scholarly journals Distribution of a putative cell surface receptor for fibronectin and laminin in the avian embryo.

1986 ◽  
Vol 103 (3) ◽  
pp. 1061-1071 ◽  
Author(s):  
D M Krotoski ◽  
C Domingo ◽  
M Bronner-Fraser
Keyword(s):  
Cell Surface ◽  
Neural Crest ◽  
Neural Crest Cell ◽  
Neural Crest Cells ◽  
Basement Membranes ◽  
Cell Surface Receptor ◽  
Avian Embryo ◽  
Epithelial Tissues ◽  
Surface Receptor ◽  
Neural Crest Migration

The cell substratum attachment (CSAT) antibody recognizes a 140-kD cell surface receptor complex involved in adhesion to fibronectin (FN) and laminin (LM) (Horwitz, A., K. Duggan, R. Greggs, C. Decker, and C. Buck, 1985, J. Cell Biol., 101:2134-2144). Here, we describe the distribution of the CSAT antigen along with FN and LM in the early avian embryo. At the light microscopic level, the staining patterns for the CSAT receptor and the extracellular matrix molecules to which it binds were largely codistributed. The CSAT antigen was observed on numerous tissues during gastrulation, neurulation, and neural crest migration: for example, the surface of neural crest cells and the basal surface of epithelial tissues such as the ectoderm, neural tube, notochord, and dermomyotome. FN and LM immunoreactivity was observed in the basement membranes surrounding many of these epithelial tissues, as well as around the otic and optic vesicles. In addition, the pathways followed by cranial neural crest cells were lined with FN and LM. In the trunk region, FN and LM were observed surrounding a subpopulation of neural crest cells. However, neither molecule exhibited the selective distribution pattern necessary for a guiding role in trunk neural crest migration. The levels of CSAT, FN, and LM are dynamic in the embryo, perhaps reflecting that the balance of surface-substratum adhesions contributes to initiation, migration, and localization of some neural crest cell populations.

Glycoconjugates mark a transient barrier to neural crest migration in the chicken embryo

Development ◽  
1994 ◽  
Vol 120 (1) ◽  
pp. 103-114 ◽  
Author(s):  
R.A. Oakley ◽  
C.J. Lasky ◽  
C.A. Erickson ◽  
K.W. Tosney
Keyword(s):  
Neural Crest ◽  
Neural Crest Cell ◽  
Neural Crest Cells ◽  
Experimental Manipulation ◽  
Binding Activity ◽  
Cell Entry ◽  
Avian Embryo ◽  
Peanut Agglutinin ◽  
Neural Crest Migration ◽  
Crest Cell

We report that two molecular markers correlate with a transient inhibition of neural crest cell entry into the dorsolateral path between the ectoderm and the somite in the avian embryo. During the period when neural crest cells are excluded from the dorsolateral path, both peanut agglutinin lectin (PNA)-binding activity and chondroitin-6-sulfate (C6S) immunoreactivity are expressed within this path. Both markers decline as neural crest cells enter. Moreover, both markers are absent after an experimental manipulation that accelerates neural crest entry into this path. Specifically, dermamyotome deletions abolish expression of both markers and allow neural crest cells to enter the dorsolateral path precociously. After partial deletions, dermatome remnants remain. These remnants retain PNA and C6S labeling and impede migration locally. Local glycoconjugate expression thus correlates directly with avoidance responses. Since both PNA-binding activity and C6S expression also typify inhibitory somitic tissues, molecules indicated by these markers (or co-regulated molecules) are likely to inhibit both neural crest and axon advance.

Evidence for collapsin-1 functioning in the control of neural crest migration in both trunk and hindbrain regions

Development ◽  
1999 ◽  
Vol 126 (10) ◽  
pp. 2181-2189 ◽  
Author(s):  
B.J. Eickholt ◽  
S.L. Mackenzie ◽  
A. Graham ◽  
F.S. Walsh ◽  
P. Doherty
Keyword(s):  
Cell Migration ◽  
Neural Crest ◽  
Neural Crest Cell ◽  
Axon Growth ◽  
Neural Crest Cells ◽  
Neural Crest Cell Migration ◽  
Neural Crest Migration ◽  
Migration Pathways ◽  
Crest Cell

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.

