Contractile properties of the myotomal muscle of sheepshead, Archosargus probatocephalus

Abstract

Swimming in fishes is powered by myotomal red, white and pink skeletal muscle. Slow swimming is powered by the red (slow-twitch muscle), fast speeds are achieved by the white (fast-twitch) muscle and pink muscle apparently serves an intermediate function. In recent years, the physiological properties and molecular composition of red (slow) and white (fast) muscle fibers have been well studied, while the intermediate pink muscle, which falls in a thin sheet between the superficial red muscle and deeper white muscle, has received less attention. The goal of this study is to determine the contractile properties of red, pink, and white muscle and to establish the molecular basis of fiber type variations in contractile properties in a sheepshead (Archosargus probatocephalus). Isometric and isovelocity muscle mechanics experiments demonstrated a general pattern of increasing contractile speed from red to pink to white muscle, although red and pink muscle did not differ significantly for most contraction kinetics variables. As myosin heavy chain (MyHC) is the most important structural protein found in the muscle fibers, MyHC content was examined through immunohistochemistry. Myosin antibodies suggest a gradient in myosin content corresponding to differences in muscle contraction kinetics.