Titin Isoforms and Kinematics of Fast Swimming Carp Larvae (Cyprinus Carpio L.)

Abstract

Titin, a striated-muscle specific protein spanning the distance between Z- and M-lines of sarcomeres, is held responsible for developing passive tension and for maintaining the central position of thick filaments in contracting sarcomeres. Different muscles express titin isoforms of different molecular mass. To improve the insight in the relation between titin isoforms and kinematics of fast swimming at different ages the presence of carp larval muscle titin (Cyprinus carpio L.) was investigated and compared with data of adult carp. Gel-electrophoresis revealed that titin isoforms were larger in adult than in larval muscle. Apparently the molecular structure of titin changed during ontogeny. A previous study showed that the size of titin is correlated with the functioning of different muscles during swimming. Fish larvae (6.5-8 mm total length), subjected to low Reynolds-number regimes during swimming (Re < 500), require special features to overcome frictional effects. Fibres with smaller titin isoforms require more passive tension when being stretched. During fast swimming of larvae, passively stretched fibres at the convex side of the body axis absorb energy, generated by activity of fibres at the concave side, that is released in the successive opposite bending.