An SEM analysis of neural crest migration in the mouse

Development ◽  
1983 ◽  
Vol 74 (1) ◽  
pp. 97-118
Author(s):  
C. A. Erickson ◽  
J. A. Weston
Keyword(s):  
Neural Crest ◽  
Basal Lamina ◽  
Neural Tube ◽  
Neural Crest Cells ◽  
Sem Analysis ◽  
Basement Membranes ◽  
Dorsal Neural Tube ◽  
Trunk Neural Crest ◽  
Unique Cell ◽  
Neural Crest Migration

The cellular morphology and migratory pathways of the trunk neural crest are described in normal mouse embryos, and in embryos homozygous for Patch in which neural crest derivatives develop abnormally. Trunk neural crest cells initially appear in 8½-day embryos as a unique cell population on the dorsal neural tube surface and are relatively rounded. Once they begin to migrate the cells flatten and orient somewhat tangentially to the neural tube, and advance ventrad between the somites and neural tube. At the onset of migration neural crest cells extend lamellipodia onto the surface of the tube while detaching their trailing processes from the lumenal surface. The basal lamina on the dorsal neural tube is discontinuous when cell migration begins in this region. As development proceeds, the basal lamina gradually becomes continuous from a lateral to dorsal direction and neural crest emigration is progressively confined to the narrowing region of discontinuous basal lamina. Cell separation from the neural tube ceases concomitant with completion of a continuous basement membrane. Preliminary observations of the mutant embryos reveal that abnormal extracellular spaces appear and patterns of crest migration are subsequently altered. We conclude that the extracellular matrix, extracellular spaces and basement membranes may delimit crest migration in the mouse.

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

1986 ◽  
Vol 102 (2) ◽  
pp. 432-441 ◽  
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.

scholarly journals The distribution of tenascin coincides with pathways of neural crest cell migration

Development ◽  
1988 ◽  
Vol 102 (1) ◽  
pp. 237-250 ◽  
Author(s):  
E.J. Mackie ◽  
R.P. Tucker ◽  
W. Halfter ◽  
R. Chiquet-Ehrismann ◽  
H.H. Epperlein
Keyword(s):  
Xenopus Laevis ◽  
Neural Crest ◽  
Neural Crest Cell ◽  
Neural Crest Cells ◽  
Rat Embryos ◽  
The Matrix ◽  
Neural Crest Cell Migration ◽  
Neural Crest Migration ◽  
Migration Pathways

The distribution of the extracellular matrix (ECM) glycoprotein, tenascin, has been compared with that of fibronectin in neural crest migration pathways of Xenopus laevis, quail and rat embryos. In all species studied, the distribution of tenascin, examined by immunohistochemistry, was more closely correlated with pathways of migration than that of fibronectin, which is known to be important for neural crest migration. In Xenopus laevis embryos, anti-tenascin stained the dorsal fin matrix and ECM along the ventral route of migration, but not the ECM found laterally between the ectoderma and somites where neural crest cells do not migrate. In quail embryos, the appearance of tenascin in neural crest pathways was well correlated with the anterior-to-posterior wave of migration. The distribution of tenascin within somites was compared with that of the neural crest marker, HNK-1, in quail embryos. In the dorsal halves of quail somites which contained migrating neural crest cells, the predominant tenascin staining was in the anterior halves of the somites, codistributed with the migrating cells. In rat embryos, tenascin was detectable in the somites only in the anterior halves. Tenascin was not detectable in the matrix of cultured quail neural crest cells, but was in the matrix surrounding somite and notochord cells in vitro. Neural crest cells cultured on a substratum of tenascin did not spread and were rounded. We propose that tenascin is an important factor controlling neural crest morphogenesis, perhaps by modifying the interaction of neural crest cells with fibronectin.

Effects of HNK-1 monoclonal antibody on the substratum attachment and survival of neural crest and sclerotome cells in culture

1988 ◽  
Vol 90 (1) ◽  
pp. 115-122
Author(s):  
E.J. Sanders ◽  
E. Cheung
Keyword(s):  
Monoclonal Antibody ◽  
Cell Surface ◽  
Neural Crest ◽  
Neurite Outgrowth ◽  
Mixed Culture ◽  
Binding Sites ◽  
Neural Crest Cell ◽  
Cell Spreading ◽  
Neural Crest Cells ◽  
Crest Cell

