Abstract
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.
Highlights
Type I collagen (COL-I) is the most abundant extracellular matrix protein in mammals
On 19 hours (Figure 1(a)), the morphology of cells did not differ in each group, whereas it is evident that more cells attached to P-COL and T-COL substrates
On 44 hours (Figure 1(b)), the cell started to proliferate and spread; cells cultured on P-COL substrate adopted elongated morphology, while those cultured on T-COL exhibited a more polygonal shape; in comparison, much less cells adhered to TCPS, and cells cultured on TCPS were poorly spread, implying immature cellular cytoskeleton assembly
Summary
Type I collagen (COL-I) is the most abundant extracellular matrix protein in mammals. It acts as the mechanical structural support to bone, skin, tendons, ligaments, and blood vessels, and the extracellular cue regulating physiological processes including cell adhesion, proliferation, and differentiation [1, 2]. COL-I is able to interact with other extracellular matrix proteins and facilitate mineralization [9, 10]. Amino acid composition of COL-1 varies between species; for example, bird feet collagen contains higher glutamic acid (Glu) and aspartic acid (Asp), while shark skin collagen contains lower aspartic acid and hydroxyproline (Hyp) [12]. Marine collagen types contain lower amount of Hyp and c3o0n.0s∘eCq)u[e1n3t]lyaslocwomerpdaernedatutoramtiaomn mtemalipaenractoullraeg(eTnmt)yp(2e5s..0∘C–
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