ArticleGlia2025
Myelin Formation by Oligodendrocytes Is Enhanced Through Laminin-411 and Its Derived Peptide.
Article in Glia, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
4 citing papers in PubMed.
- Rapid Generation of Functional Oligodendrocytes From Human Induced Pluripotent Stem Cells Through Small Molecule Guided Differentiation.Journal of neuroscience research · 2026Article
- Molecular Basis of Glia-ECM Interplay in Central Nervous System Homeostasis and Plasticity.Cells · 2026Review
- The role of ECM-PIEZO1-axis-mediated mechanosensation in the central nervous system.Frontiers in neurology · 2026Review
- Blood-spinal cord barrier disruption after spinal cord injury: a time-dependent mechanistic review.Frontiers in cellular neuroscience · 2026Review
Corrections and comments
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Authors and funding
15 authors.
Funding
Abstract
In the central nervous system, oligodendrocytes (OLs) form myelin sheaths that accomplish the efficient transmission of nerve conduction for optimal motor and cognitive functions. OL development and differentiation are regulated by a variety of molecules, including extracellular matrix (ECM) proteins. ECM proteins are also useful as substrates for OL culture. However, the functions of ECM proteins in OL development and myelination remain unclear, and only a limited number of ECM proteins have been characterized and used in in vitro experiments. Here, we investigated the expression and function of laminin (LM) isoforms in OL differentiation and myelination. We found that LM α1, α2, and α4 chains were expressed around blood vessels at the stage of myelination in mice. Functional analyses using recombinant proteins of LM isoforms containing α1, α2, and α4 chains revealed that LM411 and LM411E8, the integrin binding domain of LM411, possessed significant activities in myelin membrane formation of OLs. Furthermore, the peptide A4G47 derived from LM411E8 promoted the activity, which provides evidence of the first peptide in OL myelin formation from ECM proteins. Our findings facilitate a better understanding of ECM functions in OL biology and the development of a new material in OL myelination.
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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.