Expression of Laminin Receptors in Schwann Cell Differentiation: Evidence for Distinct Roles

Previtali, Stefano C.; Nodari, Alessandro; Taveggia, Carla; Pardini, Celia; Dina, Giorgia; Villa, Antonello; Wrabetz, Lawrence; Quattrini, Angelo; Feltri, M. Laura

doi:10.1523/jneurosci.23-13-05520.2003

Cited by 99 publications

(128 citation statements)

References 69 publications

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“…This suggests that laminins can employ other receptors to regulate Schwann cell number. DG also functions as a laminin receptor (Previtali et al, 2001(Previtali et al, , 2003. In contrast to b1 integrin-deficient Schwann cells, Schwann cell-specific ablation of DG does not severely affect radial sorting of axons.…”

Section: Laminin Receptors In the Pnsmentioning

confidence: 98%

“…The endoneurium basal lamina is disrupted, and nerve conduction velocity also is reduced in the nerves of these mutant mice (Rasminsky et al, 1978). In the peripheral nerves of the laminin a2 mutant mice, both laminins a4 and a1 are upregulated in the endoneurium, and the phenotype is mild (Patton et al, 1997;Previtali et al, 2003).…”

Section: Regulation Of Schwann Cell Function By Laminins and Laminin mentioning

confidence: 99%

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Regulation of Schwann cell function by the extracellular matrix

Chernousov

Chen

et al. 2008

Glia

171

138

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Laminins and collagens are extracellular matrix proteins that play essential roles in peripheral nervous system development. Laminin signals regulate Schwann cell proliferation and survival as well as actin cytoskeleton dynamics, which are essential steps for radial sorting and myelination of peripheral axons by Schwann cells. Collagen and their receptors promote Schwann cell adhesion, spreading, and myelination as well as neurite outgrowth. In this article, we will review the recent advances in the studies of laminin and collagen function in Schwann cell development. V V C

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Section: Laminin Receptors In the Pnsmentioning

confidence: 98%

Section: Regulation Of Schwann Cell Function By Laminins and Laminin mentioning

confidence: 99%

Regulation of Schwann cell function by the extracellular matrix

Chernousov

Chen

et al. 2008

Glia

171

138

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“…Against a role for α6β4 integrin, myelination starts normally in newborn nerves and dorsal root ganglia explants from mice dying at post-natal day 1 (P1) due to β4 inactivation (Frei et al, 1999). However, β4 expression in Schwann cells is just beginning in P1 mice and follows, not precedes, the onset of myelination (Previtali et al, 2003b). Thus a role for β4 in myelin maturation or maintenance could not be addressed from these studies.…”

Section: Introductionmentioning

confidence: 97%

“…First, β4 integrin expression in Schwann cells is induced by axons during myelination (Einheber et al, 1993;Feltri et al, 1994). In contrast to α6β1 integrin that decreases during myelination (Einheber et al, 1993), α6β4 appears during myelin synthesis and its expression continues to increase in adulthood (Previtali et al, 2003b;Verheijen et al, 2003). Thus, Schwann cells may switch their laminin-binding integrins from α6β1 to α6β4 to promote or maintain myelination (Einheber et al, 1993).…”

Section: Introductionmentioning

confidence: 99%

6 4 Integrin and Dystroglycan Cooperate to Stabilize the Myelin Sheath

Nodari¹,

Previtali²,

Dati³

et al. 2008

Journal of Neuroscience

103

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Schwann cells integrate signals deriving from the axon and the basal lamina to myelinate peripheral nerves. Integrin α6β4 is a laminin receptor synthesized by Schwann cells and displayed apposed to the basal lamina. α6β4 integrin expression in Schwann cells is induced by axons at the onset of myelination, and rise in adulthood. The β4 chain has a uniquely long cytoplasmic domain that interacts with intermediate filaments such as dystonin, important in peripheral myelination. Furthermore, α6β4 integrin binds peripheral myelin protein 22, whose alteration causes the most common demyelinating hereditary neuropathy. All these data suggest a role for α6β4 integrin in peripheral nerve myelination. Here we show that ablating α6β4 integrin specifically in Schwann cells of transgenic mice does not affect peripheral nerve development, myelin formation, maturation or regeneration. However, consistent with maximal expression in adult nerves, α6β4 integrin-null myelin is more prone to abnormal folding with aging. When the laminin receptor dystroglycan is also ablated, major folding abnormalities occur, associated with acute demyelination in some peripheral nervous system districts. These data indicate that, similar to its role in skin, α6β4 integrin confers stability to myelin in peripheral nerves.

