Calponin, caldesmon, and chromatophores: The smooth muscle connection

Abstract

Observations on pigment translocations in fish chromatophores and speculations on the chemo-mechanical transduction processes responsible for the recorded chromatosome motilities are briefly reviewed. The presence of the two smooth muscle proteins caldesmon and calponin is confirmed by immunocytochemistry for melanophores and iridophores of the Antarctic fishes Pagothenia borchgrevinki and Trematomus bernacchii. Troponin, a typical vertebrate skeletal muscle protein is absent from the chromatophores of the two fish species. It is suggested that calponin's role, in the presence of Ca(2+) and calmodulin, is that of a modulator and that caldesmon, a molecule that competes with calponin for actin binding sites, is in a position in which it can switch on and off Ca(2+)-dependent contractility and relaxation. Freshly caught Antarctic fish are receiving conflicting signals, when hauled from the dark under-ice to the bright above-ice environment (nor-adrenaline secretion promoting aggregation, but exposure to bright light bringing on pigment dispersion); it is in such situations that the two proteins in question could play important roles. The precise nature of their involvement still needs to be worked out, but the fact that they do exist in the chromatophores at all, appears to have an ontogenetic background.