Relevant bibliographies by topics / Schwann cell, dystroglycan

Academic literature on the topic 'Schwann cell, dystroglycan'

Author: Grafiati
Published: 9 March 2023
Last updated: 10 March 2023

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Journal articles on the topic "Schwann cell, dystroglycan"

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Masaki, Toshihiro, and Kiichiro Matsumura. "Biological Role of Dystroglycan in Schwann Cell Function and Its Implications in Peripheral Nervous System Diseases." Journal of Biomedicine and Biotechnology 2010 (2010): 1–17. http://dx.doi.org/10.1155/2010/740403.

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Dystroglycan is a central component of the dystrophin-glycoprotein complex (DGC) that links extracellular matrix with cytoskeleton, expressed in a variety of fetal and adult tissues. Dystroglycan plays diverse roles in development and homeostasis including basement membrane formation, epithelial morphogenesis, membrane stability, cell polarization, and cell migration. In this paper, we will focus on biological role of dystroglycan in Schwann cell function, especially myelination. First, we review the molecular architecture of DGC in Schwann cell abaxonal membrane. Then, we will review the loss-of-function studies using targeted mutagenesis, which have revealed biological functions of each component of DGC in Schwann cells. Based on these findings, roles of dystroglycan in Schwann cell function, in myelination in particular, and its implications in diseases will be discussed in detail. Finally, in view of the fact that understanding the role of dystroglycan in Schwann cells is just beginning, future perspectives will be discussed.
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Feltri, M. Laura, Diana Graus Porta, Stefano C. Previtali, Alessandro Nodari, Barbara Migliavacca, Arianna Cassetti, Amanda Littlewood-Evans, et al. "Conditional disruption of β1 integrin in Schwann cells impedes interactions with axons." Journal of Cell Biology 156, no. 1 (January 3, 2002): 199–210. http://dx.doi.org/10.1083/jcb.200109021.

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In dystrophic mice, a model of merosin-deficient congenital muscular dystrophy, laminin-2 mutations produce peripheral nerve dysmyelination and render Schwann cells unable to sort bundles of axons. The laminin receptor and the mechanism through which dysmyelination and impaired sorting occur are unknown. We describe mice in which Schwann cell–specific disruption of β1 integrin, a component of laminin receptors, causes a severe neuropathy with impaired radial sorting of axons. β1-null Schwann cells populate nerves, proliferate, and survive normally, but do not extend or maintain normal processes around axons. Interestingly, some Schwann cells surpass this problem to form normal myelin, possibly due to the presence of other laminin receptors such as dystroglycan and α6β4 integrin. These data suggest that β1 integrin links laminin in the basal lamina to the cytoskeleton in order for Schwann cells to ensheath axons, and alteration of this linkage contributes to the peripheral neuropathy of congenital muscular dystrophy.
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Tsiper, Maria V., and Peter D. Yurchenco. "Laminin assembles into separate basement membrane and fibrillar matrices in Schwann cells." Journal of Cell Science 115, no. 5 (March 1, 2002): 1005–15. http://dx.doi.org/10.1242/jcs.115.5.1005.

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Laminins are important for Schwann cell basement membrane assembly and axonal function. In this study, we found that exogenous laminin-1, like neuromuscular laminins-2/4, formed two distinct extracellular matrices on Schwann cell surfaces, each facilitated by laminin polymerization. Assembly of one, a densely-distributed reticular matrix, was accompanied by a redistribution of cell-surface dystroglycan and cytoskeletal utrophin into matrix-receptor-cytoskeletal complexes. The other, a fibrillar matrix,accumulated in separate zones associated with pre-existing β1-integrin arrays. The laminin-1 fragment E3 (LG-modules 4-5), which binds dystroglycan and heparin, inhibited reticular-matrix formation. By contrast,β1-integrin blocking antibody (Ha2/5) prevented fibrillar assembly. Ultrastructural analysis revealed that laminin treatment induced the formation of a linear electron-dense extracellular matrix (lamina densa)separated from plasma membrane by a narrow lucent zone (lamina lucida). This structure was considerably reduced with non-polymerizing laminin, fully blocked by E3, and unaffected by Ha2/5. Although it formed in the absence of type IV collagen, it was nonetheless able to incorporate this collagen. Finally, cell competency to bind laminin and form a basement membrane was passage-dependent. We postulate that laminin induces the assembly of a basement membrane on competent cell surfaces probably mediated by anchorage through LG 4-5. Upon binding, laminin interacts with dystroglycan,mobilizes utrophin, and assembles a `nascent' basement membrane, independent of integrin, that is completed by incorporation of type IV collagen. However,the fibrillar β1-integrin dependent matrix is unlikely to be precursor to basement membrane.
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Rambukkana, A. "Role of -Dystroglycan as a Schwann Cell Receptor for Mycobacterium leprae." Science 282, no. 5396 (December 11, 1998): 2076–79. http://dx.doi.org/10.1126/science.282.5396.2076.

