Dystroglycan regulates structure, proliferation and differentiation of neuroepithelial cells in the developing vertebrate CNS

Schröder, Jörn E.; Tegeler, Marion R.; Groβhans, Uli; Porten, Elmar; Blank, Martina; Lee, Jun; Esapa, Chris; Blake, Derek J.; Kröger, Stephan

doi:10.1016/j.ydbio.2007.04.020

Cited by 33 publications

(24 citation statements)

References 74 publications

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“…4 b-d). Confirming a previous report [Schroder et al, 2007], the ␤ -dystroglycan antibody used in this work, generated against a peptide in human ␤ -dystroglycan that is 100% conserved in chicken ␤ -dystroglycan, recognized a band of expected size (43 kDa) in Western blot with stage HH1 and HH3-4 embryonic lysates ( fig. 4 g), suggesting that this antibody also specifically recognizes ␤ -dystroglycan in chicken tissues.…”

Section: Resultssupporting

confidence: 89%

“…This region is 100% conserved in the chicken ␤ -dystroglycan protein. The antibody was reported to cross-react with chicken dystroglycan according to the company product datasheet and published literature [Schroder et al, 2007], confirmed by us with Western blot analysis of early embryonic lysates ( fig. 4g).…”

Section: Methodssupporting

confidence: 64%

“…Dystroglycan was isolated from skeletal muscles as a membrane component of the dystrophin-glycoprotein complex, playing an essential role as a cytolinker that connects muscle BM, sarcolemma and muscle cytoskeleton [Ervasti and Campbell, 1991;Ibraghimov-Beskrovnaya et al, 1992;Ervasti and Campbell, 1993]. Its functions in non-muscle tissues, including Reichert's membrane, kidney, salivary gland and neural epithelia, as well as epithelial tumors in human breast, colon and prostate tissues, have been extensively documented [Williamson et al, 1997;Henry et al, 2001;Muschler et al, 2002;Jing et al, 2004;Sgambato and Brancaccio, 2005;Schroder et al, 2007;Sgambato et al, 2007;Satz et al, 2008;Bao et al, 2009;Giannico et al, 2009].…”

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confidence: 99%

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Involvement of Dystroglycan in Epithelial-Mesenchymal Transition during Chick Gastrulation

Nakaya¹,

Sukowati²,

Alev³

et al. 2010

Cells Tissues Organs

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Regulated disruption of the basement membrane (BM) is a critical step in many epithelial-mesenchymal transition (EMT) processes. Molecular mechanisms controlling the interaction between the BM and the basal membrane of epithelial cells and its subsequent disruption during EMT are poorly understood. Using chick embryos as a model, we analyzed the molecular complexity of this interaction during gastrulation EMT. Transcriptome data indicated that the BM of the gastrulation stage chick epiblast contains a full range of BM component proteins with unique subtype combinations. Integrins and dystroglycan are 2 major groups of basal membrane proteins involved in BM interaction. We provide evidence that dystroglycan gene expression is restricted to the epiblast during early development and its expression is downregulated in cells undergoing gastrulation EMT. The β-dystroglycan protein is localized to the basolateral membrane in epiblast cells and the basal localization is lost in cells undergoing EMT. Disruption of actin filaments leads to a decrease in the lateral membrane localization of β-dystroglycan and a relative increase in basal membrane localization, whereas disruption of microtubules leads to the loss of BM/basal membrane interaction and basal membrane β-dystroglycan localization. Overall, these data suggest an involvement of dystroglycan, especially the regulation of its expression and localization, in gastrulation EMT.

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Section: Resultssupporting

confidence: 89%

Section: Methodssupporting

confidence: 64%

mentioning

confidence: 99%

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Involvement of Dystroglycan in Epithelial-Mesenchymal Transition during Chick Gastrulation

Nakaya¹,

Sukowati²,

Alev³

et al. 2010

Cells Tissues Organs

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“…Although the role of b1-integrins in radial glial cells during development has been well studied (Beggs et al, 2003;Belvindrah et al, 2007a;Georges-Labouesse et al, 1998;Haubst et al, 2006;Herms et al, 2004;Schroder et al, 2007), still very little is known about the interaction between astrocytes and the leptomeningeal and vascular BMs in the postnatal and adult brain.…”

