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Cited by 2Hereditary Neurological DisordersPeripheral Neuropathies and DisordersCancer Treatment and Pharmacology

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Aberrant Molecular Myelin Architecture in Charcot–Marie–Tooth Disease Type 1A and Hereditary Neuropathy With Liability to Pressure Palsies

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Moss, Kathryn R., Arowolo, Marvis A., Gutierrez, Dave R., Höke, Ahmet·2026·Glia
DOI 10.1002/glia.70124PMC PMC12706824

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Abstract

Charcot–Marie–Tooth Disease Type 1A (CMT1A) and Hereditary Neuropathy with Liability to Pressure Palsies (HNPP) are the most common inherited peripheral neuropathies and arise from copy number variation of the Peripheral Myelin Protein 22 ( PMP22 ) gene. While secondary axon degeneration has been proposed as the primary driver of disability, our prior work demonstrated pronounced neuromuscular impairment in CMT1A model mice in the absence of overt axonal loss, prompting investigation into primary myelin dysfunction. Here, we reveal that altered PMP22 dosage profoundly disrupts molecular architecture at critical myelin domains, Schmidt‐Lanterman incisures (SLIs) and Nodes of Ranvier. Using high‐resolution confocal imaging of teased peripheral nerve fibers from CMT1A and HNPP model mice, we identified widespread disorganization of adherens junctions, mislocalization of Connexin29 and aberrant distribution of nodal ion channels, with several defects more severe in CMT1A, consistent with disease burden. Notably, nodal widening and abnormal spreading of Kv1.2 and Caspr along internodes indicate compromised axo‐glial compartmentalization essential for saltatory conduction. Together, these findings support a model in which PMP22 functions as a structural organizer of myelin, coordinating adherens junction patterning and nodal subdomain integrity. Dysregulation of this function is predicted to compromise Schwann‐cell architecture, metabolic support and axonal excitability. Our findings support a paradigm shift in which molecular destabilization of myelin, rather than secondary axonal degeneration alone, contributes to disease progression in CMT1A and HNPP. This work also identifies junctional complexes as potential actionable molecular targets and establishes a mechanistic framework applicable to a broad spectrum of inherited dysmyelinating and acquired demyelinating neuropathies.

