Glypican-1 and α4(V) Collagen Are Required for Schwann Cell Myelination
| Autor: | Richard C. Stahl, David J. Carey, Ann Evans, Katrina Rothblum, Lisa Prentiss, Michael A. Chernousov |
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| Rok vydání: | 2006 |
| Předmět: |
Recombinant Fusion Proteins
Cellular differentiation Development/Plasticity/Repair Schwann cell Transfection Culture Media Serum-Free Extracellular matrix Myelin chemistry.chemical_compound Laminin Ganglia Spinal Cell Adhesion medicine Animals RNA Messenger RNA Small Interfering Cell adhesion Cells Cultured Myelin Sheath Neurons biology General Neuroscience Cell Differentiation Heparan sulfate Sciatic Nerve Coculture Techniques Extracellular Matrix Protein Structure Tertiary Rats Cell biology Collagen type I alpha 1 medicine.anatomical_structure nervous system chemistry biology.protein Schwann Cells Collagen Type V Neuroscience Heparan Sulfate Proteoglycans |
| Zdroj: | The Journal of Neuroscience. 26:508-517 |
| ISSN: | 1529-2401 0270-6474 |
| Popis: | Schwann cell myelination requires interactions with the extracellular matrix (ECM) mediated by cell surface receptors. Previously, we identified a type V collagen family member, alpha4(V) collagen, which is expressed by Schwann cells during peripheral nerve differentiation. This collagen binds with high affinity to heparan sulfate through a unique binding motif in the noncollagenous N-terminal domain (NTD). The principal alpha4(V) collagen-binding protein on the Schwann cell surface is the heparan sulfate proteoglycan glypican-1. We investigated the role of alpha4(V) collagen and glypican-1 in Schwann cell terminal differentiation in cultures of Schwann cells and dorsal root ganglion neurons. Small interfering RNA-mediated suppression of glypican-1 expression decreased binding of alpha4(V)-NTD to Schwann cells, adhesion and spreading of Schwann cells on alpha4(V)-NTD, and incorporation of alpha4(V) collagen into Schwann cell ECM. In cocultures, alpha4(V) collagen coassembles with laminin on the surface of polarized Schwann cells to form tube-like ECM structures that are sites of myelination. Suppression of glypican-1 or alpha4(V) collagen expression significantly inhibited myelination. These results demonstrate an important role for these proteins in peripheral nerve terminal differentiation. |
| Databáze: | OpenAIRE |
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