Cartilage of Marine Vertebrates

Ehrlich, Hermann

doi:10.1007/978-94-007-5730-1_2

Cited by 8 publications

(9 citation statements)

References 90 publications

(106 reference statements)

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“…It is recognized that so-called spongioblasts—derived from the epithelium of sponges—are responsible for the formation of spongin. Minchin claims that the fibers of skeletal spongin are formed extracellularly; however, the cuticular spongin fibrils are of intracellular origin [ 19 ]. In contrast to such structural proteins as collagen, fibroin (silk), elastin, resilin, and keratin, the chemistry and molecular biology—including the sequences—of spongins so far remain unknown.…”

Section: Spongins As Enigmatic Structural Proteins In Spongesmentioning

confidence: 99%

“…Marine vertebrate collagens have attracted scientific attention, mostly as products of fisheries [ 19 ]. In particular, fish-sourced collagens from skins and scales [ 20 , 21 , 22 ] have been studied and used as alternative collagen sources to avoid the potential risks associated with mammalian collagen due to bovine spongiform encephalopathy and the swine influenza crisis [ 23 ].…”

Section: Introductionmentioning

confidence: 99%

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Collagens of Poriferan Origin

Ehrlich

Wysokowski

Żółtowska-Aksamitowska

et al. 2018

Marine Drugs

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The biosynthesis, structural diversity, and functionality of collagens of sponge origin are still paradigms and causes of scientific controversy. This review has the ambitious goal of providing thorough and comprehensive coverage of poriferan collagens as a multifaceted topic with intriguing hypotheses and numerous challenging open questions. The structural diversity, chemistry, and biochemistry of collagens in sponges are analyzed and discussed here. Special attention is paid to spongins, collagen IV-related proteins, fibrillar collagens from demosponges, and collagens from glass sponge skeletal structures. The review also focuses on prospects and trends in applications of sponge collagens for technology, materials science and biomedicine.

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Section: Spongins As Enigmatic Structural Proteins In Spongesmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Collagens of Poriferan Origin

Ehrlich

Wysokowski

Żółtowska-Aksamitowska

et al. 2018

Marine Drugs

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“…Indeed, a few recent studies have also demonstrated that low molecular weight polypeptides from the T-cell determinant of human CII possess the ability to suppress T-cell activation in rheumatoid arthritis (RA), both in vitro and in the development of collagen induced arthritis (CIA) (Myers et al 2004). Recently, few studies have been focused on the preparation and biomedical application of type-II collagen peptides from cartilagous fish species (Ehrlich 2015;Xie et al 2014). To the best of our knowledge, the physicochemical and functional properties of these low molecular weight type-II collagenous polypeptides have not yet been reported.…”

Section: Introductionmentioning

confidence: 99%

Purification, characterization and antioxidant properties of low molecular weight collagenous polypeptide (37 kDa) prepared from whale shark cartilage (Rhincodon typus)

et al. 2015

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A low molecular weight type-II collagenous polypeptide (CIIp) from whale shark (WS) cartilage was prepared by thermolysin digestion; and examined for their physico-functional and antioxidant properties. The purified collagen was composed of an identical (α 1 ) 3 chains and was characterized as type-II. After hydrolysis with thermolysin, the α-chain of the WS collagen was degraded into smaller peptides with molecular weight ranging from 70 to 20KDa. CIIp was successfully separated from the hydrolysates with molecular weight of approximately 37 kDa. Amino acid analysis of CII, and CIIp indicated imino acid contents of 155 and 121 amino acid residues per 1000 residues, respectively. Differing Fourier transform infrared (FTIR) spectra of CII and CIIp were observed, which suggested that the hydrolysis process by thermolysin affected the secondary structure and molecular order of collagen, particularly the triple-helical structure. The denaturation temperature of CII (34°C) was higher than that of CIIp. Low content of glycoprotein was observed in CII than CIIp due to removal of some polypeptides by thermolysin digestion. The antioxidant activity against 1,1-diphenyl-2-picrylhydrazyl radicals and the reducing power of CIIp was greater than that of CII. The results proposed that the purified CIIp from WS cartilage with excellent antioxidant activities could be the suitable biomaterial for therapeutic applications.

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“…For the first time in scientific literature, the author gives the most coherent analysis of the nature, origin and evolution of biomaterials and biopolymers isolated from marine sources. Moreover, the variety of marine vertebrate organisms (fish, reptilian, birds and mammals) and within their unique hierarchically organized structural formations has been highlighted [ 61 ]. This can be a reference for performing future studies and research about the possibility of using chitin and collagen marine in the field of the biomedicine.…”

Section: Discussionmentioning

confidence: 99%

Facial Bone Reconstruction Using both Marine or Non-Marine Bone Substitutes: Evaluation of Current Outcomes in a Systematic Literature Review

et al. 2018

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The aim of the present investigation was to systematically analyse the literature on the facial bone reconstruction defect using marine collagen or not and to evaluate a predictable treatment for their clinical management. The revision has been performed by searched MEDLINE and EMBASE databases from 2007 to 2017. Clinical trials and animal in vitro studies that had reported the application of bone substitutes or not for bone reconstruction defect and using marine collagen or other bone substitute material were recorded following Preferred Reporting Items for Systematic Reviews and Meta-Analyses (PRISMA) guidelines. The first selection involved 1201 citations. After screening and evaluation of suitability, 39 articles were added at the revision process. Numerous discrepancies among the papers about bone defects morphology, surgical protocols, and selection of biomaterials were found. All selected manuscripts considered the final clinical success after the facial bone reconstruction applying bone substitutes. However, the scientific evidence regarding the vantage of the appliance of a biomaterial versus autologous bone still remains debated. Marine collagen seems to favor the dimensional stability of the graft and it could be an excellent carrier for growth factors.

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Cartilage of Marine Vertebrates

Cited by 8 publications

References 90 publications

Collagens of Poriferan Origin

Collagens of Poriferan Origin

Purification, characterization and antioxidant properties of low molecular weight collagenous polypeptide (37 kDa) prepared from whale shark cartilage (Rhincodon typus)

Facial Bone Reconstruction Using both Marine or Non-Marine Bone Substitutes: Evaluation of Current Outcomes in a Systematic Literature Review

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