Smooth muscle proteins as intracellular components of the chromatophores of the Antarctic fishes Pagothenia borchgrevinki and Trematomus bernacchii (Nototheniidae).

Abstract

Melanophores, xanthophores, and iridophores from the skins of the two Antarctic fish species Pagothenia borchgrevinki and Trematomus bernacchii were tested immunocytochemically for the presence of a variety of muscle proteins. Actin, myosin, and calmodulin, not surprisingly, were confirmed for all three chromatophore types of the two fishes, but the presence of caldesmon and calponin, both characteristic proteins of smooth muscle fibers, represents a new discovery. It is not known at this stage whether these proteins occur also in the chromatophores of other fishes and are not restricted to Antarctic species. Since, however, motility control of particles in fish chromatophores and the regulation of smooth muscle tension both involve the sympathetic nervous system, the presence of similar target proteins should not come as a surprise. The fact that none of the chromatophores tested positive for troponin shows that there is no close relationship between pigment cells and striated muscle. The lack of alpha-actinin in iridophores, but its presence in melanophores and xanthrophores, is thought to be a reflection of the considerably greater pigment translocations within the latter two types of chromatophore cells.