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Figures

FIGURE 1 PMP22 exhibits structural homology to Claudins suggesting a role in myelin adhesion. (a) PMP22 is a member of the Claudin superfamily of proteins. Orthodox Claudins establish selective barriers as components of tight junctions and as such PMP22 protein topology is homologous. Topology for human PMP22, adapted from (Marinko et al. 2020). (b) AlphaFold predicted structures of human Claudin‐1 and human PMP22 ECLs viewed from above (AlphaFold Protein Structure Database (Jumper et al. 2021)). The structural similarity between the ECLs of human Claudin‐1 and human PMP22 is striking suggesting that PMP22 functions similarly to Claudin proteins. (c) Adhesion junctions, including adherens junctions and tight junctions, are localized to specialized cytoplasmic‐like compartments in peripheral nerve myelin including Schmidt‐Lanterman Incisures (SLIs) and Nodes of Ranvier. Created in https://BioRender.com. (d) 3‐month‐old WT (C57BL/6J) teased tibial nerve fibers immunostained for the adherens junction protein E‐Cadherin (red) showing prominent localization at SLIs (marked by F‐Actin [blue], arrows), Nodes of Ranvier (marked by pan Neurofascin [NF, green], arrowheads) and inner mesaxons. Scale bar, 10 μm.
FIGURE 1 PMP22 exhibits structural homology to Claudins suggesting a role in myelin adhesion. (a) PMP22 is a member of the Claudin superfamily of proteins. Orthodox Claudins establish selective barriers as components of tight junctions and as such PMP22 protein topology is homologous. Topology for human PMP22, adapted from (Marinko et al. 2020). (b) AlphaFold predicted structures of human Claudin‐1 and human PMP22 ECLs viewed from above (AlphaFold Protein Structure Database (Jumper et al. 2021)). The structural similarity between the ECLs of human Claudin‐1 and human PMP22 is striking suggesting that PMP22 functions similarly to Claudin proteins. (c) Adhesion junctions, including adherens junctions and tight junctions, are localized to specialized cytoplasmic‐like compartments in peripheral nerve myelin including Schmidt‐Lanterman Incisures (SLIs) and Nodes of Ranvier. Created in https://BioRender.com. (d) 3‐month‐old WT (C57BL/6J) teased tibial nerve fibers immunostained for the adherens junction protein E‐Cadherin (red) showing prominent localization at SLIs (marked by F‐Actin [blue], arrows), Nodes of Ranvier (marked by pan Neurofascin [NF, green], arrowheads) and inner mesaxons. Scale bar, 10 μm.CC BY · PubMed Central
FIGURE 2 Altered adherens junctions and F‐actin distributions at SLIs in CMT1A and HNPP model peripheral nerve myelin. Representative images of 3‐month‐old (a) WT (C57BL/6J) and CMT1A or (e) WT (129S1/SvImJ) and HNPP teased tibial nerve fibers stained for the adherens junction complex proteins E‐Cadherin (red), β‐Catenin (green) and F‐Actin (blue). Quantification of protein distribution at SLIs (signal volume/fiber diameter) for (b, f) E‐Cadherin, (c, g) β‐Catenin and (d, h) F‐Actin in CMT1A and HNPP, respectively. n = 5 animals (~30 SLIs/animal). Bar graphs represent mean ± SEM with individual data points. Datasets were analyzed with three complementary statistical approaches (unpaired t‐test with all individual data points, unpaired t‐test with experimental means and nested t‐test). ***p < 0.05 demonstrate statistical significance with all three t‐test statistics. Scale bar, 10 μm.
FIGURE 2 Altered adherens junctions and F‐actin distributions at SLIs in CMT1A and HNPP model peripheral nerve myelin. Representative images of 3‐month‐old (a) WT (C57BL/6J) and CMT1A or (e) WT (129S1/SvImJ) and HNPP teased tibial nerve fibers stained for the adherens junction complex proteins E‐Cadherin (red), β‐Catenin (green) and F‐Actin (blue). Quantification of protein distribution at SLIs (signal volume/fiber diameter) for (b, f) E‐Cadherin, (c, g) β‐Catenin and (d, h) F‐Actin in CMT1A and HNPP, respectively. n = 5 animals (~30 SLIs/animal). Bar graphs represent mean ± SEM with individual data points. Datasets were analyzed with three complementary statistical approaches (unpaired t‐test with all individual data points, unpaired t‐test with experimental means and nested t‐test). ***p < 0.05 demonstrate statistical significance with all three t‐test statistics. Scale bar, 10 μm.CC BY · PubMed Central
FIGURE 3 Variable changes in the distribution of p120‐Catenin at SLIs in CMT1A and HNPP model myelin. Representative images of 3‐month‐old (a) WT (C57BL/6J) and CMT1A or (c) WT (129S1/SvImJ) and HNPP teased tibial nerve fibers stained for the adherens junction complex proteins E‐Cadherin (red), p120‐Catenin (green) and F‐Actin (blue). Quantification of p120‐Catenin protein distribution at SLIs (signal volume/fiber diameter) in (b) CMT1A and (d) HNPP. n = 5 animals (~30 SLIs/animal). Bar graphs represent mean ± SEM with individual data points. Datasets were analyzed with three complementary statistical approaches (unpaired t‐test with all individual data points, unpaired t‐test with experimental means and nested t‐test). *p < 0.05 demonstrate statistical significance with a single t‐test statistic. Scale bar, 10 μm.
FIGURE 3 Variable changes in the distribution of p120‐Catenin at SLIs in CMT1A and HNPP model myelin. Representative images of 3‐month‐old (a) WT (C57BL/6J) and CMT1A or (c) WT (129S1/SvImJ) and HNPP teased tibial nerve fibers stained for the adherens junction complex proteins E‐Cadherin (red), p120‐Catenin (green) and F‐Actin (blue). Quantification of p120‐Catenin protein distribution at SLIs (signal volume/fiber diameter) in (b) CMT1A and (d) HNPP. n = 5 animals (~30 SLIs/animal). Bar graphs represent mean ± SEM with individual data points. Datasets were analyzed with three complementary statistical approaches (unpaired t‐test with all individual data points, unpaired t‐test with experimental means and nested t‐test). *p < 0.05 demonstrate statistical significance with a single t‐test statistic. Scale bar, 10 μm.CC BY · PubMed Central
