Characterization of the Single Tyrosine Containing Troponin C from Lungfish White Muscle. Comparison with Several Fast Skeletal Muscle Troponin C's from Fish Species

François, Jean-Marie; Altintaş, Arif; Gerday, Charles

doi:10.1016/s0305-0491(97)00006-0

Cited by 5 publications

(2 citation statements)

References 36 publications

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“…In birds, mammals and amphibians, a fast-fibre type and a type specific to both slow and cardiac fibres have been identified (Reinach and Karlsson, 1988;Gahlmann and Kedes, 1990;Parmacek et al, 1990;Jin et al, 1995;Tiso et al, 1997;Warkman and Atkinson, 2002). Numerous studies have investigated aspects of TnC function in teleosts at the protein level (Demaille et al, 1974;McCubbin et al, 1982;Gerday et al, 1984;Feller and Gerday, 1989;Crockford and Johnston, 1993;Francois et al, 1997), but until now the only published nucleotide sequences were those from zebrafish (showing highest identity to Xenopus fast-type; Xu et al, 2000) and trout (showing highest identity to Xenopus slow/cardiactype; Moyes et al, 1996). Because protein sequences with homology to both fast-skeletal and slow/cardiac forms have been isolated from fish, it has been supposed that their nature is equivalent to those in birds and mammals (Yuasa et al, 1998).…”

Section: Discussionmentioning

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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Section: Discussionmentioning

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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“…Through phylogenetic analysis of existing fish genome sequences, we demonstrate that ssTnC is not only present in zebrafish (as seen in embryos) but broadly across teleosts species (12, 16, 48). Using adult zebrafish and rainbow trout as models, we examined paralog gene expression tissue localization patterns as well as temperature acclimation effects to begin to examine the relevance of three fish-specific paralogs of TnC.…”

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Adult teleost heart expresses two distinct troponin C paralogs: cardiac TnC and a novel and teleost-specific ssTnC in a chamber- and temperature-dependent manner

Genge

Davidson

Tibbits

2013

Physiological Genomics

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The teleost-specific whole genome duplication created multiple copies of genes allowing for subfunctionalization of isoforms. In this study, we show that the teleost cardiac Ca2+-binding troponin C (TnC) is the product of two distinct genes: cardiac TnC (cTnC, TnnC1a) and a fish-specific slow skeletal TnC (ssTnC, TnnC1b). The ssTnC gene is novel to teleosts as mammals have a single gene commonly referred as cTnC but which is also expressed in slow skeletal muscle. In teleosts, the data strongly indicate that these are two TnC genes are different paralogs. Because we determined that ssTnC exists across many teleosts but not in basal ray-finned fish (e.g., bichir), we propose that these paralogs are the result of an ancestral tandem gene duplication persisting only in teleosts. Quantification of mRNA levels was used to demonstrate distinct expression localization patterns of the paralogs within the chambers of the heart. In the adult zebrafish acclimated at 28°C, ssTnC mRNA levels are twofold greater than cTnC mRNA levels in the atrium, whereas cTnC mRNA was almost exclusively expressed in the ventricle. Meanwhile, rainbow trout acclimated at 5°C showed cTnC mRNA levels in both chambers significantly greater than ssTnC. Distinct responses to temperature acclimation were also quantified in both adult zebrafish and rainbow trout, with mRNA in both chambers shifting to express higher levels of cTnC in 18°C acclimated zebrafish and 5°C acclimated trout. Possible subfunctionalization of TnC isoforms may provide insight into how teleosts achieve physiological versatility in chamber-specific contractile properties.

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TroponinC

Gagn��

2004

Handbook of Metalloproteins

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Regulation of contraction in skeletal and cardiac muscle occurs through calcium binding to the protein troponin C (TnC). The N‐terminal domain of TnC (NTnC) carries out the regulatory role through the binding of calcium ions – two calcium ions in skeletal muscle and one in cardiac muscle. Thirty‐nine sequences of TnC have been sequenced so far. Of the 39 sequences of TnC, 5 have had their three‐dimensional structures determined in various forms by NMR and X‐ray. Available structures include 26 uncomplexed structures in various calcium states, and 13 structures in which cardiac and skeletal TnC is complexed with fragments of troponin I and/or troponin T.

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Characterization of the Single Tyrosine Containing Troponin C from Lungfish White Muscle. Comparison with Several Fast Skeletal Muscle Troponin C's from Fish Species

Cited by 5 publications

References 36 publications

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

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

Adult teleost heart expresses two distinct troponin C paralogs: cardiac TnC and a novel and teleost-specific ssTnC in a chamber- and temperature-dependent manner

TroponinC

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