%0 Journal Article
%T Synthetic scaffolds for musculoskeletal tissue engineering: cellular responses to fiber parameters
%A Dianne Little
%A Thomas Lee Jenkins
%J Archive of "NPJ Regenerative Medicine".
%D 2019
%R 10.1038/s41536-019-0076-5
%X Fibrous proteins of the extracellular matrix. a The basic unit of collagen fibrils is the tropocollagen triple-helix comprised of three ¦Á-chains. Each ¦Á-chain forms a helix where glycine is positioned at every third amino acid, often with glycine-proline-X or glycine-X-hydroxyproline repeats. Tropocollagen molecules form collagen fibrils by binding together in a quarter-stagger pattern that gives collagen its characteristic banding pattern. Collagen fibrils vary in diameter, alignment, and packing depending on the tissue they are found in. b Fibronectin (FN) polypeptide chains are comprised of three variable domains: FNI, FNII, and FNIII. Each polypeptide chain contains 12 FNI domains, 2 FNII domains, and 15¨C17 FNIII domains. Pre-mRNA splicing produces at least 20 variants of the protein in humans. Fibronectin polypeptide chains form a ¡®V¡¯ shape at the C-terminus via two disulfide bonds. Fibronectin is secreted as a globular protein that is stretched by cells into its fibrillar form. c Tenascin fibrils are comprised of varying numbers of heptad repeats, epidermal growth factor (EGF)-like repeats, fibronectin type III (FNIII) domains, and a globular fibrinogen domain capping the C-terminus. Tenascin fibrils bind at the N-terminus to form hexamers and trimers. d Tropoelastin molecules contain alternating hydrophobic domains and crosslinking domains. Elastin fibers are generally relaxed and coiled. Lysyl-oxidase crosslinks the fibers together to form a network. When the tissue is stressed, the elastin uncoils and elongates. e Each laminin contains an ¦Á-chain, a ¦Â-chain, and a ¦Ã-chain. There are five ¦Á-chain, four ¦Â-chain, and three ¦Ã-chain variants. Each chain contains a combination of laminin N-terminal domains, laminin IV type A domains, laminin IV type B domains, and EGF-like repeats. ¦Á-chains contain laminin G-like domains at the C-terminal of the peptide. Laminins form helical glycoproteins composed of three polypeptide chains (¦Á, ¦Â, ¦Ã). There are 15 known combinations of ¦Á-, ¦Â-, and ¦Ã- chains. Three short chains (¦Á, ¦Â, ¦Ã) at the N-terminal interact with the ECM, and a long chain (¦Á) at the C-terminal binds to cell-membrane integrins. Laminin 111 show
%K Tissues
%K Tissue engineering
%K Biomaterials - cells
%U https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6597555/