FIGURE 4 Distinct Connexin29 distribution defects but unchanged CADM4 at SLIs in peripheral nerve myelin from CMT1A and HNPP model mice. Representative images of 3‐month‐old (a) WT (C57BL/6J) and CMT1A or (e) WT (129S1/SvImJ) and HNPP teased tibial nerve fibers stained for CADM4 (red), Connexin29 (Cx29, green) and F‐Actin (blue). Note the focal accumulations of Cx29 outside the SLI compartment in CMT1A model myelin (arrowheads). Quantification of protein distribution at SLIs (signal volume/fiber diameter) for (b, f) CADM4 and (c, g) Cx29 in CMT1A and HNPP, respectively. Quantification of mean Cx29 signal intensity at SLIs in (d) CMT1A and (h) HNPP. n = 5 animals (~30 SLIs/animal). Bar graphs represent mean ± SEM with individual data points. Datasets were analyzed with three complementary statistical approaches (unpaired t‐test with all individual data points, unpaired t‐test with experimental means and nested t‐test). ***p < 0.05 demonstrate statistical significance with all three t‐test statistics and *p < 0.05 demonstrate statistical significance with a single t‐test statistic. Scale bars, 10 μm.
FIGURE 4 Distinct Connexin29 distribution defects but unchanged CADM4 at SLIs in peripheral nerve myelin from CMT1A and HNPP model mice. Representative images of 3‐month‐old (a) WT (C57BL/6J) and CMT1A or (e) WT (129S1/SvImJ) and HNPP teased tibial nerve fibers stained for CADM4 (red), Connexin29 (Cx29, green) and F‐Actin (blue). Note the focal accumulations of Cx29 outside the SLI compartment in CMT1A model myelin (arrowheads). Quantification of protein distribution at SLIs (signal volume/fiber diameter) for (b, f) CADM4 and (c, g) Cx29 in CMT1A and HNPP, respectively. Quantification of mean Cx29 signal intensity at SLIs in (d) CMT1A and (h) HNPP. n = 5 animals (~30 SLIs/animal). Bar graphs represent mean ± SEM with individual data points. Datasets were analyzed with three complementary statistical approaches (unpaired t‐test with all individual data points, unpaired t‐test with experimental means and nested t‐test). ***p < 0.05 demonstrate statistical significance with all three t‐test statistics and *p < 0.05 demonstrate statistical significance with a single t‐test statistic. Scale bars, 10 μm.CC BY · PubMed Central
FIGURE 5 Mag exhibits distribution changes similar to Connexin29 whereas Connexin32 mean intensity is reduced at SLIs in CMT1A and HNPP model myelin. Representative images of 3‐month‐old (a) WT (C57BL/6J) and CMT1A or (e) WT (129S1/SvImJ) and HNPP teased tibial nerve fibers stained for (top panels) MAG (green) and F‐Actin (blue) or (bottom panels) Cx32 (green) and F‐Actin (blue). Quantification of (b, f) MAG protein distribution (signal volume/fiber diameter) and (c, f) MAG and (d, h) Cx32 mean signal intensity at SLIs in CMT1A and HNPP, respectively. n = 5 animals (~30 SLIs/animal). Bar graphs represent mean ± SEM with individual data points. Datasets were analyzed with three complementary statistical approaches (unpaired t‐test with all individual data points, unpaired t‐test with experimental means and nested t‐test). *p < 0.05 demonstrate statistical significance with a single t‐test statistic. Scale bars, 10 μm.
FIGURE 5 Mag exhibits distribution changes similar to Connexin29 whereas Connexin32 mean intensity is reduced at SLIs in CMT1A and HNPP model myelin. Representative images of 3‐month‐old (a) WT (C57BL/6J) and CMT1A or (e) WT (129S1/SvImJ) and HNPP teased tibial nerve fibers stained for (top panels) MAG (green) and F‐Actin (blue) or (bottom panels) Cx32 (green) and F‐Actin (blue). Quantification of (b, f) MAG protein distribution (signal volume/fiber diameter) and (c, f) MAG and (d, h) Cx32 mean signal intensity at SLIs in CMT1A and HNPP, respectively. n = 5 animals (~30 SLIs/animal). Bar graphs represent mean ± SEM with individual data points. Datasets were analyzed with three complementary statistical approaches (unpaired t‐test with all individual data points, unpaired t‐test with experimental means and nested t‐test). *p < 0.05 demonstrate statistical significance with a single t‐test statistic. Scale bars, 10 μm.CC BY · PubMed Central
FIGURE 6 Disrupted ion channel distribution at nodes of Ranvier in CMT1A and HNPP model peripheral nerve myelin. (a) Diagram demonstrating the molecular organization of three distinct subdomains at Nodes of Ranvier: Nodes (N, containing Nav), paranodes (P, containing Caspr and E‐Cadherin) and Juxtaparanodes (J, containing Kv1.2). Created in https://BioRender.com. Representative images of 3‐month‐old (b) WT (C57BL/6J) and CMT1A or (f) WT (129S1/SvImJ) and HNPP teased tibial nerve fibers stained with anti‐Pan Nav (red) and anti‐Kv1.2 (green). Quantification of protein distribution at Nodes of Ranvier (signal volume/fiber diameter) for (c, g) Nav and (d, h) Kv1.2 in CMT1A and HNPP, respectively. (e, i) Quantification Kv1.2 internodal spread away from Nodes of Ranvier in CMT1A and HNPP, respectively. n = 5 animals (~15–25 nodes/animal). Bar graphs represent mean ± SEM with individual data points. Datasets were analyzed with three complementary statistical approaches (unpaired t‐test with all individual data points, unpaired t‐test with experimental means and nested t‐test). ***p < 0.05 demonstrate statistical significance with all three t‐test statistics, **p < 0.05 demonstrate statistical significance with two t‐test statistics and *p < 0.05 demonstrate statistical significance with a single t‐test statistic. Scale bar, 10 μm.
