Abstract

The compass depressors (CDs) of the sea-urchin lantern are ligaments consisting mainly of discontinuous collagen fibrils associated with a small population of myocytes. They are mutable collagenous structures, which can change their mechanical properties rapidly and reversibly under nervous control. The aims of this investigation were to characterise the baseline (i.e. unmanipulated) static mechanical properties of the CDs of Paracentrotus lividus by means of creep tests and incremental force-extension tests, and to determine the effects on their mechanical behaviour of a range of agents. Under constant load the CDs exhibited a three-phase creep curve, the mean coefficient of viscosity being 561±365 MPa.s. The stress-strain curve showed toe, linear and yield regions; the mean strain at the toe-linear inflection was 0.86±0.61; the mean Young’s modulus was 18.62±10.30 MPa; and the mean tensile strength was 8.14±5.73 MPa. Hyaluronidase from Streptomyces hyalurolyticus had no effect on creep behaviour, whilst chondroitinase ABC prolonged primary creep but had no effect on secondary creep or on any force-extension parameters; it thus appears that neither hyaluronic acid nor sulphated glycosaminoglycans have an interfibrillar load transfer function in the CD. Acetylcholine, the muscarinic agonists arecoline and methacholine, and the nicotinic agonists nicotine and 1-[1-(3,4-dimethyl-phenyl)-ethyl]-piperazine produced an abrupt increase in CD viscosity; the CDs were not differentially sensitive to muscarinic or nicotinic agonists. CDs showed either no, or no consistent, response to adrenaline, L-glutamic acid, 5-hydroxytryptamine and γ-aminobutyric acid. Synthetic echinoid tensilin-like protein had a weak and inconsistent stiffening effect, indicating that, in contrast to holothurian tensilins, the echinoid molecule may not be involved in the regulation of collagenous tissue tensility. We compare in detail the mechanical behaviour of the CD with that of mammalian tendon and highlight its potential as a model system for investigating poorly understood aspects of the ontogeny and phylogeny of vertebrate collagenous tissues.

Highlights

  • The feeding apparatus (Aristotle’s lantern) of regular sea-urchins is an integrated complex of skeletal elements, muscles and connective tissue structures

  • Resource limitations prevented us from conducting a proper dose-response investigation, which would have revealed if the compass depressors (CDs) are more responsive to higher tensilin-like protein (TLP) concentrations. In both the creep and incremental force-extension tests the CDs were subjected to a range of stresses that extended well above the inferred in vivo limit, our results, like those derived from non-physiological investigations of mammalian tissues, provide an insight into the properties of the CD as a material

  • The CD demonstrated (1) a three-phase creep curve under constant loads, (2) a three-phase stress-strain curve most of the parameters of which exhibited strain rate dependence and (3) rapid slow phases of stress relaxation when held at a constant strain, with stress relaxation rates increasing as constant strain increased

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Summary

Introduction

The feeding apparatus (Aristotle’s lantern) of regular sea-urchins is an integrated complex of skeletal elements, muscles and connective tissue structures It includes a sub-set of components comprising the compass system, which appears to serve primarily as a respiratory pump whose role is to oxygenate the lantern muscles [1], [2]. The compass depressors (CDs) have attracted considerable attention, because their collagenous component has the capacity to undergo rapid and reversible changes in mechanical properties under physiological control [4,5,6,7,8,9]. This has already resulted in the development of a polymer nanocomposite with chemoresponsive tensile properties [19], and the feasibility of designing biocompatible materials with site-specific and/or adjustable tensile properties is being explored using collagen matrices prepared from sea-urchin sources [20], [21]

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