Abstract
A striking example of topographic specificity in synapse formation is the preferential reinnervation of original synaptic sites on denervated muscle fibres by regenerating motor axons. This specificity is mediated by the basal lamina of the synaptic cleft. A glycoprotein, s-laminin, has now been iden-tified that is selectively associated with synaptic basal lamina and is recognized by motoneurons. Molecular cloning reveals that s-laminin is a novel homologue of laminin, a potent promoter of neurite outgrowth.
This is a preview of subscription content, access via your institution
Access options
Subscribe to this journal
Receive 51 print issues and online access
$199.00 per year
only $3.90 per issue
Buy this article
- Purchase on Springer Link
- Instant access to full article PDF
Prices may be subject to local taxes which are calculated during checkout
Similar content being viewed by others
References
Tello, F. Trab. Lab. Invest. biol. Univ. Madr. 5, 117–149 (1907).
Bennett, M. R. & Pettigrew, A. G. Cold Spring Harb. Symp. quant. Biol. 40, 409–424 (1975).
Sanes, J. R., Marshall, L. M. & McMahan, U. J. J. Cell Biol. 78, 176–198 (1978).
Glicksman, M. & Sanes, J. R. J. Neurocytol. 12, 661–671 (1983).
Sanes, J. R. & Hall, Z. W. J. Cell Biol. 83, 357–370 (1979).
Sanes, J. R. & Chiu, A. Y. Cold Spring Harbor Symp. quant. Biol. 48, 667–678 (1983).
Anderson, M. J. & Fambrough, D. M. J. Cell Biol. 97, 1396–1411 (1983).
Fallon, J. R., Nitkin, R. M., Reist, N. E., Wallace, B. G. & McMahan, U. J. Nature 315, 571–574 (1985).
Sanes, J. R. A. Rev. Neurosci. 12, 521–546 (1989).
Hunter, D. D., Sanes, J. R. & Chiu, A. Y. Soc. Neurosci. Abstr. 13, 375 (1987).
Eldridge, C. F., Sanes, J. R., Chiu, A. Y., Bunge, R. P. & Cornbrooks, C. J. J. Neurocytol. 15, 37–51 (1986).
Fawcett, D. W. Histology (W. B. Saunders, Philadelphia, 1986).
Timpl, R. & Dziadek, M. Int. Rev. exptl Path. 29, 1–112 (1986).
Pilar, G., Landmesser, L. & Burstein, L. J. Neurophysiol. 43, 233–254 (1980).
Covault, J., Cunningham, J. M. & Sanes, J. R. J. Cell Biol. 105, 2479–2488 (1987).
Martin, G. R. & Timpl, R. A. Rev. Cell Biol. 3, 57–85 (1987).
Barlow, D. P., Green, N. M., Kurkinen, M. & Hogan, B. L. M. EMBO J. 3, 2355–2362 (1984).
Sasaki, M., Kato, S., Kohno, K., Martin, G. R. & Yamada, Y. Proc. natn. Acad. Sci. U.S.A. 84, 935–939 (1987).
Pikkarainen, T. et al. J. biol. Chem. 262, 10454–10462 (1987).
Sasaki, M. & Yamada, Y. J. biol. Chem. 262, 17111–17117 (1987).
Pikkarainen, T., Kallunki, T. & Tryggvason, K. J. biol. Chem. 263, 6751–6758 (1988).
Durkin, M. E., Bartos, B. B., Liu, S.-H., Phillips, S. L. & Chung, A. E. Biochemistry 27, 5198–5204 (1988).
Sasaki, M., Kleinman, H. K., Huber, H., Deutzmann, R. & Yamada, Y. J. biol. Chem. 263, 16536–16544 (1988).
Montell, D. J. & Goodman, C. S. Cell 53, 463–473 (1988).
Graf, J. et al. Biochemistry 26, 6900–6904 (1987).