FIGURE 6 Disrupted ion channel distribution at nodes of Ranvier in CMT1A and HNPP model peripheral nerve myelin. (a) Diagram demonstrating the molecular organization of three distinct subdomains at Nodes of Ranvier: Nodes (N, containing Nav), paranodes (P, containing Caspr and E‐Cadherin) and Juxtaparanodes (J, containing Kv1.2). Created in https://BioRender.com. Representative images of 3‐month‐old (b) WT (C57BL/6J) and CMT1A or (f) WT (129S1/SvImJ) and HNPP teased tibial nerve fibers stained with anti‐Pan Nav (red) and anti‐Kv1.2 (green). Quantification of protein distribution at Nodes of Ranvier (signal volume/fiber diameter) for (c, g) Nav and (d, h) Kv1.2 in CMT1A and HNPP, respectively. (e, i) Quantification Kv1.2 internodal spread away from Nodes of Ranvier in CMT1A and HNPP, respectively. n = 5 animals (~15–25 nodes/animal). Bar graphs represent mean ± SEM with individual data points. Datasets were analyzed with three complementary statistical approaches (unpaired t‐test with all individual data points, unpaired t‐test with experimental means and nested t‐test). ***p < 0.05 demonstrate statistical significance with all three t‐test statistics, **p < 0.05 demonstrate statistical significance with two t‐test statistics and *p < 0.05 demonstrate statistical significance with a single t‐test statistic. Scale bar, 10 μm.CC BY · PubMed Central
FIGURE 7 Altered Caspr and E‐Cadherin distributions at paranodes CMT1A and HNPP model myelin. Representative images of 3‐month‐old (a) WT (C57BL/6J) and CMT1A or (e) WT (129S1/SvImJ) and HNPP teased tibial nerve fibers stained for E‐Cadherin (red) and Caspr (green). Quantification of protein distribution at Nodes of Ranvier (signal volume/fiber diameter) for (b, f) E‐Cadherin and (c, g) Caspr in CMT1A and HNPP, respectively. (d, h) Quantification of Caspr internodal spread away from Nodes of Ranvier in CMT1A and HNPP, respectively. n = 5 animals (~15–25 nodes/animal). Bar graphs represent mean ± SEM with individual data points. Datasets were analyzed with three complementary statistical approaches (unpaired t‐test with all individual data points, unpaired t‐test with experimental means and nested t‐test). ***p < 0.05 demonstrate statistical significance with all three t‐test statistics and *p < 0.05 demonstrate statistical significance with a single t‐test statistic. Scale bars, 10 μm.
FIGURE 7 Altered Caspr and E‐Cadherin distributions at paranodes CMT1A and HNPP model myelin. Representative images of 3‐month‐old (a) WT (C57BL/6J) and CMT1A or (e) WT (129S1/SvImJ) and HNPP teased tibial nerve fibers stained for E‐Cadherin (red) and Caspr (green). Quantification of protein distribution at Nodes of Ranvier (signal volume/fiber diameter) for (b, f) E‐Cadherin and (c, g) Caspr in CMT1A and HNPP, respectively. (d, h) Quantification of Caspr internodal spread away from Nodes of Ranvier in CMT1A and HNPP, respectively. n = 5 animals (~15–25 nodes/animal). Bar graphs represent mean ± SEM with individual data points. Datasets were analyzed with three complementary statistical approaches (unpaired t‐test with all individual data points, unpaired t‐test with experimental means and nested t‐test). ***p < 0.05 demonstrate statistical significance with all three t‐test statistics and *p < 0.05 demonstrate statistical significance with a single t‐test statistic. Scale bars, 10 μm.CC BY · PubMed Central
FIGURE 8 Overview of molecular alterations in relation to mouse model disease severity. Because CMT1A is typically a more severe disease than HNPP, with earlier onset and greater functional impairment, molecular and cellular phenotypes that are more pronounced in CMT1A, or that display opposing trends between the two models in accordance with PMP22 gene dosage, are likely to align with disease burden and represent key contributors to pathogenesis. Several of the observations that we report here fit this trend. In SLIs, E‐Cadherin, β‐Catenin, and F‐Actin demonstrate reduced distributions in CMT1A but are increased or unchanged in HNPP, whereas Connexin29 exhibits dramatically increased distribution in CMT1A and less so in HNPP. At Nodes of Ranvier, Kv1.2 distribution is reduced at juxtaparanodes and is spread internodally in CMT1A more so than in HNPP; Nav demonstrates nodal widening (increased distribution) in CMT1A but is unchanged in HNPP, and Caspr demonstrates potentially more internodal spread in CMT1A than in HNPP. These results suggest that changes at Nodes of Ranvier, such as nodal widening and disrupted domain‐specific molecular patterning, along with accompanying abnormalities at SLIs, likely impair proper functionality of these key myelin domains, with more severe impairments in CMT1A than HNPP. These architectural alterations are predicted to compromise metabolic support and alter axonal excitability despite grossly intact compact myelin. Created in https://BioRender.com.
FIGURE 8 Overview of molecular alterations in relation to mouse model disease severity. Because CMT1A is typically a more severe disease than HNPP, with earlier onset and greater functional impairment, molecular and cellular phenotypes that are more pronounced in CMT1A, or that display opposing trends between the two models in accordance with PMP22 gene dosage, are likely to align with disease burden and represent key contributors to pathogenesis. Several of the observations that we report here fit this trend. In SLIs, E‐Cadherin, β‐Catenin, and F‐Actin demonstrate reduced distributions in CMT1A but are increased or unchanged in HNPP, whereas Connexin29 exhibits dramatically increased distribution in CMT1A and less so in HNPP. At Nodes of Ranvier, Kv1.2 distribution is reduced at juxtaparanodes and is spread internodally in CMT1A more so than in HNPP; Nav demonstrates nodal widening (increased distribution) in CMT1A but is unchanged in HNPP, and Caspr demonstrates potentially more internodal spread in CMT1A than in HNPP. These results suggest that changes at Nodes of Ranvier, such as nodal widening and disrupted domain‐specific molecular patterning, along with accompanying abnormalities at SLIs, likely impair proper functionality of these key myelin domains, with more severe impairments in CMT1A than HNPP. These architectural alterations are predicted to compromise metabolic support and alter axonal excitability despite grossly intact compact myelin. Created in https://BioRender.com.CC BY · PubMed Central

