Abstract
SYNAPSE formation requires a complex interchange of information between the pre- and postsynaptic partners. At the skeletal neuro-muscular junction, some of this information is contained in the basal lamina (BL), which runs through the synaptic cleft between the motor nerve terminal and the muscle fibre. During regeneration following injury, components of synaptic BL can trigger several features of postsynaptic differentiation in the absence of the nerve terminal, and of presynaptic differentiation in the absence of the muscle fibre1–3. One nerve-derived component of synaptic BL, agrin, is known to affect postsynaptic differentiation3, but no muscle-derived components have yet been shown to influence motor nerve terminals. A candidate for such a role is s-laminin (also called laminin β2), a homologue of the Bl (β1) chain of the widely distributed BL glycoprotein, laminin30. s-laminin is synthesized by muscle cells5 and concentrated in synaptic BL4. In vitro, recombinant s-laminin fragments are selectively adhesive for motor neuron-like cells, inhibit neurite outgrowth promoted by other matrix molecules, and act as a 'stop signal' for growing neurites6,7. By generating and characterizing mice with a targeted mutation of the S-laminin gene, we show here that s-laminin regulates formation of motor nerve terminals.
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References
Sanes, J. R., Marshall, L. M. & McMahan, U. J. J. Cell Biol. 78, 176–198 (1978).
Burden, S. J., Sargent, P. B. & McMahan, U. J. J. Cell Biol. 82, 412–425 (1979).
Hall, Z. W. & Sanes, J. R. Cell 72/Neuron 10 (suppl.) 99–121 (1993).
Sanes, J. R., Engvall, E., Butkowski, R. & Hunter, D. D. J. Cell Biol. 111, 1685–1699 (1990).
Green, T. L., Hunter, D. D., Chan, W., Merlie, J. P. & Sanes, J. R. J. biol. Chem. 267, 2014–2022 (1992).
Hunter, D. D. et al. Cell 59, 905–913 (1989).
Porter, B. E., Weis, J. & Sanes, J. R. Neuron (in the press).
Merlie, J. P. & Sanes, J. R. Nature 317, 66–68 (1985).
Karnovsky, M. J. J. Cell Biol. 23, 217–232 (1964).
Gurney, M. E., Yamamoto, H. & Kwon, Y. J. Neurosci. 12, 3241–3247 (1992).
Bailce-Gordon, R. J. & Lichtman, J. W. J. Neurosci. 13, 834–855 (1993).
Balice-Gordon, R. J., Chua, C. K., Nelson, C. C. & Lichtman, J. W. Neuron 11, 801–815 (1993).
Gu, Y. & Hall, Z. W. Neuron 1, 117–125 (1988).
Covault, J. & Sanes, J. R. J. Cell Biol. 102, 716–730 (1986).
Greengard, P., Valtorta, F., Czernik, A. J. & Benfenati, F. Science 259, 708–784 (1993).
Hirokawa, N., Sobue, K., Kanda, K., Harada, A. & Yorifuji, H. J. Cell Biol. 108, 111–126 (1989).
Rosahl, T. W. et al. Cell 75, 661–670 (1993).
Hutchinson, D. O. et al. Brain 116, 633–653 (1993).
Jirmanová, I. J. Neurocyt. 4, 141–155 (1975).
Inoue, A., Obata, K. & Akagawa, K. J. biol. Chem. 267, 10613–10619 (1992).
Buckley, K. & Kelly, R. B. J. Cell Biol. 100, 1284–1294 (1985).
Südhof, T. C., Lottspeich, F., Greengard, P., Ehrenfried, M. & Jahn, R. Science 238, 1142–1144 (1987).
Matthew, W. D., Tsavaler, L. & Reichardt, L. F. J. Cell Biol. 91, 257–269 (1981).
Scott, L. J. C., Bacou, F. & Sanes, J. R. J. Neurosci. 8, 932–944 (1988).
Miner, J. H. & Sanes, J. R. J. Cell Biol. 127, 879–891 (1994).
Phillips, W. D., Maimone, M. M. & Merlie, J. P. J. Cell Biol. 115, 1713–1723 (1991).
Ervasti, J. M. & Campbell, K. P. Cell 66, 1121–1131 (1991).
McMahan, A. P. & Bradley, A. Cell. 62, 1073–1085 (1990).
Nagy, A., Rossant, J., Nagy, T., Abramow-Newerly, W. & Roder, J. C. Proc. natn. Acad. Sci. U.S.A. 90, 8424–8428 (1993).
Hunter, D. D., Shah, V., Merlie, J. P. & Sanes, J. R. Nature 338, 229–234 (1989).
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Noakes, P., Gautam, M., Mudd, J. et al. Aberrant differentiation of neuromuscular junctions in mice lacking s-laminin/laminin β2. Nature 374, 258–262 (1995). https://doi.org/10.1038/374258a0
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DOI: https://doi.org/10.1038/374258a0
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