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Yamada, Hiroki, Alain J. Denzer, Hisae Hori, Takeshi Tanaka, Louise V. B. Anderson, Sachiko Fujita, Hiroko Fukuta-Ohi, Teruo Shimizu, Markus A. Ruegg, and Kiichiro Matsumura. "Dystroglycan Is a Dual Receptor for Agrin and Laminin-2 in Schwann Cell Membrane." Journal of Biological Chemistry 271, no. 38 (September 20, 1996): 23418–23. http://dx.doi.org/10.1074/jbc.271.38.23418.

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Saito, Fumiaki, Toshihiro Masaki, Keiko Kamakura, Louise V. B. Anderson, Sachiko Fujita, Hiroko Fukuta-Ohi, Yoshihide Sunada, Teruo Shimizu, and Kiichiro Matsumura. "Characterization of the Transmembrane Molecular Architecture of the Dystroglycan Complex in Schwann Cells." Journal of Biological Chemistry 274, no. 12 (March 19, 1999): 8240–46. http://dx.doi.org/10.1074/jbc.274.12.8240.

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Li, Shaohua, Patricia Liquari, Karen K. McKee, David Harrison, Raj Patel, Sean Lee, and Peter D. Yurchenco. "Laminin–sulfatide binding initiates basement membrane assembly and enables receptor signaling in Schwann cells and fibroblasts." Journal of Cell Biology 169, no. 1 (April 11, 2005): 179–89. http://dx.doi.org/10.1083/jcb.200501098.

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Endoneurial laminins (Lms), β1-integrins, and dystroglycan (DG) are important for Schwann cell (SC) ensheathment and myelination of axons. We now show that SC expression of galactosyl-sulfatide, a Lm-binding glycolipid, precedes that of Lms in developing nerves. This glycolipid anchors Lm-1 and -2 to SC surfaces by binding to their LG domains and enables basement membrane (BM) assembly. Revealingly, non–BM-forming fibroblasts become competent for BM assembly when sulfatides are intercalated into their cell surfaces. Assembly is characterized by coalescence of sulfatide, DG, and c-Src into a Lm-associated complex; by DG-dependent recruitment of utrophin and Src activation; and by integrin-dependent focal adhesion kinase phosphorylation. Collectively, our findings suggest that sulfated glycolipids are key Lm anchors that determine which cell surfaces can assemble Lms to initiate BM assembly and DG- and integrin-mediated signaling.
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Court, F. A., D. Zambroni, E. Pavoni, C. Colombelli, C. Baragli, G. Figlia, L. Sorokin, et al. "MMP2-9 Cleavage of Dystroglycan Alters the Size and Molecular Composition of Schwann Cell Domains." Journal of Neuroscience 31, no. 34 (August 24, 2011): 12208–17. http://dx.doi.org/10.1523/jneurosci.0141-11.2011.

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Sherman, Diane L., and Peter J. Brophy. "A murine model of Charcot-Marie-Tooth disease 4F reveals a role for the C-terminus of periaxin in the formation and stabilization of Cajal bands." Wellcome Open Research 3 (March 1, 2018): 20. http://dx.doi.org/10.12688/wellcomeopenres.13673.1.

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Charcot-Marie-Tooth (CMT) disease comprises up to 80 monogenic inherited neuropathies of the peripheral nervous system (PNS) that collectively result in demyelination and axon degeneration. The majority of CMT disease is primarily either dysmyelinating or demyelinating in which mutations affect the ability of Schwann cells to either assemble or stabilize peripheral nerve myelin. CMT4F is a recessive demyelinating form of the disease caused by mutations in the Periaxin (PRX) gene. Periaxin (Prx) interacts with Dystrophin Related Protein 2 (Drp2) in an adhesion complex with the laminin receptor Dystroglycan (Dag). In mice the Prx/Drp2/Dag complex assembles adhesive domains at the interface between the abaxonal surface of the myelin sheath and the cytoplasmic surface of the Schwann cell plasma membrane. Assembly of these appositions causes the formation of cytoplasmic channels called Cajal bands beneath the surface of the Schwann cell plasma membrane. Loss of either Periaxin or Drp2 disrupts the appositions and causes CMT in both mouse and man. In a mouse model of CMT4F, complete loss of Periaxin first prevents normal Schwann cell elongation resulting in abnormally short internodal distances which can reduce nerve conduction velocity, and subsequently precipitates demyelination. Distinct functional domains responsible for Periaxin homodimerization and interaction with Drp2 to form the Prx/Drp2/Dag complex have been identified at the N-terminus of Periaxin. However, CMT4F can also be caused by a mutation that results in the truncation of Periaxin at the extreme C-terminus with the loss of 391 amino acids. By modelling this in mice, we show that loss of the C-terminus of Periaxin results in a surprising reduction in Drp2. This would be predicted to cause the observed instability of both appositions and myelin, and contribute significantly to the clinical phenotype in CMT4F.
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Sherman, D. L., L. M. N. Wu, M. Grove, C. S. Gillespie, and P. J. Brophy. "Drp2 and Periaxin Form Cajal Bands with Dystroglycan But Have Distinct Roles in Schwann Cell Growth." Journal of Neuroscience 32, no. 27 (July 4, 2012): 9419–28. http://dx.doi.org/10.1523/jneurosci.1220-12.2012.

