Focused ion beam-scanning electron microscopy links pathological myelin outfoldings to axonal changes in mice lacking Plp1 or Mag.
anastomosed axons
axon-glia interaction
axonal diameter
axonal sprouting
focused ion beam-scanning electron microscopy (FIB-SEM)
myelin outfoldings
myelin sheath
neuropathology
oligodendrocyte
spastic paraplegia (SPG)
Journal
Glia
ISSN: 1098-1136
Titre abrégé: Glia
Pays: United States
ID NLM: 8806785
Informations de publication
Date de publication:
Mar 2023
Mar 2023
Historique:
revised:
10
10
2022
received:
11
07
2022
accepted:
17
10
2022
pubmed:
11
11
2022
medline:
25
1
2023
entrez:
10
11
2022
Statut:
ppublish
Résumé
Healthy myelin sheaths consist of multiple compacted membrane layers closely encasing the underlying axon. The ultrastructure of CNS myelin requires specialized structural myelin proteins, including the transmembrane-tetraspan proteolipid protein (PLP) and the Ig-CAM myelin-associated glycoprotein (MAG). To better understand their functional relevance, we asked to what extent the axon/myelin-units display similar morphological changes if PLP or MAG are lacking. We thus used focused ion beam-scanning electron microscopy (FIB-SEM) to re-investigate axon/myelin-units side-by-side in Plp- and Mag-null mutant mice. By three-dimensional reconstruction and morphometric analyses, pathological myelin outfoldings extend up to 10 μm longitudinally along myelinated axons in both models. More than half of all assessed outfoldings emerge from internodal myelin. Unexpectedly, three-dimensional reconstructions demonstrated that both models displayed complex axonal pathology underneath the myelin outfoldings, including axonal sprouting. Axonal anastomosing was additionally observed in Plp-null mutant mice. Importantly, normal-appearing axon/myelin-units displayed significantly increased axonal diameters in both models according to quantitative assessment of electron micrographs. These results imply that healthy CNS myelin sheaths facilitate normal axonal diameters and shape, a function that is impaired when structural myelin proteins PLP or MAG are lacking.
Substances chimiques
Myelin Proteins
0
Myelin-Associated Glycoprotein
0
Plp1 protein, mouse
0
Mag protein, mouse
0
Myelin Proteolipid Protein
0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
509-523Subventions
Organisme : Deutsche Forschungsgemeinschaft
ID : WE 2720/2-2 to HBW
Informations de copyright
© 2022 The Authors. GLIA published by Wiley Periodicals LLC.
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