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“…The ␣6␤4 integrin is a laminin-5 receptor expressed in many epithelial cells, in endothelial cells, and in MC (17)(18)(19). ␤4 integrin, originally identified as a tumor-associated antigen (20), was subsequently documented in human premalignant lesions and incipient neoplasms (11,21).…”

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confidence: 99%

Oxidative Stress-mediated Mesangial Cell Proliferation Requires RAC-1/Reactive Oxygen Species Production and β4 Integrin Expression

Dentelli

Rosso

Zeoli

et al. 2007

Journal of Biological Chemistry

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Lipid abnormalities and oxidative stress, by stimulating mesangial cell (MC) proliferation, can contribute to the development of diabetes-associated renal disease. In this study we investigated the molecular events elicited by oxidized low density lipoproteins (ox-LDL) in MC. We demonstrate that in MC cultured in the presence of ox-LDL, survival and mitogenic signals on Akt and Erk1/2 MAPK pathways are induced, respectively. Moreover, as shown by the expression of the dominant negative Rac-1 construct, we first report that ox-LDL-mediated cell survival and cell cycle progression depend on Rac-1 GTPase-mediated reactive oxygen species production and on epidermal growth factor receptor transactivation. By silencing Akt and blocking Erk1/2 MAPK pathways, we also demonstrate that these signals are downstream to Rac-1/reactive oxygen species production and epidermal growth factor receptor activation. Finally, by endogenous depletion of ␤4 integrin, expressed in MC, we provide evidence that the expression of this adhesion molecule is essential for ox-LDL-mediated MC dysfunction. Our data identify a novel signaling pathway involved in oxidative stress-induced diabetes-associated renal disease and provide the rationale for therapeutically targeting ␤4 integrin.Abnormalities in lipoprotein metabolism are commonly observed in patients with renal disease. Specifically, hyperlipidemia and glomerular lipid deposition of atherogenic lipoproteins (low density lipoproteins (LDL), 2 and their oxidized variants, ox-LDL) are implicated in key pathobiological processes involved in the development of glomerular diseases, including mesangial cell (MC) hypercellularity (1). The relevance of mitogen intracellular signaling in mesangial proliferative disease has only recently been recognized (2). Indeed, accumulation of atherogenic lipoproteins within the glomerulus, by activating membrane receptor protein-tyrosine kinases (RPTK), such as the epidermal growth factor receptor (EGFR), triggers MAPK cascades leading to cyclin/cyclin-dependent kinase activation of DNA synthesis and MC proliferation (2). Moreover, in smooth muscle cells, ox-LDL (3) has been shown to trigger the phosphatidylinositol 3-kinase/Akt signaling pathway (4). These data thus suggest that atherogenic lipoproteins may act as one of the major endogenous modulators for mitogenic signaling response within the glomerulus.Although superoxide anions and hydrogen peroxide are generally considered to be toxic, recent evidence suggests that the production of the reactive oxygen species (ROS) might be an integral component of membrane receptor signaling (5). In mammalian cells, a vast array of intracellular stimuli have been shown to induce a transient increase in the intracellular ROS concentrations, and specific inhibition of ROS generation results in a complete blockage of stimulant-dependent signaling (5). In particular, growth factor-mediated ROS generation seems to be necessary for propagation of downstream mitogenic and antiapoptotic signals (5).Rho family GTPases are imp...

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Expression of Laminin Receptors in Schwann Cell Differentiation: Evidence for Distinct Roles

Cited by 99 publications

References 69 publications

Regulation of Schwann cell function by the extracellular matrix

Regulation of Schwann cell function by the extracellular matrix

6 4 Integrin and Dystroglycan Cooperate to Stabilize the Myelin Sheath

Oxidative Stress-mediated Mesangial Cell Proliferation Requires RAC-1/Reactive Oxygen Species Production and β4 Integrin Expression

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