Urokinase-type plasminogen activator regulates cranial neural crest cell migration in vitro

Collapsin-1 belongs to the Semaphorin family of molecules, several members of which have been implicated in the co-ordination of axon growth and guidance. Collapsin-1 can function as a selective chemorepellent for sensory neurons, however, its early expression within the somites and the cranial neural tube (Shepherd, I., Luo, Y., Raper, J. A. and Chang, S. (1996) Dev. Biol. 173, 185–199) suggest that it might contribute to the control of additional developmental processes in the chick. We now report a detailed study on the expression of collapsin-1 as well as on the distribution of collapsin-1-binding sites in regions where neural crest cell migration occurs. collapsin-1 expression is detected in regions bordering neural crest migration pathways in both the trunk and hindbrain regions and a receptor for collapsin-1, neuropilin-1, is expressed by migrating crest cells derived from both regions. When added to crest cells in vitro, a collapsin-1-Fc chimeric protein induces morphological changes similar to those seen in neuronal growth cones. In order to test the function of collapsin-1 on the migration of neural crest cells, an in vitro assay was used in which collapsin-1-Fc was immobilised in alternating stripes consisting of collapsin-Fc/fibronectin versus fibronectin alone. Explanted neural crest cells derived from both trunk and hindbrain regions avoided the collapsin-Fc-containing substratum. These results suggest that collapsin-1 signalling can contribute to the patterning of neural crest cell migration in the developing chick.

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Biologically active synthetic peptides as probes of embryonic development: a competitive peptide inhibitor of fibronectin function inhibits gastrulation in amphibian embryos and neural crest cell migration in avian embryos.

The Journal of Cell Biology ◽

10.1083/jcb.99.5.1822 ◽

1984 ◽

Vol 99 (5) ◽

pp. 1822-1830 ◽

Cited By ~ 270

Author(s):

J C Boucaut ◽

T Darribère ◽

T J Poole ◽

H Aoyama ◽

K M Yamada ◽

...

Keyword(s):

Cell Migration ◽

Neural Crest ◽

Synthetic Peptides ◽

Neural Crest Cell ◽

Extracellular Proteins ◽

Biologically Active ◽

Recognition Sequence ◽

Neural Crest Cell Migration ◽

Crest Cell

We describe a new method for analyzing embryonic events dependent on a specific peptide recognition signal. A short, specific amino acid sequence in fibronectin has been implicated as a recognition site in fibronectin-mediated interactions. Fibroblast adhesion to fibronectin is competitively inhibited by certain synthetic peptides, including the decapeptide Arg-Gly-Asp-Ser-Pro-Ala-Ser-Ser-Lys-Pro, which appears to contain the cell recognition sequence. We found that this peptide inhibited both amphibian gastrulation and avian neural crest cell migration in vivo, as well as the attachment and migration of neural crest cells in vitro. These processes are major cell migratory events previously suggested to involve fibronectin. Negative controls included another conserved fibronectin peptide from the collagen-binding region containing the sequence Cys-Gln-Asp-Ser-Glu-Thr-Arg-Thr-Phe-Tyr and another peptide. Our results demonstrate the feasibility of using synthetic peptides directed at recognition sites in extracellular proteins as probes of morphogenetic processes, and they provide further support for the hypothesis that fibronectin is involved in gastrulation and neural crest cell migration.

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The Wnt Co-Receptor Lrp5 Is Required for Cranial Neural Crest Cell Migration in Zebrafish

PLoS ONE ◽

10.1371/journal.pone.0131768 ◽

2015 ◽

Vol 10 (6) ◽

pp. e0131768 ◽

Cited By ~ 20

Author(s):

Bernd Willems ◽

Shijie Tao ◽

Tingsheng Yu ◽

Ann Huysseune ◽

Paul Eckhard Witten ◽

...

Keyword(s):

Cell Migration ◽

Neural Crest ◽

Neural Crest Cell ◽

Cranial Neural Crest ◽

Cranial Neural Crest Cell ◽

Neural Crest Cell Migration ◽

Crest Cell

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Evidence for a novel enzymatic mechanism of neural crest cell migration on extracellular glycoconjugate matrices.