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Dissertations / Theses on the topic "Schwann cell, dystroglycan"

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COLOMBELLI, CRISTINA. "Schwann cell dystroglycan regulates the architecture of nodes of Ranvier and internodes in the peripheral nervous system." Doctoral thesis, Università degli Studi di Milano-Bicocca, 2012. http://hdl.handle.net/10281/29838.

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This thesis addresses the role of a Schwann cell laminin-receptor, dystroglycan, in the regulation of both nodal and internodal architecture, to provide the nerve with the proper structure that is ultimately needed to accomplish its electrical function. By pairing with different dystrophin-like proteins (utrophin, Dp116 and DRP2), cytoskeletal and cytoskeletal-adaptor proteins (actin) and extracellular-matrix ligands (laminins, agrin and perlecan), dystroglycan forms complexes that are differently localized throughout the nerve and that may have specific functions in radial sorting, compartmentalization of the myelinated fiber and organization of nodes of Ranvier. In the present thesis I will focus on the role of Schwann cell dystroglycan in nodal architecture (1), and I will analyze how DG cleavage by matrix metalloproteinases 2 and 9 (MMP-2 and MMP-9) can regulate Schwann cell cytoplasm compartmentalization and internodal lenght in both physiological and pathological conditions (2). These two sub-projects have the following specific objectives: 1. To understand if the defect in Nav clustering at nodes of Ranvier in the absence of dystroglycan is developmentally-determined or acquired with age; to unravel the mechanism/s through which Schwann cell dystroglycan aids Nav clustering (Chapter 2). 2. To understand if post-translational modification of dystroglycan by metalloproteainases 2 and 9 can alter the compartmentalization of Schwann cell cytoplasm and how this influence the Schwann cell phenotype in physiological conditions; to evaluate if the ablation of MMP9, which is elevated in nerves of dystrophic mice (model of MDC1A), could ameliorate the peripheral neuropathy (Chapter 3).
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Conference papers on the topic "Schwann cell, dystroglycan"

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Santos, Ronaldi Gonçalves dos, Bhenise Vitória Santos Nunes, Gabriela Santos Domiciano, Humberto Gessinger Nascimento dos Santos, Jean Cardek Paulino Silva, Mariana Goulart de Souza Martins, Pedro Henrique Delfino, and Fernando Mesquita Júnior. "Leprosy: a view of the molecular interaction of Mycobacterium leprae with Schwann Cells." In XIII Congresso Paulista de Neurologia. Zeppelini Editorial e Comunicação, 2021. http://dx.doi.org/10.5327/1516-3180.469.

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Introduction: Leprosy is an infectious disease whose etiologic agent is Mycobacterium leprae. Despite its notoriety, there are mechanisms of molecular interaction that have not been elucidated. Therefore, it was carried out a literary review about the molecular interaction between M. leprae and the Schwann cell (SC), characterizing the mechanisms of endocytosis and cellular damage. Methods: It was delimited a 10-year timeframe (2010 to 2020). The research bases used were Portal de Periódicos CAPES/MEC, National Library of Medicine - PubMed, World Health Organization (WHO) Statistical Data, Pan American Health Organization (PAHO), Ministry of Health of Brazil Data, Scielo, Fundação Oswaldo Cruz (ARCA-FIOCRUZ) and UpToDate Inc. Results: M. Leprae is endocitized through interactions with basal lamina of the SC, whose α-laminin 2 enables the formation of the dystrophin-dystroglycan complex. Moreover, the activity of the pathogen in the SC is associated with direct, indirect and additional damage. It was verified the need for continuous studies due to the complexity of this molecular biointeraction, given the cellular reprogramming of SC and its neuronal impact. Conclusion: There are still many scientific gaps, requiring further clarification in the area, which results in uncertainties in the tropism of the pathogen with the peripheral nerves.
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