ArticleBiological psychiatry2020
Neuroprotective Peptide NAPVSIPQ Antagonizes Ethanol Inhibition of L1 Adhesion by Promoting the Dissociation of L1 and Ankyrin-G.
Article in Biological psychiatry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 11 citations in OpenAlex.
- ADNP Functions During Early Brain Development and Their Relevance to ASD and ADNP Syndrome.International journal of molecular sciences · 2026Review
- Article
- Altered Expression of Neuroplasticity-Related Genes in Alcohol Addiction and Treatment.International journal of molecular sciences · 2024Article
- An overview of current advances in perinatal alcohol exposure and pathogenesis of fetal alcohol spectrum disorders.Journal of neurodevelopmental disorders · 2024Review
- Fetal alcohol spectrum disorders.Nature reviews. Disease primers · 2023Review
- Vineland Adaptive Behavior Scale in a Cohort of Four ADNP Syndrome Patients Implicates Age-Dependent Developmental Delays with Increased Impact of Activities of Daily Living.Journal of molecular neuroscience : MN · 2022Article
- Altering Cell-Cell Interaction in Prenatal Alcohol Exposure Models: Insight on Cell-Adhesion Molecules During Brain Development.Frontiers in molecular neuroscience · 2021Review
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
backgroundEthanol causes developmental neurotoxicity partly by blocking adhesion mediated by the L1 neural cell adhesion molecule. This action of ethanol is antagonized by femtomolar concentrations of the neuropeptide NAPVSIPQ (NAP), an active fragment of the activity-dependent neuroprotective protein (ADNP). How femtomolar concentrations of NAP antagonize millimolar concentrations of ethanol is unknown. L1 sensitivity to ethanol requires L1 association with ankyrin-G; therefore, we asked whether NAP promotes the dissociation of ankyrin-G and L1.
methodsL1-ankyrin-G association was studied using immunoprecipitation, Western blotting, and immunofluorescence in NIH/3T3 cells transfected with wild-type and mutated human L1 genes. Phosphorylation of the ankyrin binding motif in the L1 cytoplasmic domain was studied after NAP treatment of intact cells, rat brain homogenates, and purified protein fragments.
resultsFemtomolar concentrations of NAP stimulated the phosphorylation of tyrosine-1229 (L1-Y1229) at the ankyrin binding motif of the L1 cytoplasmic domain, leading to the dissociation of L1 from ankyrin-G and the spectrin-actin cytoskeleton. NAP increased the association of L1 and EphB2 and directly activated EphB2 phosphorylation of L1-Y1229. These actions of NAP were reproduced by P7A-NAP, a NAP variant that also blocks the teratogenic actions of ethanol, but not by I6A-NAP, which does not block ethanol teratogenesis as potently. Finally, knockdown of EPHB2 prevented ethanol inhibition of L1 adhesion in NIH/3T3 cells.
conclusionsNAP potently antagonizes ethanol inhibition of L1 adhesion by stimulating EphB2 phosphorylation of L1-Y1229. EphB2 plays a critical role in synaptic development; its potent activation by NAP suggests that ADNP may mediate synaptic development partly by activating EphB2.
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