Cited by 385Collagen: Extraction and CharacterizationTissue Engineering and Regenerative MedicineSilk-based biomaterials and applications

The application of recombinant human collagen in tissue engineering

Yang, Chunlin, Hillas, Patrick J, B??ez, Julio A, Nokelainen, Minna, Balan, Juliana, Tang, James, Spiro, Robert, Polarek, James W·2004·BioDrugs

Abstract

Collagen is the main structural protein in vertebrates. It plays an essential role in providing a scaffold for cellular support and thereby affecting cell attachment, migration, proliferation, differentiation, and survival. As such, it also plays an important role in numerous approaches to the engineering of human tissues for medical applications related to tissue, bone, and skin repair and reconstruction. Currently, the collagen used in tissue engineering applications is derived from animal tissues, creating concerns related to the quality, purity, and predictability of its performance. It also carries the risk of transmission of infectious agents and precipitating immunological reactions. The recent development of recombinant sources of human collagen provides a reliable, predictable and chemically defined source of purified human collagens that is free of animal components. The triple-helical collagens made by recombinant technology have the same amino acid sequence as human tissue-derived collagen. Furthermore, by achieving the equivalent extent of proline hydroxylation via coexpression of genes encoding prolyl hydroxylase with the collagen genes, one can produce collagens with a similar degree of stability as naturally occurring material. The recombinant production process of collagen involves the generation of single triple-helical molecules that are then used to construct more complex three-dimensional structures. If one loosely defines tissue engineering as the use of…

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Crossref · 10.2165/00063030-200418020-00004

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  • Collagen mimetic peptides and recombinant human collagen offer reduced immunogenicity and antigenicity compared to animal-derived collagen.

    “Collagen mimetic peptides (CMPs) and recombinant human collagen (rhCollagen) offer the benefit of reduced immunogenicity and antigenicity compared to animal-derived collagen, making them less likely to provoke immune responses [37,38,39].”

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Authors
Yang, C., Hillas, P. J., B??ez, J. A., Nokelainen, M., Balan, J., Tang, J., Spiro, R., & Polarek, J. W.
Affiliations
FibroGen (United States) (US)
Corresponding author
Polarek, James W
Venue
BioDrugs
Published
2004
Volume
18
Issue
2
Pages
103-119
ISSN
  • 1172-7039 (ISSN-L)
  • 1173-8804
OpenAlex
W2045285226
Cited by
385
References
1
Citations by year
2026: 15 · 2025: 17 · 2024: 21 · 2023: 27 · 2022: 22 · 2021: 21 · 2020: 19 · 2019: 22 · 2018: 18 · 2017: 22 · 2016: 21 · 2015: 25 · 2014: 11 · 2013: 20 · 2012: 19
FWCI
0.94
Type
journal article
Language
en
Open access
closed
Locations
  • BioDrugs (publishedVersion)
  • PubMed (publishedVersion)
Funders
National Institute of Arthritis and Musculoskeletal and Skin Diseases (AR 45879, R01AR045879)
Topics
  • Physical Sciences › Materials Science › Biomaterials › Collagen: Extraction and Characterization
  • Health Sciences › Medicine › Surgery › Tissue Engineering and Regenerative Medicine
  • Physical Sciences › Materials Science › Biomaterials › Silk-based biomaterials and applications
Keywords
recombinant human collagen, tissue engineering scaffolds, triple-helical collagen, proline hydroxylation, bone regeneration, bone morphogenetic proteins, skin tissue engineering, cartilage tissue engineering, periodontal ligament regeneration, biocompatible scaffolds
MeSH terms
Animals, Biocompatible Materials, Collagen, Humans, Recombinant Proteins, Tissue Engineering

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