ArticleThe Journal of neuroscience : the official journal of the Society for Neuroscience2011
MMP2-9 cleavage of dystroglycan alters the size and molecular composition of Schwann cell domains.
Article in The Journal of neuroscience : the official journal of the Society for Neuroscience, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 50 citations in OpenAlex.
- Molecular basis of proteolytic cleavage regulation by the extracellular matrix receptor dystroglycan.Structure (London, England : 1993) · 2024Article
- Schwann Cell Development and Myelination.Cold Spring Harbor perspectives in biology · 2024Review
- Shrinkage Properties and Their Relationship with Degradation of Proteins Linking the Endomysium and Myofibril in Lamb Meat Submitted to Heating or Air Drying.Foods (Basel, Switzerland) · 2022Article
- Review
- The Complex Work of Proteases and Secretases in Wallerian Degeneration: Beyond Neuregulin-1.Frontiers in cellular neuroscience · 2019Review
- Acute- and late-phase matrix metalloproteinase (MMP)-9 activity is comparable in female and male rats after peripheral nerve injury.Journal of neuroinflammation · 2018Article
- The enzymatic processing of α-dystroglycan by MMP-2 is controlled by two anchoring sites distinct from the active site.PloS one · 2018Article
- Reciprocal relationship between membrane type 1 matrix metalloproteinase and the algesic peptides of myelin basic protein contributes to chronic neuropathic pain.Brain, behavior, and immunity · 2017Article
- Rab27a/Slp2-a complex is involved in Schwann cell myelination.Neural regeneration research · 2016Article
- Tadalafil Treatment Delays the Onset of Cardiomyopathy in Dystrophin-Deficient Hearts.Journal of the American Heart Association · 2016Article
- Dopamine increases NMDA-stimulated calcium flux in striatopallidal neurons through a matrix metalloproteinase-dependent mechanism.The European journal of neuroscience · 2016Article
- Matrix Metalloproteinase 9 in Epilepsy: The Role of Neuroinflammation in Seizure Development.Mediators of inflammation · 2016Review
- CD300f immunoreceptor contributes to peripheral nerve regeneration by the modulation of macrophage inflammatory phenotype.Journal of neuroinflammation · 2015Article
- Schwann cell myelination.Cold Spring Harbor perspectives in biology · 2015Review
- Matrix metalloproteinase-14 both sheds cell surface neuronal glial antigen 2 (NG2) proteoglycan on macrophages and governs the response to peripheral nerve injury.The Journal of biological chemistry · 2015Article
- Perlecan is recruited by dystroglycan to nodes of Ranvier and binds the clustering molecule gliomedin.The Journal of cell biology · 2015Article
- Reduction of α-dystroglycan expression is correlated with poor prognosis in glioma.Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine · 2014Article
- Molecules involved in the crosstalk between immune- and peripheral nerve Schwann cells.Journal of clinical immunology · 2014Review
- Functionally distinct PI 3-kinase pathways regulate myelination in the peripheral nervous system.The Journal of cell biology · 2014Article
- Heterogeneity of serum gelatinases MMP-2 and MMP-9 isoforms and charge variants.Journal of cellular and molecular medicine · 2014Article
Corrections and comments
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Authors and funding
11 authors at 4 institutions in 3 countries.
Funding
Abstract
Myelinating glial cells exhibit a spectacular cytoarchitecture, because they polarize on multiple axes and domains. How this occurs is essentially unknown. The dystroglycan-dystrophin complex is required for the function of myelin-forming Schwann cells. Similar to other tissues, the dystroglycan complex in Schwann cells localizes with different dystrophin family members in specific domains, thus promoting polarization. We show here that cleavage of dystroglycan by matrix metalloproteinases 2 and 9, an event that is considered pathological in most tissues, is finely and dynamically regulated in normal nerves and modulates dystroglycan complex composition and the size of Schwann cell compartments. In contrast, in nerves of Dy(2j/2j) mice, a model of laminin 211 deficiency, metalloproteinases 2 and 9 are increased, causing excessive dystroglycan cleavage and abnormal compartments. Pharmacological inhibition of cleavage rescues the cytoplasmic defects of Dy(2j/2j) Schwann cells. Thus, regulated cleavage may be a general mechanism to regulate protein complex composition in physiological conditions, whereas unregulated processing is pathogenic and a target for treatment in disease.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.