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Migration of neural crest cells on vitronectin adsorbed to the substratum at the concentrations of 50 µg/ml (A,B) and 0.5 µg/ml (C,D). (B,D) Higher magnifications of A and C, respectively, showing the morphology of cells. Neural tube explants were deposited onto vitronectincoated bacteriological Petri dishes and neural crest cells were allowed to migrate on the substratum for 15 hours in serum-free medium and then photographed. At high coating concentrations, vitronectin yields a large number of well-spread cells that migrate long distances from the neural tube. At low concentrations, vitronectin also produces significant migration of cells, though most of them are poorly spread. nt, neural tube.
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To identify potentially important extracellular matrix adhesive molecules in neural crest cell migration, the possible role of vitronectin and its corresponding integrin receptors was examined in the adhesion and migration of avian neural crest cells in vitro. Adhesion and migration on vitronectin were comparable to those found on fibronectin and c...
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Context 1
... number of migrating neural crest cells and their cell shape on vitronectin substrata were also found to be virtually identical to those exhibited by neural crest cells cultured onto fibronectin ( Fig. 5; see also Duband et al., 1991). When neural tubes were deposited on substrata coated with vitronectin at high concentrations (≥10 µg/ml), neural crest cells migrated out within 2-4 hours and actively moved about on the substra- tum. After 15 hours in culture (Fig. 5A,B), the neural crest cell population organized into a large halo ...
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... identical to those exhibited by neural crest cells cultured onto fibronectin ( Fig. 5; see also Duband et al., 1991). When neural tubes were deposited on substrata coated with vitronectin at high concentrations (≥10 µg/ml), neural crest cells migrated out within 2-4 hours and actively moved about on the substra- tum. After 15 hours in culture (Fig. 5A,B), the neural crest cell population organized into a large halo around the neural tube and individual cells exhibited a well-spread morphology with several processes per cell. At low coating concentrations of vit- ronectin (≤1 µg/ml), the cell population was sparse and indi- vidual cells were less spread and more elongated in shape (Fig. ...
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... (Fig. 5A,B), the neural crest cell population organized into a large halo around the neural tube and individual cells exhibited a well-spread morphology with several processes per cell. At low coating concentrations of vit- ronectin (≤1 µg/ml), the cell population was sparse and indi- vidual cells were less spread and more elongated in shape (Fig. 5C,D). A significant proportion of cells remained ...
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Citations
... The copyright holder for this preprint this version posted October 14, 2021. ; https://doi.org/10.1101/2021.10.13.464255 doi: bioRxiv preprint response to Fn and laminin (Duband & Thiery, 1982;Newgreen & Thiery, 1980;Sternberg & Kimber, 1986) via integrin receptors such as a1b1, a4b1, a5b1, aVb1 (Alfandari et al., 2003;Delannet et al., 1994;Desban & Duband, 1997;Kil et al., 1996;Lallier et al., 1994). Although neural crest cells are initially highly migratory, they remain relatively stationary upon their localization in the periocular region. ...
During development, cells aggregate at tissue boundaries to form normal tissue architecture of organs. However, how cells are segregated into tissue precursors remains largely unknown. Cornea development is a perfect example of this process whereby neural crest cells aggregate in the periocular region prior to their migration and differentiation into corneal cells. Our recent RNA-Seq analysis identified upregulation of Nephronectin (Npnt) transcripts during early stages of corneal development where its function has not been investigated. We found that Npnt mRNA and protein are expressed by various ocular tissues including the migratory periocular neural crest (pNC), which also express the integrin alpha 8 (Itgα8) receptor. Knockdown of either Npnt or Itgα8 attenuated cornea development, whereas overexpression of Npnt resulted in cornea thickening. Moreover, overexpression of Npnt variants lacking RGD binding sites did not affect corneal thickness. Neither the knockdown or augmentation of Npnt caused significant changes in cell proliferation, suggesting that Npnt directs pNC migration into the cornea. In vitro analyses showed that Npnt promotes pNC migration from explanted periocular mesenchyme, which requires Itgα8. Combined, these findings show that Npnt specifies and tunes cell migration into the presumptive cornea ECM by providing a substrate for Itgα8-positive pNC cells.
