Ultrastructural and biochemical characterization of mechanically adaptable collagenous structures in the edible sea urchin Paracentrotus lividus

Barbaglio, Alice, Tricarico, Serena, Ribeiro, Ana R., Di Benedetto, Cristiano, Barbato, Marta, Dessì, Desirèe, Fugnanesi, Valeria, Magni, Stefano, Mosca, Fabio, Sugni, Michela, Bonasoro, Francesco, Barbosa, Mario A., Wilkie, Iain C., and Candia Carnevali, M. Daniela (2015) Ultrastructural and biochemical characterization of mechanically adaptable collagenous structures in the edible sea urchin Paracentrotus lividus. Zoology, 118. pp. 147-160.

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Abstract

The viscoelastic properties of vertebrate connective tissues rarely undergo significant changes within physiological timescales, the only major exception being the reversible destiffening of the mammalian uterine cervix at the end of pregnancy. In contrast to this, the connective tissues of echinoderms (sea urchins, starfish, sea cucumbers, etc.) can switch reversibly between stiff and compliant conditions in timescales of around a second to minutes. Elucidation of the molecular mechanism underlying such mutability has implications for the zoological, ecological and evolutionary field. Important information could also arise for veterinary and biomedical sciences, particularly regarding the pathological plasticization or stiffening of connective tissue structures. In the present investigation we analyzed aspects of the ultrastructure and biochemistry in two representative models, the compass depressor ligament and the peristomial membrane of the edible sea urchin Paracentrotus lividus, compared in three different mechanical states. The results provide further evidence that the mechanical adaptability of echinoderm connective tissues does not necessarily imply changes in the collagen fibrils themselves. The higher glycosaminoglycan (GAG) content registered in the peristomial membrane with respect to the compass depressor ligament suggests a diverse role of these molecules in the two mutable collagenous tissues. The possible involvement of GAG in the mutability phenomenon will need further clarification. During the shift from a compliant to a standard condition, significant changes in GAG content were detected only in the compass depressor ligament. Similarities in terms of ultrastructure (collagen fibrillar assembling) and biochemistry (two alpha chains) were found between the two models and mammalian collagen. Nevertheless, differences in collagen immunoreactivity, alpha chain migration on SDS-PAGE and BLAST alignment highlighted the uniqueness of sea urchin collagen with respect to mammalian collagen.

Item ID: 44420
Item Type: Article (Research - C1)
ISSN: 1873-2720
Keywords: echinoderm; sea urchin; collagen; mutable collagenous tissue; glycosaminoglycans
Funders: CARIPLO Foundation
Projects and Grants: MIMESIS Project, Advanced Materials 2009-25-65
Date Deposited: 17 Jun 2016 05:35
FoR Codes: 06 BIOLOGICAL SCIENCES > 0606 Physiology > 060604 Comparative Physiology @ 50%
06 BIOLOGICAL SCIENCES > 0608 Zoology > 060807 Animal Structure and Function @ 50%
SEO Codes: 97 EXPANDING KNOWLEDGE > 970106 Expanding Knowledge in the Biological Sciences @ 100%
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