The sclerotome portion of the differentiating embryonic chick somite becomes infiltrated by neural crest cells prior to its dispersal towards the embryonic axis. This means that sclerotome cells explanted into culture for the purpose of examining their interactions in vitro are contaminated with a proportion of neural crest cells. The purpose of this study was to explore the neural crest cell adhesion epitope recognized by the HNK-1 monoclonal antibody and ways in which this antibody can be used to eliminate neural crest cells from mixed culture by selective cytotoxicity. Immunofluorescence technique, under the conditions used here, indicated that the antibody appeared to stain all the mesenchymal (i.e. neural crest) cells emigrating from pieces of embryonic neural tube in culture. Examination of the effects of HNK-1 suggests that the antibody interacts with substratum-binding sites on the neural crest cell surface. On fibronectin-coated substrata the antibody tended to inhibit neurite outgrowth but left the cells relatively well spread, while on laminin substrata the effect was to discourage both neurite extension and cell spreading, causing cell retraction. These results suggest that the cell surface epitope recognized by HNK-1 influences neurite outgrowth, neurite adhesiveness or both. Failure of cell spreading on laminin suggests interaction with the laminin binding sites on the cell body. Elimination of the crest cells from mixed culture with sclerotome was achieved by culturing the cells in the presence of HNK-1 antibody and complement during the period required for complete cell outgrowth from the sclerotome explant.(ABSTRACT TRUNCATED AT 250 WORDS)

Distinct roles for dystroglycan, (β)1 integrin and perlecan in cell surface laminin organization

2001 ◽  
Vol 114 (6) ◽  
pp. 1137-1144 ◽  
Author(s):  
M.D. Henry ◽  
J.S. Satz ◽  
C. Brakebusch ◽  
M. Costell ◽  
E. Gustafsson ◽  
...  
Keyword(s):  
Cell Surface ◽  
Es Cells ◽  
Embryonic Stem ◽  
Basement Membranes ◽  
Cell Surface Receptor ◽  
Complex Structures ◽  
Assembly Process ◽  
Matrix Assembly ◽  
Surface Receptor ◽  
Laminin 1

Dystroglycan (DG) is a cell surface receptor for several extracellular matrix (ECM) molecules including laminins, agrin and perlecan. Recent data indicate that DG function is required for the formation of basement membranes in early development and the organization of laminin on the cell surface. Here we show that DG-mediated laminin clustering on mouse embryonic stem (ES) cells is a dynamic process in which clusters are consolidated over time into increasingly more complex structures. Utilizing various null-mutant ES cell lines, we define roles for other molecules in this process. In (β)1 integrin-deficient ES cells, laminin-1 binds to the cell surface, but fails to organize into more morphologically complex structures. This result indicates that (β)1 integrin function is required after DG function in the cell surface-mediated laminin assembly process. In perlecan-deficient ES cells, the formation of complex laminin-1 structures is defective, implicating perlecan in the laminin matrix assembly process. Moreover, laminin and perlecan reciprocally modulate the organization of the other on the cell surface. Taken together, the data support a model whereby DG serves as a receptor essential for the initial binding of laminin on the cell surface, whereas (β)1 integrins and perlecan are required for laminin matrix assembly processes after it binds to the cell.

scholarly journals An in vitro assay for neural crest cell migration through the somites

Development ◽  
1986 ◽  
Vol 98 (1) ◽  
pp. 85-97
Author(s):  
Georgia Guillory ◽  
Marianne Bronner-Fraser
Keyword(s):  
Neural Crest ◽  
Neural Crest Cell ◽  
Neural Crest Cells ◽  
Enzymatic Digestion ◽  
Pigment Cells ◽  
Avian Embryo ◽  
Vitro Assay ◽  
Neural Crest Cell Migration ◽  
Migratory Routes

Neural crest cells in the trunk of the avian embryo come into contact with the somites and neural tube during the course of their migration. However, the relationship between the somites and the early migratory routes followed by these cells is not yet completely understood. Here, we use a tissue culture assay to examine if avian neural crest cells migrate through the somites. Cultures of quail somites were prepared from four adjacent regions along the neural axis in the trunk. Each region had four pairs of consecutive somites with region I being most anterior and region IV containing the last four segments. Within each region, the somites were separated from other tissues by enzymatic digestion and plated onto collagen-coated dishes. Immuno-cytochemical techniques were used to confirm that no neural crest cells, recognized by the HNK-1 antibody, were present on the surface of the somites at the time of explantation. After several days in culture, the explanted somites were screened to identify pigment cells. Because neural crest cells give rise to all of the melanocytes in the trunk, the presence of pigment cells indicated that neural crest precursors were contained within the initial explant. After 5–11 days in vitro, the percentage of somite cultures containing pigment cells in regions I through IV, respectively, was 36%, 51%, 31% and 1%. These results suggest that neural crest cells migrate through the somitic mesenchyme and first enter the somites between 5 to 9 segments rostral to the most recently formed somite.

