Abstract
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.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
Similar content being viewed by others
References
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.
Beck, K. (1989). Structural model of vinculin: correlation of amino acid sequence with electron-microscopical shape. FEBS Lett., 249: 1–4.
Beck, K., Hunter, I., and Engel, J. (1990). Structure and function of laminin: anatomy of a multidomain glycoprotein. FASEB J., 4: 148–160.
Bruch, M., Landwehr, R., and Engel, J. (1989). Dissection of laminin by cathepsin G into its long arm and short arm structures and localization of regions involved in calcium dependent stabilization and self-association. Eur. J. Biochem., 185: 271–279.
Chiquet, M. (1989). Tenascin J1 cytotactin: the potential function of hexabrachion proteins in neural development. Dev. Neurosci., 11: 266–275.
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.
Chiquet-Ehrismann, R., Kalla, P., Pearson, C. A., Beck, K., and Chiquet, M. (1988). Tenascin interferes with fibronectin action. Cell, 53: 383–390.
Chiquet-Ehrismann, R., Mackie, E. J., Pearson, C. A., and Sakakura, T. (1986). Tenascin: an extracellular matrix protein involved in tissue interactions during fetal development and oncogenesis. Cell, 47: 131–139.
Conway, J. E and Parry, D. A. D. (1990). Structural features in the heptad substructure and longer range repeats of two stranded a-fibrous proteins. Int. J. Biol. Macromol., 12: 328–334.
Cooke, R. M., Wilkinson, A. J., Baron, M., Pastore, A., Tappin, M. J., Campbell, I. D., Gregory, H., and Sheard, B. (1987). The solution structure of human epidermal growth factor. Nature, 327: 339–341.
Dang, C. V., Ebert, R. F., and Bell, W. R. (1985). Localization of a fibrinogen calcium binding site between 7-subunit positions 311 and 336 by terbium fluorescence. J. Biol. Chem., 260: 9713–9719.
Deutzmann, R., Huber, H., Schmetz, K. A., OberMumer, I., and Hartl, L. (1988). Structural study of long arm fragments of laminin. evidence for repetitive C- terminal sequences in the A-chain, not present in the B-chains. Eur. J. Biochem., 177: 35–45.
Doolittle, R. F. (1984). Fibrinogen and fibrin. Annu. Rev. Biochem., 53: 195–229.
Ekblom, P. (1989). Developmentally regulated conversion of mesenchyme to epithelium. EASES J., 3: 2141–2150.
Engel, J. (1989). EGF-like domains in extracellular matrix proteins: localized signals for growth and differentiation? FEBS Lett., 251: 1–7.
Engel, J. and Furthmayr, H. (1987). Electron microscopy and other physical methods for the characterization of extracellular matrix components: laminin, fibronectin, collagen IV, collagen VI, and proteoglycans. Methods Enzymol., 145: 3–78.
Engel, J., Odermatt, E., Engel, A., Madri, J. A., Furthmayr, H., Rohde, H., and Umpl, R. (1981). Shapes, domain organization and flexibility of laminin and fibronectin, two multifunctional proteins of the extracellular matrix. J. Mol Biol., 120: 97–120.
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.
Erickson, H. P. and Bourdon, M. A. (1989). Tenascin: an extracellular matrix protein prominent in specialized embryonic tissues and tumors. Annu. Rev. Cell Biol., 5: 71–92.
Erickson, H. P. and Inglesias, J. L. (1984). A six-armed oligomer isolated from cell surface fibronectin preparations. Nature, 311: 267–269.
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.
Friedlander, D. R., Hoffman, S., and Edelman, D. M. (1988). Functional mapping of cytotactin: proteolytic fragments active in cell substrate adhesion. J. Cell Biol., 107: 2329–2340.
Gershagen, S., Fernlund, P., and Lundwall, A. (1987). A cDNA coding for human sex hormone binding globulin, homology to vitamin K-dependent protein S. FEBS Lett., 220: 129–135.
Graf, J., Iwamoto, Y., Sasaki, M., Martin, G. R., Kleinman, H. K., Robey, F. A., and Yamada, Y. (1987). Identification of an amino acid sequence in laminin mediating cell attachment, chemotaxis and receptor binding. Cell, 48: 989–996.
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.
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.
Hunter, D. D., Shah, V., Merlie, J. P., and Sanes, J. R. (1989). A laminin-like adhesive protein concentrated in the synaptic cleft of the neuromuscular junction. Nature, 338: 229–234.
