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First published online December 26, 2008
Journal of Experimental Biology 212, 184-193 (2009)
Published by The Company of Biologists 2009
doi: 10.1242/jeb.021857
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Regional variation in parvalbumin isoform expression correlates with muscle performance in common carp (Cyprinus carpio)

Philip Brownridge1,*, Luciane Vieira de Mello2,*, Mary Peters1,*, Lynn McLean1, Amy Claydon1, Andrew R. Cossins2, Phillip D. Whitfield1 and Iain S. Young1,{dagger}

1 Faculty of Veterinary Science, University of Liverpool, Liverpool, UK
2 School of Biological Sciences, University of Liverpool, Liverpool, UK


Figure 1
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  		Fig. 1. The different analyses performed. Transcript and protein level analyses were employed to detect and characterise PARV isoforms, and biomechanics was used to quantify the physiological outputs.

 

Figure 2
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  		Fig. 2. A typical twitch record, chosen as it has kinetics close to the mean values obtained. Time to peak twitch tension Tpeak was measured as the time from baseline force to peak force during activation. The time taken for the muscle force to decline from its peak to 50% of its peak (RT50%) and to 10% of its peak (i.e. a 90% decline in force; RT90%) were used as indices for the rate of relaxation.

 

Figure 3
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  		Fig. 3. A sequence consensus alignment for all the parvalbumin genes from the carpBase database (120 transcripts). The phylogenetic connection between the isoforms alongside their theoretical physical properties is also shown. The figure was made with Jalview (www.ebi.ac.uk/~michele/jalview) and a consensus, neighbour-joining phylogenetic tree illustrating the relationship between the isoforms [drawn with the PHYLIP package (Felsenstein, 1989Go)].

 

Figure 4
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  		Fig. 4. A 15% 1D-SDS-PAGE gel of the unboiled soluble fraction of fast-twitch muscle.

 

Figure 5
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  		Fig. 5. MALDI–TOF (matrix assisted laser desorption ionisation–time of flight) mass spectrum of an in-gel tryptic digestion of the band corresponding to PARV from a 1D-SDS-PAGE of the unboiled soluble fraction of fast-twitch muscle. Proposed peak identities are shown in Table 1.

 

Figure 6
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  		Fig. 6. Peptide maps representing the peptides observed by MALDI–mass spectrometry (MS) of the in-gel tryptic digestion of the band corresponding to PARV from a 1D-SDS-PAGE of the unboiled soluble fraction of fast-twitch muscle (see Fig. 5). The black regions indicate that the peptide is observed and the light grey regions indicate that the peptide is observed as part of a missed cleavage. Figure produced using PeptideMapper (Beynon, 2005Go).

 

Figure 7
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  		Fig. 7. The cropped region of a 15% 2D-PAGE gel displaying the separation of PARV isoforms by a 24 cm, pH 4–5 immobilised pH gradient (IPG) strip. The spots were identified by in-gel tryptic digestion followed by nanospray-tandom mass spectrometry (MS/MS) sequencing of the N-terminal peptides (except for {alpha}, which was identified from the C-terminus).

 

Figure 8
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  		Fig. 8. Cropped regions of 2D-PAGE using a 24 cm IPG strip of boiled sample showing the difference between the anterior (top image in each frame) and posterior (lower image in each frame) areas of the fish.

 

Figure 9
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  		Fig. 9. Mechanical properties of the anterior and posterior axial muscles: maximum isometric force and activation. Error bars are ±s.e.m. (A) Maximum isometric force measured during a tetanic contraction. (B) Activation measured as the time from zero force to the peak twitch force. *P<0.05.

 

Figure 10
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  		Fig. 10. Mechanical properties of the anterior and posterior axial muscles: relaxation kinetics. Error bars are ±s.e.m. The graph shows time to 90% maximum force (left) and 50% maximum force (right) during the relaxation phase. *P<0.05.

 

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© The Company of Biologists Ltd 2009