On the tropomyosin-paramyosin system in relation to the viscous tone of lamellibranch ‘catch’ muscle

Author:

Abstract

Some lamellibranch muscles are able to maintain tension for prolonged periods with very little energy expenditure, possibly by means of a special ‘catch' mechanism. Whilst actomyosin seems to be associated with active contraction, the 'catch' might well be linked with tropomyosin A ( TM A ) which is more abundant in these muscles than actomyosin ( AM ) and located in special filaments known as paramyosin. There is in fact a correlation of tropo­myosin content and ‘tonic’ properties in three different portions of Pecten maximus adductor muscle, the striated adductor ( AM/TM = 9:1), the translucent portion of the smooth adductor ( AM/TM = 2:1), and the opaque portion of the latter ( AM/TM = 1:2). A typical ‘catch’ can be demonstrated in the glycerinated fibres of the tropomyosin-rich but not in the tropomyosin-poor type by measuring fibre rigidity in presence of adenosine triphosphate ( ATP ) and Mg ions. Quick release and stretch experiments have shown that, unlike active contraction, rigidity in presence of ATP is not dependent on a functional AM system, which can be inactivated with Salyrgan, denatured with ethanol or plasticized with pyrophosphate. Instead, a change in fibre rigidity is always found to be associated with a change in the colloidal state of TM A when the latter is selectively modified in situ , as, for example, by varying the pH between 6⋅5 and 8 or the ratio of the Mg- ATP chelate to 'free' ATP . The latter increases the solubility and the electrophoretic mobility of TM A and it plasticizes artificial tropomyosin threads or the tropomyosin system in situ . Its action is best explained in terms of a decrease in protein-protein interaction caused by an increase in net charge due to binding, an effect which it counteracted by divalent cations which combine with ATP . Extra­-polating these findings to the behaviour of living muscle one might tentatively suggest that the high rigidity of glycerinated tonic adductor muscle fibres in presence of Mg- ATP corresponds to the high muscle ‘viscosity’ of tonically contracted living molluscan muscle and that free ATP acts as a physiological plasticizer, inducing changes in muscle ‘viscosity’ by affecting the electrostatic tropomyosin-tropomyosin interaction either within or between the para­myosin (tropomyosin) filaments.

Publisher

The Royal Society

Subject

General Medicine

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