... Therefore, a constant switch between strong and weak attachment of the cell to the ECM is necessary for cell migration, as new adhesions are formed at the leading edge and old cell-ECM adhesions are disassembled (Shafqat-Abbasi et al., 2016). Thus, NCCs express several integrin receptors that are able to bind to ECM proteins like fibronectin, laminin, vitronectin, collagen and tenascin ( Fig. 1.4) (Delannet et al., 1994;McKeown et al., 2013b). These integrins are linked to cytoskeletal proteins in the NCCs and regulate migration (Testaz et al., 1999). ...
... To explore further the mechanism of the tissue response to mechanical or electromechanical stimulation, we investigated the correlation between the activation of mechanotransductive (MAPK and FAK) and osteospecific Wnt and BMP signalling pathways with of two different groups of proteins that act as "active sensors" of mechanical and electrical cues. The two groups were receptors (integrins β1, β3 and β5 and BMP receptor) [85][86][87] and ion channels sensitive to mechanical and/or electrical stimuli (KCNK, Ca 2+ L-type, TRPA1, TRPV1, Piezo1 and Piezo2) [88][89][90][91] . ...
Tendon disease constitutes an unmet clinical need and remains a critical challenge in the field of orthopaedic surgery. Innovative solutions are required to overcome the limitations of current tendon grafting approaches, and bioelectronic therapies are showing promise in the treatment of musculoskeletal disease, accelerating functional recovery through the activation of tissue regeneration signalling pathways (guided regeneration). Self-powered bioelectronic devices, and in particular piezoelectric materials represent a paradigm shift in biomedicine, negating the need for battery or external powering and complementing existing mechanotherapy to accelerate the repair processes. Here, we show the dynamic response of tendon cells to a piezoelectric collagen-analogue scaffold comprised of aligned nanoscale fibres made of the ferroelectric material poly(vinylidenefluoride-co-trifluoroethylene), (PVDF-TrFE). We demonstrate that electromechanical stimulation of tendon tissue results in guided regeneration by ion channel modulation. Finally, we show the potential of the bioelectronic device in regulating the progression of tendinopathy associated processes using a rat Achilles tendinopathy model. This study indicates that body motion-powered electromechanical stimulation can control the expression of TRPA1 and PIEZO2 receptors and stimulate tendon-specific tissue repair processes.
... I n X e n o p u s , A D A M 1 3 ( A disintegrating and metalloproteinase 13) is expressed in both premigratory and migratory NC where it assists in detachment from neuroepithelium and cleavage of ECM barriers (Alfandari et al. 2001). Expression of B1 integrin by Fox3D allows the cell to rapidly assemble and disassemble focal contacts with extracellular matrix, an essential process in directional cell migration (Delannet et al. 1994;Lallier and Bronner-Fraser 1993). ...
Neuroblastoma (NB) is an aggressive pediatric cancer that originates from neural crest tissues of the sympathetic nervous system. NB is highly heterogeneous both from a clinical and a molecular perspective. Clinically, this cancer represents a wide range of phenotypes ranging from spontaneous regression of 4S disease to unremitting treatment-refractory progression and death of high-risk metastatic disease. At a cellular level, the heterogeneous behavior of NB likely arises from an arrest and deregulation of normal neural crest development. In the present review, we summarize our current knowledge of neural crest development as it relates to pathways promoting ‘stemness’ and how deregulation may contribute to the development of tumor-initiating CSCs. There is an emerging consensus that such tumor subpopulations contribute to the evolution of drug resistance, metastasis and relapse in other equally aggressive malignancies. As relapsed, refractory disease remains the primary cause of death for neuroblastoma, the identification and targeting of CSCs or other primary drivers of tumor progression remains a critical, clinically significant goal for neuroblastoma. We will critically review recent and past evidence in the literature supporting the concept of CSCs as drivers of neuroblastoma pathogenesis.
... Indeed it has been shown that neural crest cells move along permissive ECM routes mainly supported by integrin interaction (Theveneau and Mayor, 2012). In avian trunk neural crest cells ECM components involved in migration include fibronectin, collagen, laminin and integrins (Delannet et al., 1994;Dufour et al., 1988;Newgreen, 1982;Perris and Perissinotto, 2000;Rovasio et al., 1983;Testaz and Duband, 2001). Especially fibronectin has been shown to be expressed in neural crest cell migratory pathways (Newgreen and Thiery, 1980). ...
