Biological collagen

Schofer, M.D., et al., 2009. Influence of nanofibres on the growth and osteogenic differentiation of stem cells a comparison of biological collagen nanofibers and synthetic PLLA fibers. Journal of Materials Science-Materials in Medicine 20 (3), 767—774. 

Prockop, D.J., Kivirikko, K.l. Collagens molecular biology, diseases and potentials for therapy. Annu. Rev. 

Nagata, K., Saga, S. Yamada, K.M. (1986). A major collagen-binding protein of chick embryo fibroblasts is a novel heat shock protein. Journal of Cell Biology, 103, 223-9. 

Self-assembling systems made of proteins provide many biological systems with essential structural elements, including viral envelopes, bacterial S-layers, microtubules, collagens, and keratins (see Ref. 6 for a review). Detailed studies on in vitro self-assembly optimization were carried out for several systems as a part of an ongoing effort to elucidate the in vivo mechanism. Data reported from such studies may provide an optional basis for the design and in vitro fabrication of nanostructures made of natural proteins (Fig. 1). 

The complex series of events in collagen maturation provide a model that illustrates the biologic consequences of incomplete polypeptide maturation. The best-known defect in collagen biosynthesis is scurvy, a result of a dietary deficiency of vitamin C required by... 

Silk fibroin and collagen illustrate the close linkage of protein stmcture and biologic function. Diseases of collagen mamration include Ehlers-Danlos syndrome and the vitamin C deficiency disease scurvy. 

Many other peptides are synthesized as proproteins that require modifications before attaining biologic activity. Many of the posttranslational modifications involve the removal of amino terminal amino acid residues by specific aminopeptidases. Collagen, an abundant protein in the extracellular spaces of higher eukaryotes, is synthesized as procollagen. Three procol-... 

Prockop DJ, Kivirikko KI Collagens molecular biology, diseases, and potential therapy. Annu Rev Biochem 1995 64 403. 

Chromium is also important in converting animal hides into leather. In the tanning process, hides are treated with basic solutions of Cr(HI) salts, which causes cross-linking of collagen proteins. The hides toughen and become pliable and resistant to biological decay. 

Proteins, the main constituents of the animals body, are polypeptides, biopolymers consisting of many amino acid molecules (the monomers) combined together (see Chapter 11) collagen, for example, the main component of animal skin, is a complex protein consisting of many molecules of amino acids combined together into polypeptide chains (see Fig. 71). Polysaccharides, the essential constituents of plants, also consist of many monosaccharide molecules combined together. Cellulose, the most abundant biological material on earth, which makes up most of the structural... 

All the tannins readily react with proteins, forming insoluble, stable compounds when they react with collagen, the main constituent of animal skin, they form leather, a material that is resistant to hydrolysis, oxidation, and biological attack and therefore stable to weathering and resistant to decomposition. Since tannins from different plant sources have different chemical compositions, each tannin used for tanning skin produces a leather having slightly different properties and color. Tannins that have... 

Cox, G.N. (1990) Molecular biology of the cuticle collagen gene families of Caenorhabditis elegans and Haemonchus contortus. Acta Tropica 47, 269-281. 

Cox, G.N. and Hirsh, D. (1985) Stage-specific patterns of collagen gene-expression during development of Caenorhabditis elegans. Molecular and Cellular Biology 5, 363-372. 

Kivirikko, K.I. and Pihlajaniemi, T. (1998) Collagen hydroxylases and the protein disulfide isomerase subunit of prolyl 4-hydroxylases. Advances inEnzymology and Related Areas of Molecular Biology 72, 325-400. 

Lamberg, A., Helaakoski, T., Myllyharju, J., Peltonen, S., Notbohm, H., Pihlajaniemi, T. and Kivirikko, K.I. (1996) Characterization of human type III collagen expressed in a baculovirus system - production of a protein with a stable triple helix requires coexpression with the two types of recombinant prolyl 4-hydroxylase subunit.Journal of Biological Chemistry 271, 11988-11995. 

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