Tyrosine Hydroxylase Is Short-Term Regulated by the Ubiquitin-Proteasome System in PC12 Cells and Hypothalamic and Brainstem Neurons from Spontaneously Hypertensive Rats: Possible Implications in Hypertension
Open accessAbstract
Aberrations in the ubiquitin-proteasome system (UPS) are implicated in the pathogenesis of various diseases. Tyrosine hydroxylase (TH), the rate-limiting enzyme in catecholamines biosynthesis, is involved in hypertension development. In this study we investigated whether UPS regulated TH turnover in PC12 cells and hypothalamic and brainstem neurons from spontaneously hypertensive rats (SHR) and whether this system was impaired in hypertension. PC12 cells were exposed to proteasome or lysosome inhibitors and TH protein level evaluated by Western blot. Lactacystin, a proteasome inhibitor, induced an increase of 86 ± 15% in TH levels after 30 min of incubation, then it started to decrease up to 6 h to reach control levels and finally it rose up to 35.2 ± 8.5% after 24 h. Bafilomycin, a lysosome inhibitor, did not alter TH protein levels during short times, but it increased TH by 92 ± 22% above basal after 6 h treatment. Before degradation proteasome substrates are labeled by conjugation with ubiquitin. Efficacy of proteasome inhibition on TH turnover was evidenced by accumulation of ubiquitinylated TH after 30 min. Further, the inhibition of proteasome increased the quantity of TH phosphorylated at Ser40, which is essential for TH activity, by 2.7 ± 0.3 fold above basal. TH protein level was upregulated in neurons from hypothalami and brainstem of SHR when the proteasome was inhibited during 30 min, supporting that neuronal TH is also short-term regulated by the proteasome. Since the increased TH levels reported in hypertension may result from proteasome dysfunction, we evaluate proteasome activity. Proteasome activity was significantly reduced by 67 ± 4% in hypothalamic and brainstem neurons from SHR while its protein levels did not change. Present findings show that TH is regulated by the UPS. The impairment in proteasome activity observed in SHR neurons may be one of the causes of the increased TH protein levels reported in hypertension.
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Short-term inhibition of proteasome increases the accumulation of ubiquitinated TH protein in PC12 cells and brainstem neurons.
“Carbajosa et al. also reported that short-term inhibition of proteasome increases the accumulation of ubiquitinated TH protein in PC12 cells and brainstem neurons [102]”
From Degradation of Tyrosine Hydroxylase by the Ubiquitin-Proteasome System in the Pathogenesis of Parkinson’s Disease and Dopa-Responsive Dystonia (2020) · cites this paper as [102]
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Self-citation
- Authors
- Carbajosa, N. A. L., Corradi, G., Verrilli, M. A. L., Guil, M. J., Vatta, M. S., & Gironacci, M. M.
- Affiliations
- Consejo Nacional de Investigaciones Científicas y Técnicas (AR)
- Corresponding author
- Gironacci, Mariela M.
- Venue
- PLOS ONE
- Publisher
- Public Library of Science (PLoS)
- Published
- 2015-02-24
- Volume
- 10
- Issue
- 2
- Pages
- e0116597
- ISSN
- 1932-6203 (ISSN-L)
- PMC
- PMC4339701
- OpenAlex
- W2008259882
- Cited by
- 27
- References
- 44
- Citations by year
- 2025: 1 · 2024: 2 · 2022: 3 · 2021: 3 · 2020: 3 · 2019: 6 · 2018: 1 · 2017: 2 · 2016: 4 · 2015: 2
- FWCI
- 1.30
- Type
- journal article
- Language
- en
- Update notices
- correction (2015-06-25)
- Open access
- gold
- doi.org
- Licence
- Locations
- PLoS ONE (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Americanae (AECID Library) (submittedVersion, cc-by-nc-sa)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- LA Referencia (Red Federada de Repositorios Institucionales de Publicaciones Científicas) (submittedVersion, cc-by-nc-sa)
- Greater South Information System
- Funders
- Consejo Nacional de Investigaciones Científicas y Técnicas
- Universidad de Buenos Aires (CONICET, 20020120100194)
- Agencia Nacional de Promoción Científica y Tecnológica (PICT-2010-1998, CONICET, PICT 2010)
- Secretaría de Ciencia y Técnica, Universidad de Buenos Aires
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Health Sciences › Medicine › Neurology › Parkinson's Disease Mechanisms and Treatments
- Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
- Keywords
- tyrosine hydroxylase, ubiquitin-proteasome system, proteasome activity, spontaneously hypertensive rats, hypertension, catecholamine synthesis, hypothalamic neurons, brainstem neurons, PC12 cells, lactacystin, bafilomycin, protein turnover
- MeSH terms
- Acetylcysteine, Animals, Brain Stem, Hypertension, Hypothalamus, Male, Neurons, Rats, Inbred SHR, Tyrosine 3-Monooxygenase, PC12 Cells, Rats, Wistar, Ubiquitin, Proteasome Endopeptidase Complex, Rats, Proteasome Inhibitors
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
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