Characterization of recombinant humanized collagen type III and its influence on cell behavior and phenotype

Abstract

Collagen made a tremendous impact in the field of regenerative medicine as a bioactive material. For decades, collagen has been used not only as a scaffolding material but also as an active component in regulating cells' biological behavior and phenotype. However, animal-derived collagen as a major source suffered from problems of immunogenicity, risk of viral infection, and the unclear relationship between bioactive sequence and function. Recombinant humanized collagen (rhCol) provided alternatives for regenerative medicine with more controllable risks. However, the characterization of rhCol and the interaction between rhCol and cells still need further investigation, including cell behavior and phenotype. The current study preliminarily demonstrated that recombinant humanized collagen type III (rhCol III) conformed to the theoretical amino acid sequence and had an advanced structure resembling bovine collagen. Furthermore, rhCol III could facilitate basal biological behaviors of human skin fibroblasts, such as adhesion, proliferation and migration. rhCol III was beneficial for some extracellular matrix-expressing cell phenotypes. The study would shed light on the mechanism research of rhCol and cell interactions and further understanding of effectiveness in tissue regeneration. Graphical abstract

Proteomic Identification and Characterization of Collagen from Bactrian Camel (Camelus bactrianus) Hoof

“…The intersection of G and G gradually increased with increasing concentration, and the corresponding frequencies were mainly distributed in 14.68-21.54, 14.68-21.54 Hz, 31.62-46.42 Hz, 46.42-68.13 Hz, and 46.42-68.13 Hz. The findings were superior to earlier studies on bovine collagen [21], which could be attributed to the camel's colossal body weight, hostile environment, camel hoof protein composition, and molecular structure [11]. Figure 6c shows the changes in tan δ as a function of frequency.…”

“…Type I collagen is mainly involved in forming protofibrils in tendons, ligaments, and bones [19]. Type III collagen and type VI collagen are primarily associated with developing type III and V collagen trimers and assembling collagen fibers and other multimeric structures [20,21]. The CHC had the highest percentage (Figure 1) of type I collagen (48.85% for IBAQ), followed by type III collagen (α1) and type VI collagen (α1, α2, α3).…”

Components and physical properties of hydrogels modulate inflammatory response and cartilage repair

“…Type I collagen (Col I) was prepared in the laboratory. 17 HA-MA and Col-MA were synthesized using a method adapted from Kong et al and Dong et al 14,18 The degree of substitution (DS) of HA-MA and Col-MA was analyzed using 1 H NMR (400 MHz, Bruker/AV11) with D 2 O and DMSO as solvents, respectively. MestReNova was used for data analysis.…”

Structure, extraction, processing, and applications of collagen as an ideal component for biomaterials - a review

“…Specifically, based on the liquid crystal properties of ASC, an artificial stroma was created to promote the adhesion and proliferation of epithelial cells, thereby contributing to corneal recovery [168]. With regards to recombinant collagen, it is commonly manufactured into scaffolds with structured micro-architecture for the regeneration of corneal stroma by facilitating cellular growth and collagen deposition [169]. Common modifications to collagen are used in corneal repair, such as the application of hydroxypropyl methylcellulose to improve light transmittance and refractive indices [170], riboflavin to enhance the biochemical properties [171], and hyaluronic acid to improve biocompatibility [172].…”