Charonis, A. S. et al. J. Cell Biol. 107, 1253–1260 (1988).
Edgar, D., Timpl, R. & Thoenen, H. EMBO J. 3, 1463–1468 (1984).
Engvall, E. et al. J. Cell Biol. 103, 2457–2465 (1986).
Kornblihtt, A. R., Umezawa, K., Vibe-Pederson, K. & Baralle, F. E. EMBO J. 4, 1755–1759 (1985).
Durkin, M. E. et al. Proc. natn. Acad. Sci. U.S.A. 84, 1570–1574 (1987).
Wood, L., Theriault, N. & Vogeli, G. FEBS Lett. 227, 5–8 (1988).
Santoni, M. J. et al. Nucleic Acids Res. 15, 8621–8641 (1987).
Moos, L. et al. Nature 334, 701–703 (1988).
Pearson, C. A., Pearson, D., Shibahara, S., Hofsteenge, J. & Chiquet-Ehrismann, R. EMBO J. 7, 2977–2981 (1988).
Kubo, T. et al. Eur. J. Biochem. 149, 5–13 (1985).
Frail, D. E. et al. J. biol. Chem. 263, 15602–15607 (1988).
Schumacher, M. et al. Nature 319, 407–409 (1986).
Lee, S. I., Heinemann, S. & Taylor, P. J. biol. Chem. 257, 12283–12291 (1982).
Nitkin, R. M. et al. J. Cell Biol. 105, 2471–2478 (1987).
Rosenberg, A. H. et al. Gene 56, 125–135 (1987).
Mayne, R. & Burgeson, R. E. (eds) Structure and Function of Collagen Types (Academic, New York, 1987).
Buck, C. A. & Horwitz, A. F. A. Rev. Cell Biol. 3, 179–205 (1987).
Lagenaur, C. & Lemmon, V. Proc. natn. Acad. Sci. U.S.A. 84, 7753–7757 (1987).
Covault, J. & Sanes, J. R. J. Cell Biol. 102, 716–730 (1986).
Hunter, D. D. & Nathanson, N. M. J. Neurosci., 6, 3739–3748 (1986).
Towbin, H., Staehlin, T. & Gordon, J. Proc. natn. Acad. Sci. U.S.A. 76, 4350–4354 (1979).
VonHeijne, G. Eur. J. Biochem. 133, 17–21 (1983).
Huynh, T. V., Young, R. A. & Davis, R. N. in DNA Cloning: A Practical Approach (ed. Glover, D. M.) (IRL, Oxford, 1985).
Buonanno, A., Mudd, J., Shah, V. & Merlie, J. P. J. biol. Chem. 261, 16451–16458 (1986).
Sanger, F., Nicklen, S. & Coulson, A. R. Proc. natn. Acad. Sci. U.S.A. 74, 5463–5467 (1977).
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Hunter, D., Shah, V., Merlie, J. et al. A laminin-like adhesive protein concentrated in the synaptic cleft of the neuromuscular junction. Nature 338, 229–234 (1989). https://doi.org/10.1038/338229a0
Received:
Accepted:
Issue Date:
DOI: https://doi.org/10.1038/338229a0
This article is cited by
-
Laminin γ3 plays an important role in retinal lamination, photoreceptor organisation and ganglion cell differentiation
Cell Death & Disease (2018)
-
A novel mutation of laminin β2 (LAMB2) in two siblings with renal failure
European Journal of Pediatrics (2017)
-
Molecular Mechanism of Active Zone Organization at Vertebrate Neuromuscular Junctions
Molecular Neurobiology (2012)
-
A synaptic nidogen: Developmental regulation and role of nidogen-2 at the neuromuscular junction
Neural Development (2008)
-
Laminin beta 2
AfCS-Nature Molecule Pages (2008)
Comments
By submitting a comment you agree to abide by our Terms and Community Guidelines. If you find something abusive or that does not comply with our terms or guidelines please flag it as inappropriate.