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• W2023642934 endingPage "1269" @default.
• W2023642934 startingPage "1262" @default.
• W2023642934 abstract "Myelin-derived Nogo-A protein limits axonal growth after CNS injury. One domain binds to the Nogo-66 receptor to inhibit axonal outgrowth, whereas a second domain, Amino-Nogo, inhibits axonal outgrowth and cell adhesion through unknown mechanisms. Here, we show that Amino-Nogo inhibition depends strictly on the composition of the extracellular matrix, suggesting that Amino-Nogo inhibits the function of certain integrins. Amino-Nogo inhibition can be partially overcome by antibodies that activate integrin β1 or by the addition of Mn 2+ , an integrin activator. Furthermore, Amino-Nogo reduces focal adhesion kinase activation by fibronectin. Analysis of various cell lines reveals that αvβ3, α5, and α4 integrins are sensitive to Amino-Nogo, but α6 integrin is not. Both αv and α5 integrins have widespread expression in adult brain and are found in axonal growth cones. Thus, inhibition of integrin signaling by Amino-Nogo contributes to the failure of CNS axon regeneration." @default.
• W2023642934 created "2016-06-24" @default.
• W2023642934 creator A5004157906 @default.
• W2023642934 creator A5026147594 @default.
• W2023642934 date "2008-01-30" @default.
• W2023642934 modified "2023-10-18" @default.
• W2023642934 title "The N-Terminal Domain of Nogo-A Inhibits Cell Adhesion and Axonal Outgrowth by an Integrin-Specific Mechanism" @default.
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• W2023642934 doi "https://doi.org/10.1523/jneurosci.1068-07.2008" @default.
• W2023642934 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2856844" @default.
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• W2023642934 hasPublicationYear "2008" @default.
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