ArticleProceedings of the National Academy of Sciences of the United States of America2008
An alcohol binding site on the neural cell adhesion molecule L1.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.
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Who cites it
44 citing papers in PubMed, 67 citations in OpenAlex.
- The Role of the Immunoglobulin Superfamily of Cell Adhesion Molecules in Intellectual Disability.Cells · 2026Review
- Extracellular Vesicle Phenotypic Trajectories During Alcohol Withdrawal Treatment.International journal of molecular sciences · 2026Article
- Clock Proteins Have the Potential to Improve Term Delivery Date Prediction: A Proof-of-Concept Study.Life (Basel, Switzerland) · 2025Article
- An overview of current advances in perinatal alcohol exposure and pathogenesis of fetal alcohol spectrum disorders.Journal of neurodevelopmental disorders · 2024Review
- Neuronal-specific methylome and hydroxymethylome analysis reveal significant loci associated with alcohol use disorder.Frontiers in genetics · 2024Article
- Neuronal-specific methylome and hydroxymethylome analysis reveal replicated and novel loci associated with alcohol use disorder.medRxiv : the preprint server for health sciences · 2023Article
- Fetal alcohol spectrum disorders.Nature reviews. Disease primers · 2023Review
- Blood Vessels as a Key Mediator for Ethanol Toxicity: Implication for Neuronal Damage.Life (Basel, Switzerland) · 2022Review
- TRPV6 channel mediates alcohol-induced gut barrier dysfunction and systemic response.Cell reports · 2022Article
- Fetal Alcohol Spectrum Disorders: Awareness to Insight in Just 50 Years.Alcohol research : current reviews · 2022Article
- Altering Cell-Cell Interaction in Prenatal Alcohol Exposure Models: Insight on Cell-Adhesion Molecules During Brain Development.Frontiers in molecular neuroscience · 2021Review
- Transcriptome-Wide Regulation of Key Developmental Pathways in the Mouse Neural Tube by Prenatal Alcohol Exposure.Alcoholism, clinical and experimental research · 2020Article
- Effect of ethanol on Munc13-1 C1 in Membrane: A Molecular Dynamics Simulation Study.Alcoholism, clinical and experimental research · 2020Article
- Neuroprotective Peptide NAPVSIPQ Antagonizes Ethanol Inhibition of L1 Adhesion by Promoting the Dissociation of L1 and Ankyrin-G.Biological psychiatry · 2020Article
- SNARE Complex-Associated Proteins and Alcohol.Alcoholism, clinical and experimental research · 2020Review
- Identification of alcohol-binding site(s) in proteins using diazirine-based photoaffinity labeling and mass spectrometry.Chemical biology & drug design · 2019Article
- L1 coupling to ankyrin and the spectrin-actin cytoskeleton modulates ethanol inhibition of L1 adhesion and ethanol teratogenesis.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2018Article
- Base-Mediated One-Pot Synthesis of Aliphatic Diazirines for Photoaffinity Labeling.Molecules (Basel, Switzerland) · 2017Article
- Titrating Tipsy Targets: The Neurobiology of Low-Dose Alcohol.Trends in pharmacological sciences · 2017Review
- Gene-environment interactions in development and disease.Wiley interdisciplinary reviews. Developmental biology · 2017Review
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 1 country.
Funding
Abstract
Prenatal ethanol exposure causes fetal alcohol spectrum disorders (FASD) in part by disrupting the neural cell adhesion molecule L1. L1 gene mutations cause neuropathological abnormalities similar to those of FASD. Ethanol and 1-butanol inhibit L1-mediated cell-cell adhesion (L1 adhesion), whereas 1-octanol antagonizes this action. To test the hypothesis that there are alcohol binding sites on L1, we used 3-azibutanol and 3-azioctanol, the photoactivatable analogs of 1-butanol and 1-octanol, to photolabel the purified Ig1-4 domain of human L1 (hL1 Ig1-4). 3-Azibutanol (11 mM), like ethanol, inhibited L1 adhesion in NIH/3T3 cells stably transfected with hL1, whereas subanesthetic concentrations of 3-azioctanol (14 microM) antagonized ethanol inhibition of L1 adhesion. 3-Azibutanol (100-1,000 microM) and 3-azioctanol (10-100 microM) photoincorporated into Tyr-418 on Ig4 and into two adjacent regions in the N terminus, Glu-33 and Glu-24 to Glu-27. A homology model of hL1 Ig1-4 (residues 33-422), based on the structure of the Ig1-4 domains of axonin-1, suggests that Glu-33 and Tyr-418 hydrogen-bond at the interface of Ig1 and Ig4 to stabilize a horseshoe conformation of L1 that favors homophilic binding. Furthermore, this alcohol binding pocket lies within 7 A of Leu-120 and Gly-121, residues in which missense mutations cause neurological disorders similar to FASD. These data suggest that ethanol or selected mutations produce neuropathological abnormalities by disrupting the domain interface between Ig1 and Ig4. Characterization of alcohol agonist and antagonist binding sites on L1 will aid in understanding the molecular basis for FASD and might accelerate the development of ethanol antagonists.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.