Preparation and Some Properties of Type I Collagen from Fish Scales

Collagen for biomedical applications is mainly isolated from animal tissues (bovine or porcine skin and bovine or equine Achilles tendons). Type I collagen has been also extracted from skin, bone, fins and scales of fresh water and marine fishes. Fish scales are composed of collagen covered with calcium salts. In the present study we report the preparation of collagen from fish scales for potential cosmetic, pharmaceutical and implant applications. In our laboratory collagen was isolated from scales ofEsox lucius. It was the first time that this species were used as sources of collagen. Extraction of collagen from fish scales was done in two steps. In the first step, fish scales were demineralized using EDTA. Energy dispersive X-ray analysis of demineralized scale was carried out for quantitative estimation of inorganic content. Then, demineralized fish scales were dissolved in acetic acid. Collagen isolated fromEsox Luciusmay serve as an attractive and safe source of collagen for biomedical and pharmaceutical applications. Fish collagen can be processed in sheet, sponges foams, injectable viscous solution, and dispersions.

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Organization and characterization of fibrillar collagens in fish scales in situ and in vitro

Journal of Cell Science ◽

10.1242/jcs.103.1.273 ◽

1992 ◽

Vol 103 (1) ◽

pp. 273-285 ◽

Cited By ~ 1

Author(s):

L. ZYLBERBERG ◽

J. BONAVENTURE ◽

L. COHEN-SOLAL ◽

D. J. HARTMANN ◽

J. BEREITERHAHN

Keyword(s):

Cyanogen Bromide ◽

Type I Collagen ◽

Collagen Fibrils ◽

Type I ◽

Fish Scales ◽

Fibrillar Collagens ◽

Collagen Genes

The characterization of the fibrillar collagens and the cellular control of their spatial deposition were studied in fish scales using immunofluorescence, electron microscopy, electrophoretic and HPLC analyses, immunoprecipitation and hybridization with cDNA probes. This study was carried out on undisturbed and regenerating scales in situ and in organ and cell cultures from regenerating scales. The hyposquamal scleroblasts forming a pseudoepithelium show an apico-basal polarization and synthesize thick collagen fibrils (100 nm) organized in a plywood pattern as long as the integrity of the cell-cell and cell-collagenous matrix contacts are preserved. In culture, scleroblasts become fibroblastlike and produce an unordered meshwork of thin collagen fibrils (30 nm). Comparison of the synthesized collagens in culture with those extracted from the scales indicates that culture conditions modify fibrillogenesis but do not change the expression of fibrillar collagen genes. Type I collagen, the predominent component, is associated with the minor type V collagen. Type III collagen was not present. In type I collagen, a third chain, α3 chain, was identified. The ratio between the 3 chains suggests the coexistence of two heterotrimers (α(I))2 α2(I) and αl(I) α2(I) α3(I). Analysis by HPLC and electrophoresis of the cyanogen bromide-derived peptides obtained from the purified a3 chain support the hypothesis that α(I) and α3(I) chains are encoded by two different genes. The presence of the two types of heterotrimers in vivo as well as in vitro could correspond to an innate property of the goldfish scleroblasts. Despite the fact that teleost cyanogen bromide-derived peptides differ from those of higher vertebrates, homologies with the mammalian collagen genes (human, for example) are sufficient to allow the detection of mRNA transcripts for αl(I), α2(I) and α2(V) from confluent scleroblast cultures with human probes.

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REGENERASI SEL LIGAMEN PERIODONTAL DENGAN KOLAGEN SISIK IKAN NILA (Oreochromis niloticus)

Jurnal Medali ◽

10.30659/medali.v3i1.16767 ◽

2021 ◽

Vol 3 (1) ◽

pp. 44

Author(s):

Adhalin Fuku Handini ◽

Rosa Pratiwi ◽

Tahta Danifatis Sunnah

Keyword(s):

Bone Graft ◽

Oreochromis Niloticus ◽

Periodontal Ligament ◽

Type I Collagen ◽

Periodontal Ligament Cells ◽

Type I ◽

Fish Scales ◽

Periodontal Ligament Cell ◽

Alternative Source ◽

Tilapia Scale

Background : Regeneration of periodontal ligament cells with tilapia scales collagen (Oreochromis niloticus) is one of the therapies that can be used in the field of periodontics. This review aims to explain the mechanism of periodontal ligament cell regeneration using tilapia scales (Oreochromis niloticus) collagen.Methods : Literature collection is done by selecting journals or articles through PubMed, NCBI, and Google Scholar based on keywords that match the author's criteria.Results : Regeneration of cells using collagen from tilapia scales can be used by using a bone graft technique because fish collagen contains calcium and phosphate that resembles human, namely hydroxyapatite (HAP). Fish scales are an alternative source of type I collagen and have the potential to be an alternative material for bone graft.Conclusions : Regeneration of periodontal ligament cells using tilapia scale collagen can be done using bone graft techniques. Fish scales have many benefits apart from having almost the same content as humans as well as materials that are still easy to obtain and a more economical price to use. The authors suggest that the researchers further conduct further research on the preparation of tilapia scales so that they can be applied in tissue engineering actions in the field of periodonsia.

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Collagen fibrillogenesis in vitro: interaction of types I and V collagen

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100142670 ◽

1986 ◽

Vol 44 ◽

pp. 210-211

Author(s):

Arthur J. Wasserman ◽

Kathy C. Kloos ◽

David E. Birk

Keyword(s):

Type I Collagen ◽

Corneal Stroma ◽

Minor Component ◽

Homogeneous Distribution ◽

Type I ◽

Type V Collagen ◽

Fibril Morphology ◽

Type V ◽

In Vitro Interaction

Type I collagen is the predominant collagen in the cornea with type V collagen being a quantitatively minor component. However, the content of type V collagen (10-20%) in the cornea is high when compared to other tissues containing predominantly type I collagen. The corneal stroma has a homogeneous distribution of these two collagens, however, immunochemical localization of type V collagen requires the disruption of type I collagen structure. This indicates that these collagens may be arranged as heterpolymeric fibrils. This arrangement may be responsible for the control of fibril diameter necessary for corneal transparency. The purpose of this work is to study the in vitro assembly of collagen type V and to determine whether the interactions of these collagens influence fibril morphology.

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