Polyamine‐Induced Actin Polymerization

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Abstract
Muscle actin apparently polymerizes reversibly upon addition of low concentrations of polyamines. This polymerization, studied by centrifugation, showed a linear relationship between the [rabbit] actin polymerization yield and polyamine chain length. Among the biological polyamines tested, spermidine and spermine were most efficient. Polymerization of actin was also induced by the corresponding mono or diguanidine derivatives of these polyamines, but monoamines or amino acids were inactive at the same concentration. Transformation of actin from a globular to a fibrous form upon addition of spermidine was also demonstrated by changes in the near-UV circular dichroic spectrum of this protein. Polyamine-induced F-actin exhibited the same properties as the salt-induced F-actin: it strongly activated the Mg2+-ATPase of myosin, its specific viscosity was enhanced to the same extent and EM showed homogeneous thin filaments.

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