Data di Pubblicazione:
2012
Citazione:
Matrix metallopreteinases in a sea urchin ligament with adaptable mechanical properties / A.R. Ribeiro, A. Barbaglio, M.J. Oliveira, C.C.Ribeiro, I.C. Wilkie, M.D. Candia Carnevali, M.A. Barbosa. - In: PLOS ONE. - ISSN 1932-6203. - 7:11(2012), pp. e49016.e49016.1-e49016.e49016.12. [10.1371/journal.pone.0049016]
Abstract:
Mutable collagenous tissues (MCTs) of echinoderms show reversible changes in tensile properties (mutability) that are
initiated and modulated by the nervous system via the activities of cells known as juxtaligamental cells. The molecular
mechanism underpinning this mechanical adaptability has still to be elucidated. Adaptable connective tissues are also
present in mammals, most notably in the uterine cervix, in which changes in stiffness result partly from changes in the
balance between matrix metalloproteinases (MMPs) and tissue inhibitors of metalloproteinases (TIMPs). There have been no
attempts to assess the potential involvement of MMPs in the echinoderm mutability phenomenon, apart from studies
dealing with a process whose relationship to the latter is uncertain. In this investigation we used the compass depressor
ligaments (CDLs) of the sea-urchin Paracentrotus lividus. The effect of a synthetic MMP inhibitor - galardin - on the
biomechanical properties of CDLs in different mechanical states (‘‘standard’’, ‘‘compliant’’ and ‘‘stiff’’) was evaluated by
dynamic mechanical analysis, and the presence of MMPs in normal and galardin-treated CDLs was determined semiquantitatively
by gelatin zymography. Galardin reversibly increased the stiffness and storage modulus of CDLs in all three
states, although its effect was significantly lower in stiff than in standard or compliant CDLs. Gelatin zymography revealed a
progressive increase in total gelatinolytic activity between the compliant, standard and stiff states, which was possibly due
primarily to higher molecular weight components resulting from the inhibition and degradation of MMPs. Galardin caused
no change in the gelatinolytic activity of stiff CDLs, a pronounced and statistically significant reduction in that of standard
CDLs, and a pronounced, but not statistically significant, reduction in that of compliant CDLs. Our results provide evidence
that MMPs may contribute to the variable tensility of the CDLs, in the light of which we provide an updated hypothesis for
the regulatory mechanism controlling MCT mutability.
Tipologia IRIS:
01 - Articolo su periodico
Elenco autori:
A.R. Ribeiro, A. Barbaglio, M.J. Oliveira, C.C. Ribeiro, I.C. Wilkie, M.D. Candia Carnevali, M.A. Barbosa
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