Antibody

Chemistry

Tilapia

Type I collagen

Fish <Actinopterygii>

Immune system

Biocompatibility

Biochemistry

Biotechnology

Organic chemistry

Fibroblast

Biology

Endocrinology

Fishery

Aquaculture of tilapia

In vivo

Antigenicity

Immunogenicity

In vitro

Immunology

Polymers

Collagen from fish has been proven to have a low antigenicity that has no difference in the genetic codes compared with mammalian-based collagen. This study was designed to investigate the impact of tilapia skin collagen on immunogenicity and biocompatibility in vivo and in vitro. The structural characteristics of both acid-soluble and pepsin-soluble collagen (ASC and PSC), determined using SDS-PAGE and atomic force microscopy imaging experiments, revealed that the collagen had the basic characteristics of type I collagen (COL-I). The in vitro biocompatibility of the collagens showed good cell proliferation against human foreskin fibroblast (HFF-1) cells. PSC and ASC were considered to be almost non-hemolytic biomaterials with favorable blood compatibility in hemolysis tests. The in vivo antigenicity of the collagen in an ICR mouse model evoked an acceptable specific inflammatory response compared to bovine collagen. The implant's position had developed a complete granulation tissue and the sponge disappeared after 8 weeks. The level of cytokines produced by the COL-I immune response was much lower than bovine collagen, which indicated the appropriate implantable property and biodegradability of the collagens. In conclusion, the tilapia COL-I has a lower immunogenicity with better compatibility than bovine COL-I and is a potential alternative to conventional mammalian collagens in biomedical uses.

Characterization of Immunogenicity Associated with the Biocompatibility of Type I Collagen from Tilapia Fish Skin