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First published online January 3, 2006
Journal of Experimental Biology 209, 227-237 (2006)
Published by The Company of Biologists 2006
doi: 10.1242/jeb.01987
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Parvalbumin correlates with relaxation rate in the swimming muscle of sheepshead and kingfish

Jennifer L. Wilwert, Nisreen M. Madhoun and David J. Coughlin*

Widener University, Department of Biology, One University Place, Chester, PA 19013, USA



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  		Fig. 1. Tetanic activation and relaxation time and twitch time for isometric contractions in sheepshead and kingfish muscle. Values (means ± s.e.m.) are given at three body positions for red muscle and two body positions for white and pink muscle. In kingfish red muscle there is a significant effect of longitudinal position on activation time (asterisk). Sheepshead red muscle there is a significant effect of longitudinal position on relaxation time and twitch time (asterisk). Definitions of variables and statistical analysis can be found in the text. N=5 (sheepshead red muscle), N=4 (kingfish red muscle and sheepshead white muscle), N=6 (sheepshead pink muscle).

 


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  		Fig. 2. Identification of parvalbumin in sheepshead muscle. Upper image is a SyproRuby-stained SDS–PAGE gel showing a pair of bands in the 10–11 kDa range in red, pink and white muscle of sheepshead. The lower image is a western blot of the same gel employing an anti-parvalbumin antibody. All three muscle fiber types appear to express the same two parvalbumin isoforms.

 


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  		Fig. 3. Identification of parvalbumin in kingfish muscle. Upper image is a SyproRuby-stained SDS–PAGE gel showing a pair of bands in the 10–11 kDa range in red and white muscle of kingfish. The lower image is a western blot of the same gel employing an anti-parvalbumin antibody. Both muscle fiber types appear to express the same two parvalbumin isoforms. The larger (upper) isoform has relatively low affinity for the antibody.

 


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  		Fig. 4. SDS–PAGE showing parvalbumin expression in sheepshead red muscle from six body positions, ranging from 35–85% of the body length from the snout. The two isoforms occur in all body positions. In this animal, there is a gradual increase in the relative contribution of Parv1, from 50% Parv1 at 35% of body length to 67% Parv1 at 85% of body length. There is also a gradual decrease in total parvalbumin expression from anterior to posterior.

 


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  		Fig. 5. SDS–PAGE showing parvalbumin expression in sheepshead white muscle from seven body positions ranging from 25–85% of the body length from the snout. The two isoforms are evident in all body positions. In this animal, there is a gradual increase in the relative contribution of Parv1, from 45% Parv1 at 25% of body length to 60% Parv1 at 85% of body length. There is a clear decrease in total parvalbumin expression from anterior to posterior.

 


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  		Fig. 6. Expression of the larger parvalbumin isoform, Parv1, relative to total parvalbumin content (expressed as a proportion). Values (mean ± s.e.m.) are given for 7 body positions for all sheepshead muscle types and three body positions for red muscle of kingfish. In sheepshead and kingfish red muscle, there is a significant longitudinal shift in parvalbumin expression, with a higher proportion of Parv1 in the posterior swimming muscle. There is also a similar pattern of Parv1 content in the other sheepshead muscle fiber types but this is not statistically significant. N=6 (sheepshead red muscle), 4 (kingfish red muscle and sheepshead white muscle), 3 (sheepshead pink muscle).

 


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  		Fig. 7. Total parvalbumin in sheepshead red and white and kingfish red muscle. Values (mean ± s.e.m.) of normalized total parvalbumin are given for each muscle fiber types from several body positions. The means reflect the relative expression for a given muscle fiber type, but comparisons of the values between muscle fiber types are not valid. All fiber types show a longitudinal pattern of higher parvalbumin content in the anterior myotome, but the effect is only statistically significant for the sheepshead red muscle. N=5 (sheepshead red muscle), 4 (sheepshead white and kingfish red muscle).

 


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  		Fig. 8. Relationship of relaxation time to parvalbumin expression in sheepshead and kingfish muscle. For each fish (different colored symbols), the relationship of relaxation time to the relative expression of the Parv1 isoform is shown. r2 values are given for lines for which there is a substantial variation in the independent variable (and at least three points). All four kingfish show the same pattern of increasing relaxation time with increasing relative contribution of Parv1. Four of the five sheepshead show the same pattern in the red muscle but no clear trend is evident in the sheepshead white muscle data.

 


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  		Fig. 9. Relationship of relaxation time to normalized total parvalbumin expression in sheepshead muscle. For each fish (different colored symbols), the relationship of relaxation time to total parvalbumin expression is shown. r2 values are given for lines for which there is a substantial variation in the independent variable (and at least three points). In the red muscle, all four kingfish and all five sheepshead show the same pattern of decreasing relaxation time with increasing total parvalbumin content. In the white muscle, there is little variation in relaxation time.

 


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  		Fig. 10. Relaxation rate as a function of both normalized total parvalbumin and relative Parv1 expression in sheepshead red muscle. The multiple regression had a P value of 0.031. Red muscle equation: relaxation rate=190.3+142.5xrelative Parv1 expression–124.0x normalized total parvalbumin.

 


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  		Fig. 11. Relaxation rate as a function of both normalized total parvalbumin and relative Parv1 expression in kingfish red muscle. The multiple regression had a P value of 0.050. Red muscle equation: relaxation rate=86.7+296.5xrelative Parv1 expression–7.3x normalized total parvalbumin.

 

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© The Company of Biologists Ltd 2006