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Metadata

Authors
Moss, K. R., Arowolo, M. A., Gutierrez, D. R., & Höke, A.
Affiliations
  • University of Missouri Health System (US)
  • Johns Hopkins University (US)
Corresponding author
Moss, Kathryn R.
ORCID
Venue
Glia
Publisher
Wiley
Published
2025-12-16
Volume
74
Issue
2
Pages
e70124-e70124
ISSN
  • 0894-1491 (ISSN-L)
  • 1098-1136
DOI
10.1002/glia.70124
PMC
PMC12706824
OpenAlex
W4417427233
Cited by
2
References
2
Citations by year
2026: 2
FWCI
0.78
Type
journal article
Language
en
Open access
Licence
Locations
  • Glia (publishedVersion, cc-by)
  • bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion)
  • Europe PMC (PubMed Central) (publishedVersion, cc-by)
  • PubMed (publishedVersion)
  • PubMed Central (publishedVersion, cc-by)
Funders
National Institute of Neurological Disorders and Stroke (K22NS125057)
Topics
  • Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Hereditary Neurological Disorders
  • Health Sciences › Medicine › Clinical Neurology › Peripheral Neuropathies and Disorders
  • Health Sciences › Medicine › Oncology › Cancer Treatment and Pharmacology
Keywords
Charcot-Marie-Tooth disease type 1A, hereditary neuropathy with liability to pressure palsies, Schmidt-Lanterman incisures, nodes of Ranvier, adherens junctions, Kv1.2, Caspr, saltatory conduction, Schwann cells, demyelinating neuropathy, peripheral nerve myelin
MeSH terms
Animals, Arthrogryposis, Axons, Charcot-Marie-Tooth Disease, Disease Models, Animal, Male, Mice, Inbred C57BL, Mice, Transgenic, Myelin Proteins, Myelin Sheath, Ranvier's Nodes, Hereditary Sensory and Motor Neuropathy, Connexins, Mice

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