Parvalbumin expression in trout swimming muscle correlates with relaxation rate.

Rainbow trout (Oncorhynchus mykiss) display longitudinal and developmental shifts in muscle relaxation rate. This study aimed to determine the role of variations in parvalbumin content in modulating muscle relaxation. Parvalbumin is a low molecular weight protein that buffers myoplasmic Ca2+ and enhances muscle relaxation. In some fish, longitudinal variations in muscle relaxation have been linked to variations in the total amount of parvalbumin present in muscle and in the relative expression of two parvalbumin isoforms. We have demonstrated previously that anterior slow-twitch or red myotomal muscle relaxes more rapidly than that from the posterior for both rainbow and brook trout. Further, younger rainbow trout parr have faster red muscle relaxation rates than older smolts. Here we report similar results for fast-twitch or white muscle. We quantified the parvalbumin expression in red and white muscle from different body positions of rainbow trout parr and smolts and for brook trout (Salvelinus fontinalis) adults. There was a significant shift in total parvalbumin content of muscle: the faster muscle from the anterior myotome contained greater amounts of parvalbumin. For brook trout, longitudinal variation in relaxation rate was also associated with shifts in the relative expression of the two parvalbumin isoforms. The faster muscle of parr contained more parvalbumin. Lastly, trout white muscle tended to have higher levels of parvalbumin and greater levels of the Parv2 (relative to Parv1) isoform as compared to red muscle. Parvalbumin expression correlated with muscle relaxation rate in trout, although there were species-specific differences in the importance of altering total parvalbumin content versus shifts in relative parvalbumin isoform expression.

Parvalbumin correlates with relaxation rate in the swimming muscle of sheepshead and kingfish.

Parvalbumin is a muscle protein that aids in relaxation from contraction. Parvalbumin binds myoplasmic Ca(2+) during contractions, reducing calcium concentration and enhancing relaxation. Different isoforms of parvalbumin have varying affinities for calcium, and relaxation rates in skeletal muscle may be affected by variations in the isoforms of parvalbumin expressed. This study examines the effect of expression levels of parvalbumin isoforms on relaxation rate in the sheepshead, Archosargus probatocephalus (Pisces, F. Sparidae). We measured relaxation rate of each of the three fiber types, white (fast-twitch), red (slow-twitch) and pink (intermediate), from three longitudinal body positions. Sheepshead show a significant longitudinal shift in relaxation rate in red muscle, with anterior muscle displaying faster rates of relaxation than posterior, but this pattern was not significant in the pink and white muscle. We hypothesized that patterns of parvalbumin expression determine relaxation rate along the length of the fish. The prediction is that total parvalbumin content and the relative expression of parvalbumin isoforms will differ between the anterior and posterior red muscle, but little longitudinal variation will be observed in parvalbumin expression in white and pink muscle. We successfully employed protein electrophoresis (SDS-PAGE) with western blots to identify two parvalbumin isoforms in each muscle fiber type. SDS-PAGE and densitometry were used to determine the relative expression levels of the two parvalbumin isoforms and total parvalbumin expression. Red muscle displays a significant shift, from anterior to posterior, in the relative expression of the two isoforms, both in their relative contribution and in total parvalbumin content, but white and pink muscle did not. The red muscle of southern kingfish, Menticirrhus americanus (Pisces, F. Scianidae) showed a pattern similar to the red muscle of sheepshead.