The DOI matches its Crossref record; 60 of the 60 references it cites were found in a registry or an index.
Pin1, a new player in the fate of HIF-1α degradation: an hypothetical mechanism inside vascular damage as Alzheimer’s disease risk factor
Open accessAbstract
Aetiology of neurodegenerative mechanisms underlying Alzheimer's disease (AD) are still under elucidation. The contribution of cerebrovascular deficiencies (such as cerebral ischemia/stroke) has been strongly endorsed in recent years. Reduction of blood supply leading to hypoxic condition is known to activate cellular responses mainly controlled by hypoxia-inducible transcription factor-1 (HIF-1). Thus alterations of oxygen responsive HIF-1α subunit in the central nervous system may contribute to the cognitive decline, especially influencing mechanisms associated to amyloid precursor protein (APP) amyloidogenic metabolism. Although HIF-1α protein level is known to be regulated by von Hippel-Lindau (VHL) ubiquitin-proteasome system, it has been recently suggested that glycogen synthase kinase-3β (Gsk-3β) promotes a VHL-independent HIF-1α degradation. Here we provide evidences that in rat primary hippocampal cell cultures, HIF-1α degradation might be mediated by a synergic action of Gsk-3β and peptidyl-prolyl cis/trans isomerase (Pin1). In post-ischemic conditions, such as those mimicked with oxygen glucose deprivation (OGD), HIF-1α protein level increases remaining unexpectedly high for long time after normal condition restoration jointly with the increase of lactate dehydrogenase (LDH) and β-secretase 1 (BACE1) protein expression (70 and 140% respectively). Interestingly the Pin1 activity decreases about 40-60% and Pin1(S16) inhibitory phosphorylation significantly increases, indicating that Pin1 binding to its substrate and enzymatic activity are reduced by treatment. Co-immunoprecipitation experiments demonstrate that HIF-1α/Pin1 in normoxia are associated, and that in presence of specific Pin1 and Gsk-3β inhibitors their interaction is reduced in parallel to an increase of HIF-1α protein level. Thus we suggest that in post-OGD neurons the high level of HIF-1α might be due to Pin1 binding ability and activity reduction which affects HIF-1α degradation: an event that may highlight the relevance of ischemia/HIF-1α as a risk factor in AD pathogenesis.
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Cited by
Blum, J. A., Klemm, S., Shadrach, J. L., Guttenplan, K. A., Nakayama, L., Kathiria, A., Hoang, P. T., Gautier, O., Kaltschmidt, J. A., Greenleaf, W. J., et al. (2021) · Nature Neuroscience · doi:10.1038/s41593-020-00795-0 · Cited by 210
Wang, J., Ethridge, L. E., Mosconi, M. W., White, S. P., Binder, D. K., Pedapati, E. V., Erickson, C. A., Byerly, M. J., & Sweeney, J. A. (2017) · Journal of Neurodevelopmental Disorders · doi:10.1186/s11689-017-9191-z · Cited by 176
Hing, B., Sathyaputri, L., & Potash, J. B. (2018) · American Journal of Medical Genetics Part B: Neuropsychiatric Genetics · doi:10.1002/ajmg.b.32616 · Cited by 137
Albanese, A., Daly, L. A., Mennerich, D., Kietzmann, T., & Sée, V. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms22010268 · Cited by 136
Millan, M. J., Goodwin, G. M., Meyer-Lindenberg, A., & Ove Ögren, S. (2015) · European Neuropsychopharmacology · doi:10.1016/j.euroneuro.2015.01.016 · Cited by 132
Metadata
- Authors
- Lonati, E., Brambilla, A., Milani, C., Masserini, M., Palestini, P., & Bulbarelli, A.
- Venue
- Frontiers in Cellular Neuroscience
- Publisher
- Frontiers Media SA
- Published
- 2014
- Volume
- 8
- Pages
- 1-1
- ISSN
- 1662-5102 (ISSN-L)
- OpenAlex
- W2001809022
- Cited by
- 347
- References
- 60
- FWCI
- 28.77
- Type
- journal article
- Language
- en
- Open access
- gold
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- Lonati, E., Brambilla, A., Milani, C., Masserini, M., Palestini, P., & Bulbarelli, A. (2014). Pin1, a new player in the fate of HIF-1α degradation: an hypothetical mechanism inside vascular damage as Alzheimer’s disease risk factor. Frontiers in Cellular Neuroscience. https://doi.org/10.3389/fncel.2014.00001
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