The collagens represent a family of trimeric extracellular matrix molecules used by cells for structural integrity and other functions. The three α chains that form the triple helical part of the molecule are composed of repeating peptide triplets of glycine-X-Y. X and Y can be any amino acid but are often proline and hydroxyproline, respectively. Flanking the triple helical regions (i.e., Col domains) are non-glycine-X-Y regions, termed non-collagenous domains. These frequently contain recognizable peptide modules found in other matrix molecules. Proper tissue function depends on correctly assembled molecular aggregates being incorporated into the matrix. This review highlights some of the structural characteristics of collagen types I-XXVIII.
KeywordsCollagens Extracellular matrix Fibrils FACITs Basement membrane
- Boot-Handford RP, Tuckwell DS, Plumb DA, Rock CF, Poulsom R (2003) A novel and highly conserved collagen (pro(alpha)1(XXVII)) with a unique expression pattern and unusual molecular characteristics establishes a new clade within the vertebrate fibrillar collagen family. J Biol Chem 278:31067–31077CrossRefPubMedGoogle Scholar
- Gerecke DR, Olson PF, Koch M, Knoll JH, Taylor R, Hudson DL, Champliaud MF, Olsen BR, Burgeson RE (1997) Complete primary structure of two splice variants of collagen XII, and assignment of alpha 1(XII) collagen (COL12A1), alpha 1(IX) collagen (COL9A1), and alpha 1(XIX) collagen (COL19A1) to human chromosome 6q12-q13. Genomics 41:236–242CrossRefPubMedGoogle Scholar
- Koch M, Laub F, Zhou P, Hahn RA, Tanaka S, Burgeson RE, Gerecke DR, Ramirez F, Gordon MK (2003) Collagen XXIV, a vertebrate fibrillar collagen with structural features of invertebrate collagens: selective expression in developing cornea and bone. J Biol Chem 278:43236–43244CrossRefPubMedGoogle Scholar
- Musso O, Theret N, Heljasvaara R, Rehn M, Turlin B, Campion JP, Pihlajaniemi T, Clement B (2001) Tumor hepatocytes and basement membrane-producing cells specifically express two different forms of the endostatin precursor, collagen XVIII, in human liver cancers. Hepatology 33:868–876CrossRefPubMedGoogle Scholar
- Tuomisto A, Sund M, Tahkola J, Latvanlehto A, Savolainen ER, Autio-Harmainen H, Liakka A, Sormunen R, Vuoristo J, West A, Lahesmaa R, Morse HC 3rd, Pihlajaniemi T (2008) A mutant collagen XIII alters intestinal expression of immune response genes and predisposes transgenic mice to develop B-cell lymphomas. Cancer Res 68:10324–10332CrossRefPubMedGoogle Scholar
- Yamaguchi N, Kimura S, McBride OW, Hori H, Yamada Y, Kanamori T, Yamakoshi H, Nagai Y (1992) Molecular cloning and partial characterization of a novel collagen chain, alpha 1(XVI), consisting of repetitive collagenous domains and cysteine-containing noncollagenous segments. J Biochem 112:856–863PubMedGoogle Scholar