Neural crest cells are a transient cell population, which migrates through the vertebrate embryonic body, and eventually gives rise to a many different cell types in the adult. Contact inhibition of locomotion (CIL) is a fundamental property of the collective migrating neural crest cells. CIL describes a process by which colliding cells change their direction upon collision and move away from each other, which has been linked to cell dispersion, boundary formation and metastasis. CIL is acquired in neural crest cells during Epithelial-to-Mesenchymal-Transition (EMT), by a switch in the expression of cadherins, from E to N-cadherin. To examine what governs this change I study PDGF signalling during Xenopus laevis cranial neural crest migration. Here I show that PDGFRα and its ligand PDGF-A are expressed in pre-migratory and migrating cranial neural crest cells. Inhibition of PDGF-A/PDGFRα impairs neural crest migration in vivo and cell dispersion in vitro. I find that PDGFRα inhibition leads to a decrease of N-cadherin levels in neural crest cells. Further, I demonstrate that PDGFRα signalling controls N-cadherin dependent CIL. This cellular response is controlled by the PI3K/AKT signalling pathway as a downstream effector of the PDGFRα cellular response in cranial neural crest cells. This data lead me to propose a novel mechanism by which PDGF signalling as a tissue-autonomous regulator of EMT is regulating N-cadherin dependent CIL during cranial neural crest cell migration in Xenopus laevis.
... Components of the extracellular matrix (ECM) can function to impede or promote migration, as demonstrated in vivo and ex vivo using explants of neural crest tissue, a system that recapitulates EMT and migration (see Cousin, Abbruzzese, McCusker, & Alfandari, 2012;Garcia-Castro, Marcelle, & Bronner-Fraser, 2002;Liu & Jessell, 1998;Taneyhill & Bronner-Fraser, 2005). For example, some collagens (Duband & Thiery, 1987), fibronectin (Newgreen & Thiery, 1980), hyaluronan (Casini, Nardi, & Ori, 2012;Ori, Nardini, Casini, Perris, & Nardi, 2006), and vitronectin (Delannet et al., 1994) support or promote neural crest migration, while other molecules such as versican (Perissinotto et al., 2000;Perris et al., 1996;Szabo et al., 2016), aggrecan (Perissinotto et al., 2000;Perris et al., 1996), laminin (Coles, Gammill, Miner, & Bronner-Fraser, 2006;Krotoski, Domingo, & Bronner-Fraser, 1986), other collagens (Duband & Thiery, 1987), and tenascin/cytotactin (Tan, Crossin, Hoffman, & Edelman, 1987) limit or restrict migration of neural crest cells, in a variety of species. Neural crest cells must also intermingle with other cells to give rise to a plethora of new cell types and other structures in vertebrates. ...
Our increasing comprehension of neural crest cell development has reciprocally advanced our understanding of cadherin expression, regulation, and function. As a transient population of multipotent stem cells that significantly contribute to the vertebrate body plan, neural crest cells undergo a variety of transformative processes and exhibit many cellular behaviors, including epithelial-to-mesenchymal-transition (EMT), motility, collective cell migration, and differentiation. Multiple studies have elucidated regulatory and mechanistic details of specific cadherins during neural crest cell development in a highly contextual manner. Collectively, these results reveal that gradual changes within neural crest cells are accompanied by often times subtle, yet important, alterations in cadherin expression and function. The primary focus of this review is to coalesce recent data on cadherins in neural crest cells, from their specification to their emergence as motile cells soon after EMT, and to highlight the complexities of cadherin expression beyond our current perceptions, including the hypothesis that the neural crest EMT is a transition involving a predominantly singular cadherin switch. Further advancements in genetic approaches and molecular techniques will provide greater opportunities to integrate data from various model systems in order to distinguish unique or overlapping functions of cadherins expressed at any point throughout the ontogeny of the neural crest. This article is protected by copyright. All rights reserved.
... Cell cultures and TUJ1 whole-mount immunostainings were performed as described previously 8,37 . Preparation of samples and immunostaining on paraffin and cryosections of embryos and embryonic guts were performed as described previously 32,59 . ...