scholarly journals T-cadherin expression alternates with migrating neural crest cells in the trunk of the avian embryo

Development ◽  
1991 ◽  
Vol 111 (1) ◽  
pp. 15-22 ◽  
Author(s):  
B. Ranscht ◽  
M. Bronner-Fraser
Keyword(s):  
Cell Migration ◽  
Neural Crest ◽  
Neural Crest Cell ◽  
Neural Crest Cells ◽  
Small Population ◽  
Avian Embryo ◽  
Caudal Portion ◽  
Neural Crest Cell Migration ◽  
Trunk Neural Crest ◽  
Crest Cell

Trunk neural crest cells and motor axons move in a segmental fashion through the rostral (anterior) half of each somitic sclerotome, avoiding the caudal (posterior) half. This metameric migration pattern is thought to be caused by molecular differences between the rostral and caudal portions of the somite. Here, we describe the distribution of T-cadherin (truncated-cadherin) during trunk neural crest cell migration. T-cadherin, a novel member of the cadherin family of cell adhesion molecules was selectively expressed in the caudal half of each sclerotome at all times examined. T-cadherin immunostaining appeared graded along the rostrocaudal axis, with increasing levels of reactivity in the caudal halves of progressively more mature (rostral) somites. The earliest T-cadherin expression was detected in a small population of cells in the caudal portion of the somite three segments rostral to last-formed somite. This initial T-cadherin expression was observed concomitant with the invasion of the first neural crest cells into the rostral portion of the same somite in stage 16 embryos. When neural crest cells were ablated surgically prior to their emigration from the neural tube, the pattern of T-cadherin immunoreactivity was unchanged compared to unoperated embryos, suggesting that the metameric T-cadherin distribution occurs independent of neural crest cell signals. This expression pattern is consistent with the possibility that T-cadherin plays a role in influencing the pattern of neural crest cell migration and in maintaining somite polarity.

Mesodermal defects and cranial neural crest apoptosis in alpha5 integrin-null embryos

Development ◽  
1997 ◽  
Vol 124 (21) ◽  
pp. 4309-4319 ◽  
Author(s):  
K.L. Goh ◽  
J.T. Yang ◽  
R.O. Hynes
Keyword(s):  
Cell Proliferation ◽  
Cell Death ◽  
Neural Crest ◽  
Neural Crest Cells ◽  
Cell Surface Receptor ◽  
Cranial Neural Crest ◽  
Wild Type ◽  
Surface Receptor ◽  
Cranial Neural Crest Cells

Alpha5beta1 integrin is a cell surface receptor that mediates cell-extracellular matrix adhesions by interacting with fibronectin. Alpha5 subunit-deficient mice die early in gestation and display mesodermal defects; most notably, embryos have a truncated posterior and fail to produce posterior somites. In this study, we report on the in vivo effects of the alpha5-null mutation on cell proliferation and survival, and on mesodermal development. We found no significant differences in the numbers of apoptotic cells or in cell proliferation in the mesoderm of alpha5-null embryos compared to wild-type controls. These results suggest that changes in overall cell death or cell proliferation rates are unlikely to be responsible for the mesodermal deficits seen in the alpha5-null embryos. No increases in cell death were seen in alpha5-null embryonic yolk sac, amnion and allantois compared with wild-type, indicating that the mutant phenotype is not due to changes in apoptosis rates in these extraembryonic tissues. Increased numbers of dying cells were, however, seen in migrating cranial neural crest cells of the hyoid arch and in endodermal cells surrounding the omphalomesenteric artery in alpha5-null embryos, indicating that these subpopulations of cells are dependent on alpha5 integrin function for their survival. Mesodermal markers mox-1, Notch-1, Brachyury (T) and Sonic hedgehog (Shh) were expressed in the mutant embryos in a regionally appropriate fashion. Both T and Shh, however, showed discontinuous expression in the notochords of alpha5-null embryos due to (1) degeneration of the notochordal tissue structure, and (2) non-maintenance of gene expression. Consistent with the disorganization of notochordal signals in the alpha5-null embryos, reduced Pax-1 expression and misexpression of Pax-3 were observed. Anteriorly expressed HoxB genes were expressed normally in the alpha5-null embryos. However, expression of the posteriormost HoxB gene, Hoxb-9, was reduced in alpha5-null embryos. These results suggest that alpha5beta1-fibronectin interactions are not essential for the initial commitment of mesodermal cells, but are crucial for maintenance of mesodermal derivatives during postgastrulation stages and also for the survival of some neural crest cells.

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