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Echinobase
ECB-ART-42795
PLoS One 2013 Jan 01;83:e58433. doi: 10.1371/journal.pone.0058433.
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Proteases from the regenerating gut of the holothurian Eupentacta fraudatrix.

Lamash NE , Dolmatov IY .


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.

PubMed ID: 23505505
PMC ID: PMC3591370
Article link: PLoS One


Species referenced: Echinodermata
Genes referenced: LOC594261 LOC752081 LOC756768


Article Images: [+] show captions
References [+] :
Adams, Regulation of development and differentiation by the extracellular matrix. 1993, Pubmed