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      Marine Origin Collagens and Its Potential Applications

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          Abstract

          Collagens are the most abundant high molecular weight proteins in both invertebrate and vertebrate organisms, including mammals, and possess mainly a structural role, existing different types according with their specific organization in distinct tissues. From this, they have been elected as one of the key biological materials in tissue regeneration approaches. Also, industry is constantly searching for new natural sources of collagen and upgraded methodologies for their production. The most common sources are from bovine and porcine origin, but other ways are making their route, such as recombinant production, but also extraction from marine organisms like fish. Different organisms have been proposed and explored for collagen extraction, allowing the sustainable production of different types of collagens, with properties depending on the kind of organism (and their natural environment) and extraction methodology. Such variety of collagen properties has been further investigated in different ways to render a wide range of applications. The present review aims to shed some light on the contribution of marine collagens for the scientific and technological development of this sector, stressing the opportunities and challenges that they are and most probably will be facing to assume a role as an alternative source for industrial exploitation.

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          Most cited references95

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          Collagens: molecular biology, diseases, and potentials for therapy.

          The collagen superfamily of proteins now contains at least 19 proteins formally defined as collagens and an additional ten proteins that have collagen-like domains. The most abundant collagens form extracellular fibrils or network-like structures, but the others fulfill a variety of biological functions. Some of the eight highly specific post-translational enzymes involved in collagen biosynthesis have recently been cloned. Over 400 mutations in 6 different collagens cause a variety of human diseases that include osteogenesis imperfecta, chondrodysplasias, some forms of osteoporosis, some forms of osteoarthritis, and the renal disease known as the Alport syndrome. Many of the disease phenotypes have been produced in transgenic mice with mutated collagen genes. There has been increasing interest in the possibility that the unique post-translational enzymes involved in collagen biosynthesis offer attractive targets for specifically inhibiting excessive fibrotic reactions in a number of diseases. A number of experiments suggest it may be possible to inhibit collagen synthesis with oligo-nucleotides or antisense genes.
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            Investigation of jumbo squid (Dosidicus gigas) skin gelatin peptides for their in vitro antioxidant effects.

            Peptides derived from tryptic hydrolysate of jumbo squid (Dosidicus gigas) skin gelatin were assessed for their antioxidant properties in different in vitro assay systems. The hydrolysate itself exhibited a strong lipid peroxidation inhibition and it was much higher than that of natural antioxidant, alpha-tocopherol. In addition, it could scavenge highly active free radicals in oxidative systems, in the order of hydroxyl and carbon-centered radicals. Two representative peptides with comparatively higher antioxidant potency were purified and characterized as Phe-Asp-Ser-Gly-Pro-Ala-Gly-Val-Leu (880.18 Da) and Asn-Gly-Pro-Leu-Gln-Ala-Gly-Gln-Pro-Gly-Glu-Arg (1241.59 Da). Furthermore, viability of radical-mediated oxidation-induced human lung fibroblasts was enhanced following the treatment of two peptides. However it did not exhibit substantial ion chelation, and we presumed that the observed radical scavenging potency of these peptides play a vital role for their strong antioxidant activity. Based on our results we suggest that hydrophobic amino acids present in peptide sequences contributed greatly for observed antioxidant activities.
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              Characterisation of acid-soluble collagen from skin and bone of bigeye snapper (Priacanthus tayenus)

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                Author and article information

                Contributors
                Role: External Editor
                Journal
                Mar Drugs
                Mar Drugs
                marinedrugs
                Marine Drugs
                MDPI
                1660-3397
                05 December 2014
                December 2014
                : 12
                : 12
                : 5881-5901
                Affiliations
                [1 ]3B’s Research Group—Biomaterials, Biodegradables and Biomimetics, University of Minho, Headquarters of the European Institute of Excellence on Tissue Engineering and Regenerative Medicine, AvePark, 4806-909 Taipas, Guimarães, Portugal; E-Mails: joana.silva@ 123456dep.uminho.pt (J.M.-S.); ana.marques@ 123456dep.uminho.pt (A.L.P.M.); albertadomingues@ 123456gmail.com (A.D.); rgreis@ 123456dep.uminho.pt (R.L.R.)
                [2 ]ICVS/3B’s—PT Government Associate Laboratory, Braga/Guimarães, Portugal
                [3 ]Covidien—Sofradim Production, F-01600 Trevoux, France; E-Mail: yves.bayon@ 123456covidien.com
                Author notes
                [* ]Author to whom correspondence should be addressed; E-Mail: tiago.silva@ 123456dep.uminho.pt ; Tel.: +351-253-510-900; Fax: +351-253-510-909.
                Article
                marinedrugs-12-05881
                10.3390/md12125881
                4278207
                25490254
                bbeeb881-799c-4db4-b613-74455de3fdc4
                © 2014 by the authors; licensee MDPI, Basel, Switzerland.

                This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution license ( http://creativecommons.org/licenses/by/4.0/).

                History
                : 01 August 2014
                : 11 November 2014
                : 19 November 2014
                Categories
                Review

                Pharmacology & Pharmaceutical medicine
                collagen,marine biotechnology,marine biomaterials,tissue engineering,biomedical application,valorization,marine byproducts

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