Jones, F. S., Hoffman, S., Cunningham, B. A., and Edelman, G. M. (1989). A detailed structural model of eytotactin: protein homologies, alternative splicing, and binding regions. Proc. Natl Acad. Sci. USA, 86: 1905–1909.
Koyama, T., Hall, L. R., Haser, W. G., Tonegawa, S., and Saito, H. (1987). Structure of a cytotactic T-lymphocyte-specific gene shows a strong homology to fibrinogen β3 and γ chains. Proc. Natl Acad. Sci. USA, 84: 1609–1613.
Labeit, S., Barlow, D. R, Gautel, M., Gibson, T., Holt, J., Hsieh, C.-L., Francke, U., Leonard, K., Wardale, J., Whiting, A., and Trinick, J. (1990). A regular pattern of two types of 100-residue motif in the sequence of titin. Nature, 345: 273 — 276.
Masuda-Nakagawa, L., Beck, K., and Chiquet, M. (1989). Identification of molecules in leech extracellular matrix that promote neurite outgrowth. Proc. R. Soc. Lond. B, 235: 247–257.
Morel, Y., Bristow, J., Gitelman, S. E., and Miller, W. L. (1989). Transcript encoded on the opposite strand of the human steroid 21-hydroxylase complement component C4 gene locus. Proc. Natl Acad. Sci. USA, 86: 6582–6586.
Nave, R., Fiirst, D. O., and Weber, K. (1989). Visualization of the polarity of isolated titin molecules: a single globular head on a long thin rod as the M-band anchoring domain? J. Cell Biol, 109: 2177–2187.
Norton, R A., Hynes, R. O., and Rees, D. J. G. (1990). Sevenless: seven found? Cell, 61: 15–16.
Panayotou, G., End, P., Aumailley, M., Timpl, R., and Engel, J. (1989). Domains of laminin with growth–factor activity. Cell, 56: 93–101.
Parry, D. A. D. (1982). Coiled-coils in a-helix containing proteins: analysis of the residue types within the heptad repeat and the use of these data in the prediction of coiled-coils in other proteins. Biosci. Rep., 2: 1017–1024.
Patthy, L. (1990). Homology of a domain of the growth hormone/prolactin receptor family with type HI modules of fibronectin. Cell, 61: 13–14.
Paulsson, M., Deutzmann, R., Timpl, R., Dalzoppo, D., Odermatt, E., and Engel, J. (1985). Evidence for coiled-coil a-helical regions in the long arm of laminin. EMBO J., 4: 309–316.
Spring, J., Beck, K., and Chiquet-Ehrismann, R. (1989). Two contrary functions of tenascin: dissection of the active sites by recombinant tenascin fragments. Cell, 59: 325–334.
Szebenyi, D. M. E. and Moffat, K. (1986). The refined structure of vitamin D-dependent calcium-binding protein from bovine intestine. Molecular details, ion binding, and implications for the structure of other calcium-binding proteins. J. Biol. Chem., 261: 8761–8777.
Timpl, R. (1989). Structure and biological activity of basement membrane proteins. Eur. J. Biochem., 180: 487–502.
Timpl, R., Aumailley, M., Gerl, M., Mann, K., Nurcombe, V., Edgar, D., and Deutzmann, R. (1990). Structure and function of the laminin–nidogen complex. Ann. N. Y. Acad. Set., 580: 311–323.
Xu, X. and Doolittle, R. F. (1990). Presence of a vertebrate fibrinogen-like sequence in an echinoderm. Proc. Natl. Acad. Sci. USA, 87: 2097–2101.
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1992 Springer-Verlag Berlin Heidelberg
About this paper
Cite this paper
Beck, K., Spring, J., Chiquet-Ehrismann, R., Engel, J., Chiquet, M. (1992). Structural Motifs of the Extracellular Matrix Proteins Laminin and Tenascin. In: Taylor, W.R. (eds) Patterns in Protein Sequence and Structure. Springer Series in Biophysics, vol 7. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-76637-4_21
Download citation
DOI: https://doi.org/10.1007/978-3-642-76637-4_21
Publisher Name: Springer, Berlin, Heidelberg
Print ISBN: 978-3-642-76639-8
Online ISBN: 978-3-642-76637-4
eBook Packages: Springer Book Archive