Structure of laminin substrate modulates cellular signaling for neuritogenesis

作者: Elisabete Freire , Flávia CA Gomes , Rafael Linden , Vivaldo Moura Neto , Tatiana Coelho-Sampaio

DOI: 10.1242/JCS.00173

关键词:

摘要: Laminin, a major component of basement membranes, can self-assemble in vitro into typical mesh-like structure, according to mass-action-driven process. Previously, we showed that pH acidification dramatically increased the efficiency laminin self-assembly, practically abolishing the necessity for minimal protein concentration. Here have characterized the morphologies matrices produced in either neutral or acidic conditions and compared their capacities induce neuritogenesis rat embryonic cortical neurons. Although formed buffer presented aggregates heterogeneous morphology, acidic matrix consisted of homogeneous hexagonal sheet-like structure. The latter was comparable to the assembled vivo at inner limiting membrane retina in newborn rats, shown here, secreted by cultivated cells, shown elsewhere. average neurite length neurons plated on acidic matrices 244.9 μm, whereas this value dropped to 104.1 μm. Increased seemed be associated with higher degree neuronal differentiation, since cell proliferation immediately arrested upon plating, neutral matrices, cell number increased six-fold within 24 hours. Investigation of the mechanisms mediating outgrowth each condition revealed the extensive observed involved activation of protein kinase A, moderate was mediated C and/or myosin light-chain kinase. Explants cerebral cortex from P2 rats did not grow laminin substrate but presented extensive migration the acidic matrix. We propose independently of contact assembling mode differentially modulates neuritogenesis neuroplasticity.

参考文章(67)
Peter D. Yurchenco, Maria V. Tsiper, Laminin assembles into separate basement membrane and fibrillar matrices in Schwann cells Journal of Cell Science. ,vol. 115, pp. 1005- 1015 ,(2002) , 10.1242/JCS.115.5.1005
P. Liesi, Do neurons in the vertebrate CNS migrate on laminin The EMBO Journal. ,vol. 4, pp. 1163- 1170 ,(1985) , 10.1002/J.1460-2075.1985.TB03755.X
Hynda K. Kleinman, Benjamin S. Weeks, H. William Schnaper, Maura C. Kibbey, Keizo Yamamura, Derrick S. Grant, The laminins: a family of basement membrane glycoproteins important in cell differentiation and tumor metastases. Vitamins and Hormones Series. ,vol. 47, pp. 161- 186 ,(1993) , 10.1016/S0083-6729(08)60446-X
Christian J. Meyer, Francis J. Alenghat, Paul Rim, Jenny Hwai-Jen Fong, Ben Fabry, Donald E. Ingber, Mechanical control of cyclic AMP signalling and gene transcription through integrins. Nature Cell Biology. ,vol. 2, pp. 666- 668 ,(2000) , 10.1038/35023621
P.D. Yurchenco, Y.S. Cheng, Self-assembly and calcium-binding sites in laminin. A three-arm interaction model. Journal of Biological Chemistry. ,vol. 268, pp. 17286- 17299 ,(1993) , 10.1016/S0021-9258(19)85334-6
P D Yurchenco, E C Tsilibary, A S Charonis, H Furthmayr, Laminin polymerization in vitro. Evidence for a two-step assembly with domain specificity. Journal of Biological Chemistry. ,vol. 260, pp. 7636- 7644 ,(1985) , 10.1016/S0021-9258(17)39656-4
Holly Colognato-Pyke, Julian J. O'Rear, Yoshihiko Yamada, Salvatore Carbonetto, Yi-Shan Cheng, Peter D. Yurchenco, Mapping of Network-forming, Heparin-binding, and α1β1 Integrin-recognition Sites within the α-Chain Short Arm of Laminin-1 (∗) Journal of Biological Chemistry. ,vol. 270, pp. 9398- 9406 ,(1995) , 10.1074/JBC.270.16.9398
Konrad Beck, Irene Hunter, Jürgen Engel, Structure and function of laminin: anatomy of a multidomain glycoprotein The FASEB Journal. ,vol. 4, pp. 148- 160 ,(1990) , 10.1096/FASEBJ.4.2.2404817
Barbara Grimpe, Sucai Dong, Catherine Doller, Katherine Temple, Alfred T. Malouf, Jerry Silver, The Critical Role of Basement Membrane-Independent Laminin γ1 Chain during Axon Regeneration in the CNS The Journal of Neuroscience. ,vol. 22, pp. 3144- 3160 ,(2002) , 10.1523/JNEUROSCI.22-08-03144.2002
Peter D Yurchenco, Yi-Shan Cheng, Holly Colognato, Laminin forms an independent network in basement membranes. Journal of Cell Biology. ,vol. 117, pp. 1119- 1133 ,(1992) , 10.1083/JCB.117.5.1119