ambiantes variables (moyenne de 4,3"C) ou dans de l'eau chauffke a environ 8°C. Comparativement aux poissons klevks aux tempkratures ambiantes, au moment de I'~closion, les poissons gardks a 8°C avaient moins de fibres musculaires et de noyaux par myotome et, en coupe transversale, leurs fibres avaient une surface moyenne moindre. La surface totale des coupes transversales de muscle blanc ktait 40% plus petite chez les poissons klevks a 8°C que chez les poissons klevks a tempkrature ambiante. La cellularitk musculaire et la rkaction a la tempkrature variaient d'une famille de poissons a l'autre, vraisemblablement influenckes par la temperature et le stade de dkveloppement atteint. Le nombre de fibres de muscle rouge et de muscle blanc a a peu prks doublk entre l'kclosion et le premier repas. A l'kclosion, les fibres de muscle rouge se coloraient en prksence d'un anticorps des chaines lkgkres de myosine de muscle rapide, mais la rkaction est disparue graduellement au cours du dkveloppement. Aprks l'kclosion, les alevins a 8°C ktaient plus aptes a utliser leur vitellus pour la croissance musculaire, que les alevins des poissons a tempkraature ambiante, si bien que, vers la fin de la rksorption du vitellus, il n'y avait plus de diffkrences significatives du nombre de fibres ou de la surface des coupes transversales entre les deux groupes de poissons. [Traduit par la Rkdaction]

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“…During ontogeny, embryonic isoforms of the myofibrillar proteins are gradually replaced by larval and adult isoforms, reflecting increases in body sizes and associated changes in swimming behaviour (Martinez et al, 1991;Chanoine et al, 1992;Mascarello et al, 1995). The relative timing of expression of developmentalstage specific isoforms varies for different myofibrillar components and is altered by rearing temperature (Johnston et al, 1997(Johnston et al, , 1998.…”

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confidence: 99%

Temperature and the expression of seven muscle-specific protein genes during embryogenesis in the Atlantic codGadus morhuaL.

Hall

Cole

Johnston

2003

Journal of Experimental Biology

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SUMMARYSeven cDNA clones coding for different muscle-specific proteins (MSPs) were isolated from the fast muscle tissue of Atlantic cod Gadus morhua L. In situ hybridization using cRNA probes was used to characterize the temporal and spatial patterns of gene expression with respect to somite stage in embryos incubated at 4°C, 7°C and 10°C. MyoDtranscripts were first observed in the presomitic mesoderm prior to somite formation, and in the lateral compartment of the forming somites. MyoD expression was not observed in the adaxial cells that give rise to the slow muscle layer, and expression was undetectable by in situhybridization in the lateral somitic mesoderm after the 35-somite stage,during development of the final ∼15 somites. RT-PCR analysis, however,confirmed the presence of low levels of the transcript during these later stages. A phylogenetic comparison of the deduced aminoacid sequences of the full-length MyoD cDNA clone and those from other teleosts, and inference from the in situ expression pattern suggested homology with a second paralogue (MyoD2) recently isolated from the gilthead seabream Sparus aurata. Following MyoD expression,α-actin was the first structural gene to be switched on at the 16-somite stage, followed by myosin heavy chain, troponin T, troponin I and muscle creatine kinase. The final mRNA in the series to be expressed was troponin C. All genes were switched on prior to myofibril assembly. The troponin C sequence was unusual in that it showed the greatest sequence identity with the rainbow trout Oncorhynchus mykiss cardiac/slow form, but was expressed in the fast myotomal muscle and not in the heart. In addition, the third TnC calcium binding site showed a lower level of sequence conservation than the rest of the sequence. No differences were seen in the timing of appearance or rate of posterior progression (relative to somite stage) of any MSP transcripts between embryos raised at the different temperatures. It was concluded that myofibrillar genes are activated asynchronously in a distinct temporal order prior to myofibrillar assembly and that this process was highly canalized over the temperature range studied.

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White muscle differentiation in the eel (Anguilla anguilla L.): changes in the myosin isoforms pattern and ATPase profile during post-metamorphic development

Cited by 13 publications

References 36 publications

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Temperature and family effects on muscle cellularity at hatch and first feeding in Atlantic salmon (Salmo salarL.)

Temperature and the expression of seven muscle-specific protein genes during embryogenesis in the Atlantic codGadus morhuaL.

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