Integrin-linked kinase is required for laminin-2–induced oligodendrocyte cell spreading and CNS myelination

Chun, Soo Jin; Rasband, Matthew N.; Sidman, Richard L.; Habib, Amyn A.; Vartanian, Timothy

doi:10.1083/jcb.200304154

Cited by 170Neurogenesis and neuroplasticity mechanismsCell Adhesion Molecules ResearchMultiple Sclerosis Research Studies

Integrin-linked kinase is required for laminin-2–induced oligodendrocyte cell spreading and CNS myelination

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Chun, Soo Jin, Rasband, Matthew N., Sidman, Richard L., Habib, Amyn A., Vartanian, Timothy·2003·The Journal of Cell Biology

DOI 10.1083/jcb.200304154PMC PMC2173507

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Abstract

Early steps in myelination in the central nervous system (CNS) include a specialized and extreme form of cell spreading in which oligodendrocytes extend large lamellae that spiral around axons to form myelin. Recent studies have demonstrated that laminin-2 (LN-2; α2β1γ1) stimulates oligodendrocytes to extend elaborate membrane sheets in vitro (cell spreading), mediated by integrin α6β1. Although a congenital LN-2 deficiency in humans is associated with CNS white matter changes, LN-2–deficient (dy/dy) mice have shown abnormalities primarily within the peripheral nervous system. Here, we demonstrate a critical role for LN-2 in CNS myelination by showing that dy/dy mice have quantitative and morphologic defects in CNS myelin. We have defined the molecular pathway through which LN-2 signals oligodendrocyte cell spreading by demonstrating requirements for phosphoinositide 3-kinase activity and integrin-linked kinase (ILK). Interaction of oligodendrocytes with LN-2 stimulates ILK activity. A dominant negative ILK inhibits LN-2–induced myelinlike membrane formation. A critical component of the myelination signaling cascade includes LN-2 and integrin signals through ILK.

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There are many examples of regional differences in dysmyelination caused by genetic manipulation of mice between areas such as the optic nerve, spinal cord, cerebellum and corpus callosum.
“There are many examples of regional differences in dysmyelination caused by genetic manipulation of mice between areas such as the optic nerve, spinal cord, cerebellum and corpus callosum.”
From SJL Mice Exposed to Cuprizone Intoxication Reveal Strain and Gender Pattern Differences in Demyelination (2009) · cites this paper as [11]
The Results section, “Ultrastructural analysis of dy/dy mice: regional differences” (page unavailable), reports dysmyelination in the optic nerve and corpus callosum but not the spinal cord of mutant mice. The Discussion, “Regional differences” (page unavailable), also mentions a similar pattern in Fyn-knockout mice. Our copy does not document cerebellar differences or substantiate the broader assertion that there are many examples. (LLM, conf=0.85)
Experimental — accuracy not yet measured
Laminin-deficient dystrophia muscularis mice exhibit hypomyelination in the corpus callosum and optic nerve, but not the spinal cord.
“For example, laminin‐deficient dystrophia muscularis mice exhibit hypomyelination in the corpus callosum and optic nerve, but not the spinal cord (11)”
From SJL Mice Exposed to Cuprizone Intoxication Reveal Strain and Gender Pattern Differences in Demyelination (2009) · cites this paper as [11]

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Laminin-2 on the brain
Dove, A. W. (2003) · The Journal of Cell Biology · doi:10.1083/jcb1632xiti5
JCB Article
Chun, S. J., Rasb, M. N., Sidman, R. L., Habib, A. A., & Vartanian, T. K. (2013)
Self-citation
Integrin-linked Kinase Functions as a Cytoskeletal Scaffold in Oligodendrocyte Migration, Differentiation and Central Nervous System Myelination
O’Meara, R. W. (2014) · uO Research (University of Ottawa) · doi:10.20381/ruor-6743
A Role for Integrin-linked Kinase In Oligodendrocyte Mediated Myelination of the Central Nervous System
Michalski, J. (2014) · uO Research (University of Ottawa) · doi:10.20381/ruor-6598
Integrin-Linked Kinase Regulates Process Extension in Oligodendrocytes via Control of Actin Cytoskeletal Dynamics
O’Meara, R. W., Michalski, J., Anderson, C., Bhanot, K., Rippstein, P. U., & Kothary, R. (2013) · Journal of Neuroscience · doi:10.1523/jneurosci.5582-12.2013 · Cited by 33 · see citing works

Authors: Chun, S. J., Rasband, M. N., Sidman, R. L., Habib, A. A., & Vartanian, T.
Affiliations: Beth Israel Deaconess Medical Center (US)
UConn Health (US)
Corresponding author: Vartanian, Timothy
ORCID: Rasband, Matthew N.
Sidman, Richard L.
Habib, Amyn A.
Vartanian, Timothy
Venue: The Journal of Cell Biology
Publisher: Rockefeller University Press
Published: 2003-10-27
Volume: 163
Issue: 2
Pages: 397-408
ISSN: 0021-9525 (ISSN-L)
1540-8140
DOI: 10.1083/jcb.200304154
PMC: PMC2173507
OpenAlex: W2120316837
Cited by: 170
References: 41
Citations by year: 2026: 4 · 2025: 3 · 2024: 3 · 2023: 2 · 2022: 5 · 2021: 6 · 2020: 5 · 2019: 10 · 2018: 4 · 2017: 8 · 2016: 6 · 2015: 10 · 2014: 4 · 2013: 7 · 2012: 8
FWCI: 2.44
Type: journal article
Language: en
Open access: green
www.ncbi.nlm.nih.gov
Licence: cc-by-nc-sa
Locations: The Journal of Cell Biology (publishedVersion)
PubMed Central (publishedVersion, cc-by-nc-sa)
PubMed (publishedVersion)
Funders: National Institutes of Health (5k02ns002028-04)
National Institute of Neurological Disorders and Stroke (K02 NS02028, P01 NS 38475, R01NS044916, P01NS038475, R01NS042317, R01 NS42317)
Topics: Life Sciences › Neuroscience › Developmental Neuroscience › Neurogenesis and neuroplasticity mechanisms
Health Sciences › Medicine › Immunology and Allergy › Cell Adhesion Molecules Research
Health Sciences › Medicine › Pathology and Forensic Medicine › Multiple Sclerosis Research Studies
Keywords: integrin-linked kinase, laminin-2, CNS myelination, alpha6beta1 integrin, phosphatidylinositol 3-kinase, myelination, integrin signaling
MeSH terms: Scaffold Protein ILK, Adenoviridae, Animals, Axons, Cell Survival, Cells, Cultured, Central Nervous System, Cytoskeletal Proteins, Enzyme Activation, Homozygote, Laminin, Mice, Mutant Strains, Mutation, Myelin Sheath, Oligodendroglia, Optic Nerve, Phosphoproteins, Cell Adhesion Molecules, Rats, Sprague-Dawley, Protein Serine-Threonine Kinases, Phosphatidylinositol 3-Kinases, Mice, Rats, Paxillin

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Integrin-linked kinase is required for laminin-2–induced oligodendrocyte cell spreading and CNS myelination

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