Comparative analysis of the structure and thermal stability of sea urchin peristome and rat tail tendon collagen

Mayne, Janice; Robinson, John J.

doi:10.1002/jcb.10048

Cited by 17 publications

(10 citation statements)

References 26 publications

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“…Fibril diameter ranged between 25 nm and 300 nm (Figure 4d) which corresponds to what has been reported for mammalian fibrils [48] as well as for the PM [10]. Sea urchin collagen denaturation temperature is 27 °C in Strongylocentrotus purpuratus [49]. Nevertheless, despite the step at 37 °C, the experimental protocol did not influence the final chance to get a matrix where fibrils maintained their integrity and could be efficiently cross-linked.…”

Section: Resultssupporting

confidence: 70%

Production, Characterization and Biocompatibility of Marine Collagen Matrices from an Alternative and Sustainable Source: The Sea Urchin Paracentrotus lividus

et al. 2014

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Collagen has become a key-molecule in cell culture studies and in the tissue engineering field. Industrially, the principal sources of collagen are calf skin and bones which, however, could be associated to risks of serious disease transmission. In fact, collagen derived from alternative and riskless sources is required, and marine organisms are among the safest and recently exploited ones. Sea urchins possess a circular area of soft tissue surrounding the mouth, the peristomial membrane (PM), mainly composed by mammalian-like collagen. The PM of the edible sea urchin Paracentrotus lividus therefore represents a potential unexploited collagen source, easily obtainable as a food industry waste product. Our results demonstrate that it is possible to extract native collagen fibrils from the PM and produce suitable substrates for in vitro system. The obtained matrices appear as a homogeneous fibrillar network (mean fibril diameter 30–400 nm and mesh < 2 μm) and display remarkable mechanical properties in term of stiffness (146 ± 48 MPa) and viscosity (60.98 ± 52.07 GPa·s). In vitro tests with horse pbMSC show a good biocompatibility in terms of overall cell growth. The obtained results indicate that the sea urchin P. lividus can be a valuable low-cost collagen source for mechanically resistant biomedical devices.

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Section: Resultssupporting

confidence: 70%

Production, Characterization and Biocompatibility of Marine Collagen Matrices from an Alternative and Sustainable Source: The Sea Urchin Paracentrotus lividus

et al. 2014

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“…It was shown that during zymography Triton X-100 replaces SDS and partially recovers the fibrillar organization of collagen making its available as a substrate for collagenase. Moreover collagen from sea urchins denaturates at 25 °C–30 °C [41]. In our experiments we tried to reduce the risk of collagen degradation and performed electrophoresis and zymography at 4° and 25 °C respectively.…”

Section: Discussionmentioning

confidence: 99%

“…It is known that echinoderm collagen denaturates at 25 °C–30 °C [41]. Thus, for determination of substrate specificity of proteases the electrophoresis and zymography were performed at 4 °C and 25 °C respectively.…”

Section: Methodsmentioning

confidence: 99%

Proteases from the Regenerating Gut of the Holothurian Eupentacta fraudatrix

Lamash

Dolmatov

2013

PLoS ONE

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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.

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“…A HE with similar properties and functions has also been found in sea stars [112,113]. In addition, various proteinases capable of degrading collagen and gelatin have been found in the eggs and developing embryos of the sea urchin S. purpuratus [87][88][89][114][115][116][117][118][119][120][121][122]. All of them show properties similar to those of the MMPs.…”

Section: Substrate Specificity and Functionmentioning

confidence: 78%

Matrix Metalloproteinases and Tissue Inhibitors of Metalloproteinases in Echinoderms: Structure and Possible Functions

Dolmatov

Nizhnichenko

Долматова

2021

Cells

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Echinoderms are one of the most ancient groups of invertebrates. The study of their genomes has made it possible to conclude that these animals have a wide variety of matrix metalloproteinases (MMPs) and tissue inhibitors of metalloproteinases (TIMPs). The phylogenetic analysis shows that the MMPs and TIMPs underwent repeated duplication and active divergence after the separation of Ambulacraria (Echinodermata+Hemichordata) from the Chordata. In this regard the homology of the proteinases and their inhibitors between these groups of animals cannot be established. However, the MMPs of echinoderms and vertebrates have a similar domain structure. Echinoderm proteinases can be structurally divided into three groups—archetypal MMPs, matrilysins, and furin-activatable MMPs. Gelatinases homologous to those of vertebrates were not found in genomes of studied species and are probably absent in echinoderms. The MMPs of echinoderms possess lytic activity toward collagen type I and gelatin and play an important role in the mechanisms of development, asexual reproduction and regeneration. Echinoderms have a large number of genes encoding TIMPs and TIMP-like proteins. TIMPs of these animals, with a few exceptions, have a structure typical for this class of proteins. They contain an NTR domain and 10–12 conservatively located cysteine residues. Repeated duplication and divergence of TIMP genes of echinoderms was probably associated with an increase in the functional importance of the proteins encoded by them in the physiology of the animals.

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Comparative analysis of the structure and thermal stability of sea urchin peristome and rat tail tendon collagen

Cited by 17 publications

References 26 publications

Production, Characterization and Biocompatibility of Marine Collagen Matrices from an Alternative and Sustainable Source: The Sea Urchin Paracentrotus lividus

Production, Characterization and Biocompatibility of Marine Collagen Matrices from an Alternative and Sustainable Source: The Sea Urchin Paracentrotus lividus

Proteases from the Regenerating Gut of the Holothurian Eupentacta fraudatrix

Matrix Metalloproteinases and Tissue Inhibitors of Metalloproteinases in Echinoderms: Structure and Possible Functions

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