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Abstract
Four proteases with molecular masses of 132, 58, 53, and 47 kDa were detected in the digestive system of the holothurian Eupentacta fraudatrix. These proteases displayed the gelatinase activity and characteristics of zinc metalloproteinases. The 58 kDa protease had similar protease inhibitor sensitivity to that of mammalian matrix metalloproteinases. Zymographic assay revealed different lytic activities of all four proteases during intestine regeneration in the holothurian. The 132 kDa protease showed the highest activity at the first stage. During morphogenesis (stages 2–4 of regeneration), the highest activity was measured for the 53 and 58 kDa proteases. Inhibition of protease activity exerts a marked effect on regeneration, which was dependent on the time when 1,10-phenanthroline injections commenced. When metalloproteinases were inhibited at the second stage of regeneration, the restoration rates were decreased. However, such an effect proved to be reversible, and when inhibition ceased, the previous rate of regeneration was recovered. When protease activity is inhibited at the first stage, regeneration is completely abolished, and the animals die, suggesting that early activation of the proteases is crucial for triggering the regenerative process in holothurians. The role of the detected proteases in the regeneration processes of holothurians is discussed.
Highlights
The extracellular matrix (ECM) plays an important role in the vitality of multicellular organisms [1]
The basis for ECM remodeling is provided by specific proteases, such as matrix metalloproteinases (MMPs) [5] and aminopeptidases [6]
The MMP activity increases because the rudiments of the main organ systems are being formed and the remodeling of the extracellular matrix takes place [39], [38], [29], [35]
Summary
The extracellular matrix (ECM) plays an important role in the vitality of multicellular organisms [1]. The ECM in each tissue or organ contains a unique set of factors that influence cell-cell interactions, cell differentiation and migration, making it very important in regulating embryonic development, growth, regeneration, and tumorigenesis [2], [3], [4]. The basis for ECM remodeling is provided by specific proteases, such as matrix metalloproteinases (MMPs) [5] and aminopeptidases [6]. These enzymes are able to degrade all known types of ECM proteins and, play an important role in embryonic development and regeneration; in the resorption and remodeling of tissue; in the migration, differentiation and proliferation of cells in both vertebrate and invertebrate animals; and in invasion and tumor metastasis [7], [8]. Page-McCaw [12] cited only five species in which the connective tissue and an MMP were studied: the fruit fly Drosophila melanogaster, nematode worm Caenorhabditis elegans, Hydra vulgaris and H. magnipapillata, and sea urchin Strongylocentrotus purpuratus
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