Extracellular matrix components HAPLN1, Lumican and collagen I cause hyaluronic acid-dependent folding of the developing human neocortex
Open accessAbstract
Neocortical expansion, thought to underlie the cognitive traits unique to humans, is accompanied by cortical folding. This folding starts around gestational week (GW) 20, but what causes it remains largely unknown. Extracellular matrix (ECM) has been previously implicated in neocortical expansion and here we investigate the potential role of ECM in the formation of neocortical folds. We focus on three specific ECM components localized in the human fetal cortical plate (CP): hyaluronan and proteoglycan link protein 1 (HAPLN1), lumican and collagen I (collectively, HLC). Addition of HLC to cultures of human fetal neocortex (11-22 GW) caused local changes in tissue stiffness, induced CP folding, increased CP hyaluronic acid (HA), and required the HA-receptor CD168 and downstream ERK signaling. Importantly, loss of HA reduced HLC-induced and 22 GW physiological nascent folds. This was altered in samples with neurodevelopmental disorders, indicating it may be a useful system to study such disorders.
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Some crucial core matrisome proteins regulating embryonic SVZ expansion and cortex folding are not enriched in the adult NSC niche.
“it is important to note that some of the crucial core matrisome proteins regulating embryonic SVZ expansion and cortex folding are not enriched in the adult NSC niche (Long et al., 2018, Long and Huttner, 2019).”
From Defining the Adult Neural Stem Cell Niche Proteome Identifies Key Regulators of Adult Neurogenesis (2020) · cites this paper as Long et al., 2018
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- Authors
- Long, K. R., Newland, B., Florio, M., Kalebic, N., Langen, B., Kolterer, A., Wimberger, P., & Huttner, W. B.
- Affiliations
- Max Planck Institute of Molecular Cell Biology and Genetics (DE)
- Leibniz Institute of Polymer Research (DE)
- University Hospital Carl Gustav Carus (DE)
- Venue
- Neuron
- Publisher
- Elsevier BV
- Published
- 2018-08
- Volume
- 99
- Issue
- 4
- Pages
- 702-719.e6
- ISSN
- 0896-6273 (ISSN-L)
- OpenAlex
- W2887106193
- Cited by
- 196
- References
- 78
- Citations by year
- 2026: 18 · 2025: 19 · 2024: 27 · 2023: 25 · 2022: 30 · 2021: 28 · 2020: 25 · 2019: 20 · 2018: 4
- FWCI
- 7.10
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Neuron (publishedVersion)
- PubMed (publishedVersion)
- ORCA Online Research @Cardiff (Cardiff University) (acceptedVersion)
- ORCA Online Research @Cardiff (Cardiff University) (submittedVersion, cc-by-nc-nd)
- Research Portal (King's College London) (submittedVersion, cc-by-nc-nd)
- MPG.PuRe (Max Planck Society) (submittedVersion)
- Funders
- Wellcome Trust
- DFG (SFB 655, A2)
- ERC (250197)
- Topics
- Life Sciences › Neuroscience › Developmental Neuroscience › Neurogenesis and neuroplasticity mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Proteoglycans and glycosaminoglycans research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular Mechanics and Interactions
- Keywords
- cortical folding, extracellular matrix, hyaluronic acid, HAPLN1, lumican, type I collagen, cortical plate, tissue stiffness, ERK signaling, neurodevelopmental disorders, gestational age
- MeSH terms
- Lumican, Proteoglycan Link Protein, Animals, Extracellular Matrix, Female, Ferrets, Humans, Hyaluronic Acid, Mice, Inbred C57BL, Organ Culture Techniques, Pregnancy, Proteoglycans, Extracellular Matrix Proteins, Neocortex, Collagen Type I, Fetal Development, Mice
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