Papaverine, a Phosphodiesterase 10A Inhibitor, Ameliorates Quinolinic Acid-Induced Synaptotoxicity in Human Cortical Neurons.
CAMP
Oxidative stress
Papaverine
Phosphodiesterase-10A
Quinolinic acid
Synaptic proteins
Journal
Neurotoxicity research
ISSN: 1476-3524
Titre abrégé: Neurotox Res
Pays: United States
ID NLM: 100929017
Informations de publication
Date de publication:
Aug 2021
Aug 2021
Historique:
received:
12
04
2021
accepted:
22
04
2021
revised:
12
04
2021
pubmed:
30
4
2021
medline:
18
12
2021
entrez:
29
4
2021
Statut:
ppublish
Résumé
Phosphodiesterase-10A (PDE10A) hydrolyse the secondary messengers cGMP and cAMP, two molecules playing important roles in neurodevelopment and brain functions. PDE10A is associated to progression of neurodegenerative diseases like Alzheimer's, Parkinson's, Huntington's diseases, and a critical role in cognitive functions. The present study was undertaken to determine the possible neuroprotective effects and the associated mechanism of papaverine (PAP), a PDE10A isoenzyme inhibitor, against quinolinic acid (QUIN)-induced excitotoxicity using human primary cortical neurons. Cytotoxicity potential of PAP was analysed using MTS assay. Reactive oxygen species (ROS) and mitochondrial membrane potential were measured by DCF-DA and JC10 staining, respectively. Caspase 3/7 and cAMP levels were measured using ELISA kits. Effect of PAP on the CREB, BNDF and synaptic proteins such as SAP-97, synaptophysin, synapsin-I, and PSD-95 expression was analysed by Western blot. Pre-treatment with PAP increased intracellular cAMP and nicotinamide adenine dinucleotide (NAD
Identifiants
pubmed: 33914237
doi: 10.1007/s12640-021-00368-4
pii: 10.1007/s12640-021-00368-4
doi:
Substances chimiques
Phosphodiesterase Inhibitors
0
Papaverine
DAA13NKG2Q
PDE10A protein, human
EC 3.1.4.-
Phosphoric Diester Hydrolases
EC 3.1.4.-
Quinolinic Acid
F6F0HK1URN
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
1238-1250Informations de copyright
© 2021. The Author(s), under exclusive licence to Springer Science+Business Media, LLC, part of Springer Nature.
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