Structural Motifs of the Extracellular Matrix Proteins Laminin and Tenascin
Laminin and tenascin are two major extracellular matrix glycoproteins. They both consist of large disulphide-linked subunits composed of multiple structural and functional domains which are reflected in a distinct pattern of sequence motifs. These molecules belong to different protein families for which more and more members are being discovered. Members of these families have been discovered down to the level of Anthomedusae laminin (cf. Beck et al., 1990) and leech tenascin (Masuda-Nakagawa et al., 1989). The molecular structure not only varies considerably between species but for laminin also differences depending on the state of development and tissue origin have been elucidated. Varying numbers of tenascin isoforms generated by alternative splicing are found during development and in different tissues.
KeywordsGlobular Domain Cyanogen Bromide Heptad Repeat Calcium Binding Site Fibronectin Type
Unable to display preview. Download preview PDF.
- Aumailley, M., Gerl, M., Sonnenberg, A., Deutzmann, R., and limpl, R. (1990). Identification of the Arg-Gly-Asp sequence in laminin A chain as a latent cell- binding site being exposed in fragment P1. Identification of the Arg-Gly-Asp sequence in laminin A chain as a latent cell-binding site being exposed in fragment PI. FEBS Lett., 262: 82–86.PubMedCrossRefGoogle Scholar
- Chiquet, M., Schenk, S., Beck, K., Nowotny, N., and Chiquet-Ehrismann, R. (1991). Protein domains of tenascin: the C-terminal 60k fragment binds to heparin and preferentially arise from the large isoform. J. Biol. Chem. Submitted.Google Scholar
- Ekblom, P. (1989). Developmentally regulated conversion of mesenchyme to epithelium. EASES J., 3: 2141–2150.Google Scholar
- Engel, J., Taylor, W., Paulsson, M., Sage, H., and Hogan, B. (1987). Calcium binding domains and calcium induced conformational transition of SPARC BM- 40 osteonectin, an extracellular glycoprotein expressed in mineralized and non-mineralized tissues. Biochemistry, 26: 6958–6965.PubMedCrossRefGoogle Scholar
- Erickson, H. P. and Lightner, V. A. (1988). Hexabrachion protein (tenascin, cytotactin, brachionectin) in connective tissues, embryonic brain and tumors. In Miller, K. R., editor, Advances in Cell Biology, pages 55–90. London, JAI.Google Scholar
- Hautanen, A., Gailit, J., Mann, D. M., and Ruoslahti, E. (1989). Effects of modifications of the RGD sequence and its context on recognition by the fibronectin receptor. J. Cell Biol, 264: 1437–1442.Google Scholar
- Holland, S. K. and Blacke, C. C. F. (1989). Multi–domain proteins: towards complete structures. In Aebi, U. and Engel, J., editors, Cytoskeletal and Extracellular Proteins, pages 137–139. Heidelberg: Springer-Verlag.Google Scholar