ArticleThe Biochemical journal2013
Nogo-A couples with Apg-1 through interaction and co-ordinate expression under hypoxic and oxidative stress.
Article in The Biochemical journal, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 17 citations in OpenAlex.
- Investigating molecular background of multiple sclerosis through multi-omics: linking via psychoneuroimmunology.Acta neurologica Belgica · 2025Article
- The Overexpression of RTN4 Significantly Associated With an Unfavourable Prognosis in Patients With Lower-Grade Gliomas.Journal of cellular and molecular medicine · 2025Article
- Amino-terminal proteolytic fragment of the axon growth inhibitor Nogo-A (Rtn4A) is upregulated by injury and promotes axon regeneration.The Journal of biological chemistry · 2023Article
- Nogo-A/NgR signaling regulates stemness in cancer stem-like cells derived from U87MG glioblastoma cells.Oncology letters · 2022Article
- New insights in ferroptosis: Potential therapeutic targets for the treatment of ischemic stroke.Frontiers in pharmacology · 2022Review
- Article
- Nogo-A expression dynamically varies after spinal cord injury.Neural regeneration research · 2015Article
- Cell type-specific Nogo-A gene ablation promotes axonal regeneration in the injured adult optic nerve.Cell death and differentiation · 2015Article
- Impacts of Rho kinase inhibitor Fasudil on Rho/ROCK signaling pathway in rabbits with optic nerve injury.International journal of clinical and experimental pathology · 2015Article
- Article
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Authors and funding
10 authors at 2 institutions in 2 countries.
Funding
Abstract
Nogo-A is the largest isoform of the Nogo/RTN4 (reticulon 4) proteins and has been characterized as a major myelin-associated inhibitor of regenerative nerve growth in the adult CNS (central nervous system). Apart from the myelin sheath, Nogo-A is expressed at high levels in principal neurons of the CNS. The specificity of Nogo-A resides in its central domain, NiG. We identified Apg-1, a member of the stress-induced Hsp110 (heat-shock protein of 110 kDa) family, as a novel interactor of NiG/Nogo-A. The interaction is selective because Apg-1 interacts with Nogo-A/RTN4-A, but not with RTN1-A, the closest paralogue of Nogo-A. Conversely, Nogo-A binds to Apg-1, but not to Apg-2 or Hsp105, two other members of the Hsp110 family. We characterized the Nogo-A-Apg-1 interaction by affinity precipitation, co-immunoprecipitation and proximity ligation assay, using primary hippocampal neurons derived from Nogo-deficient mice. Under conditions of hypoxic and oxidative stress we found that Nogo-A and Apg-1 were tightly co-regulated in hippocampal neurons. Although both proteins were up-regulated under hypoxic conditions, their expression levels were reduced upon the addition of hydrogen peroxide. Taken together, we suggest that Nogo-A is closely involved in the neuronal response to hypoxic and oxidative stress, an observation that may be of relevance not only in stroke-induced ischaemia, but also in neuroblastoma formation.
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