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- W1971295712 abstract "Myelin is a major obstacle for regenerating nerve fibers of the adult mammalian central nervous system (CNS). Several proteins including Nogo-A, myelin-associated glycoprotein (MAG), oligodendrocyte myelin glycoprotein (OMgp) and the chondroitin-sulfate proteoglycan (CSPG) Versican V2 have been identified as inhibitory components present in CNS myelin. MAG, OMgp as well as the Nogo specific domain Nogo-66 exert their inhibitory activity by binding to a neuronal receptor complex containing the Nogo-66 receptor NgR and the neurotrophin receptor p75NTR. While this suggests a converging role of the p75NTR/NgR receptor complex for myelin-derived neurite growth inhibitors, we show here that NgR/p75NTR is not required for mediating the inhibitory activity of the two myelin components NiG, unlike Nogo-66 a distinct domain of Nogo-A, and Versican V2. Primary neurons derived from a complete null mutant of p75NTR are still sensitive to NiG and Versican V2. In line with this result, neurite growth of p75NTR deficient neurons is still significantly blocked on total bovine CNS myelin. Furthermore, modulation of RhoA and Rac1 in p75NTR−/− neurons persists with NiG and Versican V2. Finally, we demonstrate that neither NiG nor Versican V2 interact with the p75NTR/NgR receptor complex and provide evidence that the binding sites of NiG and Nogo-66 are physically distinct from each other on neural tissue. These results indicate not only the existence of neuronal receptors for myelin inhibitors independent from the p75NTR/NgR receptor complex but also establish Rho GTPases as a common point of signal convergence of diverse myelin-induced regeneration inhibitory pathways." @default.
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- W1971295712 date "1973-08-01" @default.
- W1971295712 modified "2023-10-16" @default.
- W1971295712 title "Protein composition of myelin from brain and spinal cord of several species" @default.
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- W1971295712 doi "https://doi.org/10.1016/0006-8993(73)90023-1" @default.
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