Endothelin-3 (EDN3) and β1-integrins are required for the colonization of the embryonic gut by enteric neural crest cells (ENCCs) to form the enteric nervous system (ENS). β1-integrin-null ENCCs exhibit migratory defects in a region of the gut enriched in EDN3 and in specific extracellular matrix (ECM) proteins. We investigated the putative role of EDN3 on ENCC adhesion properties and its functional interaction with β1-integrins during ENS development. We show that EDN3 stimulates ENCC adhesion to various ECM components in vitro. It induces rapid changes in ENCC shape and protrusion dynamics favouring sustained growth and stabilization of lamellipodia, a process coincident with the increase in the number of focal adhesions and activated β1-integrins. In vivo studies and ex-vivo live imaging revealed that double mutants for Itgb1 and Edn3 displayed a more severe enteric phenotype than either of the single mutants demonstrated by alteration of the ENS network due to severe migratory defects of mutant ENCCs taking place early during the ENS development. Altogether, our results highlight the interplay between the EDN3 and β1-integrin signalling pathways during ENS ontogenesis and the role of EDN3 in ENCC adhesion.
... Interaction with the extracellular matrix To move forward, NCC need to make interaction with components of the extracellular matrix. For this purpose, NCC express several integrin receptors that bind to fibronectin, laminin, vitronectin, collagen and tenascin (Delannet et al., 1994;McKeown et al., 2013). Integrins are linked to cytoskeletal proteins that in turn regulate NCC migration. ...
... Neural crest cells, muscles, glial cells, epithelia, osteoclasts, and blood vessels during development or angiogenesis Delannet et al. (1994), Breuss et al. (1995), Drake et al. (1995, Isacke and Horton (2000), Kaneko et al. (2014) αIIb 125 (2011) Acting as a crucial intermediary in the transduction of signals generated by cell adhesion through integrins ...
Integrins are an important family of adhesion molecules that were first discovered two decades ago. Integrins are transmembrane heterodimeric glycoprotein receptors consisting of α and β subunits, and are comprised of an extracellular domain, a transmembrane domain, and a cytoplasmic tail. Therein, integrin cytoplasmic domains may associate directly with numerous cytoskeletal proteins and intracellular signaling molecules, which are crucial for modulating fundamental cell processes and functions including cell adhesion, proliferation, migration, and survival. The purpose of this review is to describe the unique structure of each integrin subunit, primary cytoplasmic association proteins, and transduction signaling pathway of integrins, with an emphasis on their biological functions.
... αv-containing integrins are widely expressed on many cell types, including neural crest cells, glial cells, muscle cells, osteoclasts, epithelial cells, and vascular endothelial cells during embryonic development (4)(5)(6)(7)(8) and during angiogenesis in response to tumors (9). Mouse embryos containing a null mutation in the αv gene exhibit placental defects and intracerebral hemorrhage, indicative of its important role in placentation and vasculogenesis (10,11). ...
αvβ8 is an integrin that recognizes an Arg-Gly-Asp (RGD) motif and interacts with fibronectin, vitronectin, and latent TGF-β1. We comprehensively determined the binding activity of αvβ8 integrin towards 25 secreted proteins having an RGD motif. αvβ8 integrin strongly bound to latent TGF-β1 but showed marginal activity for other RGD-containing proteins including fibronectin and vitronectin. Site-directed mutagenesis of latent TGF-β1 demonstrated that the high-affinity binding of αvβ8 integrin to latent TGF-β1 was defined by Leu-218 immediately following the RGD motif within the latency-associated peptide of TGF-β1. Consistent with the critical role of Leu-218 in latent TGF-β1 recognition by αvβ8 integrin, a 9-mer synthetic peptide containing an RGDL sequence strongly inhibited interactions of latent TGF-β1 with αvβ8 integrin, while a 9-mer peptide with an RGDA sequence was ~60-fold less inhibitory. Because αvβ3 integrin did not exhibit strong binding to latent TGF-β1 or distinguish between RGDL- and RGDA-containing peptides, we explored the mechanism by which the integrin β8 subunit defines the high-affinity binding of latent TGF-β1 by αvβ8 integrin. Production of a series of swap mutants of integrin β8 and β3 subunits indicated that the high-affinity binding of αvβ8 integrin with latent TGF-β1 was ensured by interactions between the Leu-218 residue and the β8 I-like domain, with the former serving as an auxiliary recognition residue defining the restricted ligand specificity of αvβ8 integrin towards latent TGF-β1. In support of this conclusion, high-affinity binding toward αvβ8 integrin was conferred on fibronectin by substitution of its RGDS motif with an RGDL sequence.