The Journal of Cell Biology ◽

10.1083/jcb.102.2.432 ◽

1986 ◽

Vol 102 (2) ◽

pp. 432-441 ◽

Cited By ~ 83

Author(s):

R B Runyan ◽

G D Maxwell ◽

B D Shur

Keyword(s):

Cell Migration ◽

Cell Surface ◽

Neural Crest ◽

Basal Lamina ◽

Neural Crest Cell ◽

Neural Crest Cells ◽

Neural Crest Cell Migration ◽

Dose Dependent ◽

Crest Cell

Migrating embryonic cells have high levels of cell surface galactosyltransferase (GalTase) activity. It has been proposed that GalTase participates during migration by recognizing and binding to terminal N-acetylglucosamine (GlcNAc) residues on glycoconjugates within the extracellular matrix (Shur, B. D., 1982, Dev. Biol. 91:149-162). We tested this hypothesis using migrating neural crest cells as an in vitro model system. Cell surface GalTase activity was perturbed using three independent sets of reagents, and the effects on cell migration were analyzed by time-lapse microphotography. The GalTase modifier protein, alpha-lactalbumin (alpha-LA), was used to inhibit surface GalTase binding to terminal GlcNAc residues in the underlying substrate. alpha-LA inhibited neural crest cell migration on basal lamina-like matrices in a dose-dependent manner, while under identical conditions, alpha-LA had no effect on cell migration on fibronectin. Control proteins, such as lysozyme (structurally homologous to alpha-LA) and bovine serum albumin, did not effect migration on either matrix. Second, the addition of competitive GalTase substrates significantly inhibited neural crest cell migration on basal lamina-like matrices, but as above, had no effect on migration on fibronectin. Comparable concentrations of inappropriate sugars also had no effect on cell migration. Third, addition of the GalTase catalytic substrate, UDPgalactose, produced a dose-dependent increase in the rate of cell migration. Under identical conditions, the inappropriate sugar nucleotide, UDPglucose, had no effect. Quantitative enzyme assays confirmed the presence of GalTase substrates in basal lamina matrices, their absence in fibronectin matrices, and the ability of alpha-LA to inhibit GalTase activity towards basal lamina substrates. Laminin was found to be a principle GalTase substrate in the basal lamina, and when tested in vitro, alpha-LA inhibited cell migration on laminin. Together, these experiments show that neural crest cells have at least two distinct mechanisms for interacting with the substrate during migration, one that is fibronectin-dependent and one that uses GalTase recognition of basal lamina glycoconjugates.

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Essential functions of the ADAM13 cytoplasmic domain in cranial neural crest cell migration

Developmental Biology ◽

10.1016/j.ydbio.2011.05.268 ◽

2011 ◽

Vol 356 (1) ◽

pp. 197

Author(s):

Genevieve Abbruzzese ◽

Hélène Cousin ◽

Dominique Alfandari

Keyword(s):

Cell Migration ◽

Neural Crest ◽

Neural Crest Cell ◽

Cytoplasmic Domain ◽

Cranial Neural Crest ◽

Cranial Neural Crest Cell ◽

Neural Crest Cell Migration ◽

Crest Cell

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Cell surface beta 1,4-galactosyltransferase functions during neural crest cell migration and neurulation in vivo

The Journal of Cell Biology ◽

10.1083/jcb.117.2.369 ◽

1992 ◽

Vol 117 (2) ◽

pp. 369-382 ◽

Cited By ~ 36

Author(s):

HJ Hathaway ◽

BD Shur

Keyword(s):

Cell Migration ◽

Cell Surface ◽

Neural Crest ◽

Basal Lamina ◽

Neural Tube ◽

Neural Crest Cell ◽

Cranial Neural Crest Cell ◽

Neural Crest Cell Migration ◽

Crest Cell

Mesenchymal cell migration and neurite outgrowth are mediated in part by binding of cell surface beta 1,4-galactosyltransferase (GalTase) to N-linked oligosaccharides within the E8 domain of laminin. In this study, we determined whether cell surface GalTase functions during neural crest cell migration and neural development in vivo using antibodies raised against affinity-purified chicken serum GalTase. The antibodies specifically recognized two embryonic proteins of 77 and 67 kD, both of which express GalTase activity. The antibodies also immunoprecipitated and inhibited chick embryo GalTase activity, and inhibited neural crest cell migration on laminin matrices in vitro. Anti-GalTase antibodies were microinjected into the head mesenchyme of stage 7-9 chick embryos or cranial to Henson's node of stage 6 embryos. Anti-avian GalTase IgG decreased cranial neural crest cell migration on the injected side but did not cross the embryonic midline and did not affect neural crest cell migration on the uninjected side. Anti-avian GalTase Fab crossed the embryonic midline and perturbed cranial neural crest cell migration throughout the head. Neural fold elevation and neural tube closure were also disrupted by Fab fragments. Cell surface GalTase was localized to migrating neural crest cells and to the basal surfaces of neural epithelia by indirect immunofluorescence, whereas GalTase was undetectable on neural crest cells prior to migration. These results suggest that, during early embryogenesis, cell surface GalTase participates during neural crest cell migration, perhaps by interacting with laminin, a major component of the basal lamina. Cell surface GalTase also appears to play a role in neural tube formation, possibly by mediating neural epithelial adhesion to the underlying basal lamina.

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