Effect of type I collagen derived from tilapia scale on odontoblast-like cells

Type I collagen (COL-1) is the prevailing component of the extracellular matrix in a number of tissues including skin, ligament, cartilage, bone, and dentin. It is the most widely used tissue-derived natural polymer. Currently, mammalian animals, including pig, cow, and rat, are the three major sources for purification of COL-1. To reduce the risk of zoonotic infectious diseases transmission, minimize the possibility of immunogenic reaction, and avoid problems related to religious issues, exploration of new sources (other than mammalian animals) for the purification of type I collagen is highly desirable. Hence, the purpose of the current study was to investigate the in vitro responses of MDPC-23 to type I collagen isolated from tilapia scale in terms of cellular proliferation, differentiation, and mineralization. The results suggested that tilapia scale collagen exhibited comparable biocompatibility to porcine skin collagen, indicating it might be a potential alternative to type I collagen from mammals in the application for tissue regeneration in oral-maxillofacial area.

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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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