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Is high concentration of parvalbumin a requirement for superfast relaxation?

  • Boris A. Tikunov
  • Lawrence C. RomeEmail author
original paper

Abstract

It is generally thought that the rapid relaxation of fast muscles is facilitated by the Ca2+ binding protein parvalbumin (Parv). Indeed superfast swimbladder (SWB) muscle of toadfish contains the largest concentration of this protein ever observed (up to 1.5 mM). At 15°C toadfish perform a 100 Hz call, 400 ms in duration, followed by a long (5–15 s) intercall interval. It has been proposed that Parv helps sequester the Ca2+ during the call, and then Ca2+ unbinds and is pumped back into the sarcoplasmic reticulum during the long intercall interval. Midshipman (Porichthys notatus) is another fish which calls at a high frequency; 80–100 Hz at a temperature of 12–15°C. However, unlike toadfish, midshipman call with a 100% duty cycle. Without an intercall interval, Parv would seem of little use as it would become saturated early in calling. Here we show that the midshipman SWB has only about 1/8th of the Parv in toadfish. Moreover, total Parv content in calling male midshipman SWB was not different from that in the non-calling female and the much slower locomotory muscles. These data suggest that Parv does not play a large role in the calling of midshipman, which is accomplished without a high concentration of this protein. Native gel-electrophoresis also revealed presence of three major (PA-I, PA-II and PA-III) and two minor (PA-Ia and PA-IIIa, <5% of total content) Parv isoforms in adult toadfish SWB. Midshipman SWB contained about equal amounts of PA-I and PA-II and also a small (~10%) amount of PA-III. By amino acid composition, toadfish PA-Ia and PA-I isoforms were different from PA-II and PA-III isoforms (by 24 and 14 residues, respectively).

Keywords

Parvalbumin Toadfish Midshipman Superfast muscle Calcium Swimbladder 

Notes

Acknowledgments

The authors thank Professor Andy Bass, Cornell University, for his insights and for providing the midshipman used in this study. The authors also thank Professor Taylor Allen, Oberlin College, and Professor Harold Zakon, University of Texas, for helpful discussions on molecular evolution and structure-function relationships in parvalbumin. The work was supported by NIH grants AR38404 (LCR) and AR46125(LCR).

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Copyright information

© Springer Science+Business Media B.V. 2009

Authors and Affiliations

  1. 1.Biology DepartmentUniversity of PennsylvaniaPhiladelphiaUSA
  2. 2.Marine Biological LaboratoryWoods HoleUSA

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