Benedetto CD et al. (2014), Production, characterization and biocompatibili...

ECB-ART-43633

Mar Drugs 2014 Sep 24;129:4912-33. doi: 10.3390/md12094912.

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Production, characterization and biocompatibility of marine collagen matrices from an alternative and sustainable source: the sea urchin Paracentrotus lividus.

Benedetto CD , Barbaglio A , Martinello T , Alongi V , Fassini D , Cullorà E , Patruno M , Bonasoro F , Barbosa MA , Carnevali MD , Sugni M .

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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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Genes referenced: LOC100887844 LOC115919910 LOC594261

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	Figure 2. Collagen fibrils. (a) Collagen aqueous fibrillar suspension obtained by a protocol in which the hypotonic and decellularizating solutions were omitted. The brown color is mainly due to the presence of cell debris and pigments; (b) Clean aqueous collagen fibrillar suspension obtained by the complete protocol; (c) Transmission Electron Microscope (TEM). Cuprolinic Blue staining on isolated collagen fibrils. After collagen extraction, fibril-associated glycosaminoglycans (GAGs) could be detected periodically organized along the fibril surface (arrows); (d) TEM, negative staining on isolated collagen fibrils. The collagen fibril D period is clearly visible.
	Figure 3. SDS-PAGE gel of the obtained sea urchin collagen suspension. ** = Î±1 collagen chain; * = Î±2 collagen chain. Lane 1 = marker. Lane 2 = collagen suspension.
	Figure 4. Sea urchin collagen matrix (SCM). (a) Light microscopy (LM). After the treatment with Tx-100, collagen fibrils resulted homogeneously distributed on the plastic surface; (b) Scanning Electron Microscope (SEM). No cell debris, skeletal parts or undissociated collagen fibers are visible among fibrils; (c) LM. The average thickness of SCM is 5â€“7 Âµm. The thickness could slightly vary depending on the different areas of the matrix; (d) SEM. Different fibrils with different diameters are present in the SCM; (e) SEM. The average porosity of the matrix (mesh of the fibrillar interlace) is around 1â€“2 Î¼m2. Below is an example of interlace area measurement. Pa1 = 753 nm (major length); Pa2 = 253 nm (minor length). The area resulted less than 0.2 Âµm2; (f) SEM. Collagen D period is well detectable on collagen fibrils.


	Figure 7. LM. SCM for mechanical test. Plastic support (ps), sea urchin collagen matrix (scm).