Section: Discussionmentioning

confidence: 99%

Conditional deletion of β1‐integrin in astroglia causes partial reactive gliosis

Robel

Mori

Zoubaa

et al. 2009

Glia

106

100

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Astrocytes play many pivotal roles in the adult brain, including their reaction to injury. A hallmark of astrocytes is the contact of their endfeet with the basement membrane surrounding blood vessels, but still relatively little is known about the signaling mediated at the contact site. Here, we examine the role of beta1-integrin at this interface by its conditional deletion using different Cre lines. Thereby, the protein was reduced only at postnatal stages either in both glia and neurons or specifically only in neurons. Strikingly, only the former resulted in reactive gliosis, with the hallmarks of reactive astrocytes comprising astrocyte hypertrophy and up-regulation of the intermediate filaments GFAP and vimentin as well as pericellular components, such as Tenascin-C and the DSD-1 proteoglycan. In addition, we also observed to a certain degree a non-cell autonomous activation of microglial cells after conditional beta1-integrin deletion. However, these reactive astrocytes did not divide, suggesting that the loss of beta1-integrin-mediated signaling is not sufficient to elicit proliferation of these cells as observed after brain injury. Interestingly, this partial reactive gliosis appeared in the absence of cell death and blood brain barrier disturbances. As these effects did not appear after neuron-specific deletion of beta1-integrin, we conclude that beta1-integrin-mediated signaling in astrocytes is required to promote their acquisition of a mature, nonreactive state. Alterations in beta1-integrin-mediated signaling may hence be implicated in eliciting specific aspects of reactive gliosis after injury.

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“…Transfection and staining of HEK293 cells Full-length complementary DNA (cDNA) coding for human LRP4 (huLRP4) was obtained from Imagenes GmbH (Berlin, Germany) and subcloned into the pMES vector [28], which allows identification of transfected cells by simultaneous expression of enhanced green fluorescent protein (EGFP). Successful cloning and surface expression of LRP4 was confirmed by Western blotting and immunocytochemistry, respectively.…”

Section: Methodsmentioning

confidence: 99%

Anti-LRP4 autoantibodies in AChR- and MuSK-antibody-negative myasthenia gravis

Schöser²,

et al. 2011

Self Cite

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Myasthenia gravis (MG) is an autoimmune disorder characterized by a defect in synaptic transmission at the neuromuscular junction causing fluctuating muscle weakness with a decremental response to repetitive nerve stimulation or altered jitter in single-fiber electromyography (EMG). Approximately 80% of all myasthenia gravis patients have autoantibodies against the nicotinic acetylcholine receptor in their serum. Autoantibodies against the tyrosine kinase muscle-specific kinase (MuSK) are responsible for 5-10% of all myasthenia gravis cases. The autoimmune target in the remaining cases is unknown. Recently, low-density lipoprotein receptor-related protein (LRP4) has been identified as the agrin receptor. LRP4 interacts with agrin, and the binding of agrin activates MuSK, which leads to the formation of most if not all postsynaptic specializations, including aggregates containing acetylcholine receptors (AChRs) in the junctional plasma membrane. In the present study we tested if autoantibodies against LRP4 are detectable in patients with myasthenia gravis. To this end we analyzed 13 sera from patients with generalized myasthenia gravis but without antibodies against AChR or MuSK. The results showed that 12 out of 13 antisera from double-seronegative MG patients bound to proteins concentrated at the neuromuscular junction of adult mouse skeletal muscle and that approximately 50% of the tested sera specifically bound to HEK293 cells transfected with human LRP4. Moreover, 4 out of these 13 sera inhibited agrin-induced aggregation of AChRs in cultured myotubes by more than 50%, suggesting a pathogenic role regarding the dysfunction of the neuromuscular endplate. These results indicate that LRP4 is a novel target for autoantibodies and is a diagnostic marker in seronegative MG patients.

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Dystroglycan regulates structure, proliferation and differentiation of neuroepithelial cells in the developing vertebrate CNS

Cited by 33 publications

References 74 publications

Involvement of Dystroglycan in Epithelial-Mesenchymal Transition during Chick Gastrulation

Involvement of Dystroglycan in Epithelial-Mesenchymal Transition during Chick Gastrulation

Conditional deletion of β1‐integrin in astroglia causes partial reactive gliosis

Anti-LRP4 autoantibodies in AChR- and MuSK-antibody-negative myasthenia gravis

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