Patterning of the neural ectoderm of Xenopus laevis by the amino-terminal product of hedgehog autoproteolytic cleavage

Development ◽  
1995 ◽  
Vol 121 (8) ◽  
pp. 2349-2360 ◽  
Author(s):  
C.J. Lai ◽  
S.C. Ekker ◽  
P.A. Beachy ◽  
R.T. Moon
Keyword(s):  
Gene Family ◽  
Neural Induction ◽  
Neural Tissue ◽  
Internal Deletion ◽  
Anteroposterior Patterning ◽  
Amino Terminal ◽  
Neural Genes ◽  
Neural Ectoderm ◽  
Amino Terminal Domain ◽  
Autoproteolytic Cleavage

The patterns of embryonic expression and the activities of Xenopus members of the hedgehog gene family are suggestive of role in neural induction and patterning. We report that these hedgehog polypeptides undergo autoproteolytic cleavage. Injection into embryos of mRNAs encoding Xenopus banded-hedgehog (X-bhh) or the amino-terminal domain (N) demonstrates that the direct inductive activities of X-bhh are encoded by N. In addition, both N and X-bhh pattern neural tissue by elevating expression of anterior neural genes. Unexpectedly, an internal deletion of X-bhh (delta N-C) was found to block the activity of X-bhh and N in explants and to reduce dorsoanterior structures in embryos. As elevated hedgehog activity increases the expression of anterior neural genes, and as delta N-C reduces dorsoanterior structures, these complementary data support a role for hedgehog in neural induction and anteroposterior patterning.

scholarly journals Analysis of Xwnt-4 in embryos of Xenopus laevis: a Wnt family member expressed in the brain and floor plate

Development ◽  
1992 ◽  
Vol 115 (2) ◽  
pp. 463-473 ◽  
Author(s):  
L.L. McGrew ◽  
A.P. Otte ◽  
R.T. Moon
Keyword(s):  
Gene Family ◽  
Neural Induction ◽  
Neural Tissue ◽  
Floor Plate ◽  
Specific Pattern ◽  
Northern Analysis ◽  
Sequence Motifs ◽  
Dorsal Midline ◽  
Stage Of Development ◽  
Neural Ectoderm

This study characterizes the temporal and spatial expression during early Xenopus development of Xwnt-4, a member of the Wnt gene family. The Xwnt-4 protein contains all of the sequence motifs that are hallmarks of the Wnt gene family and is 84% identical to the mouse homolog, Wnt-4. The highest level of Xwnt-4 expression occurs during the early neurula stage of development although its expression persists throughout embryogenesis and can be found in the adult testis, brain and epithelium. Consistent with its localization to head and dorsal regions of microdissected embryos, the expression of Xwnt-4 is enhanced in anterodorsalized embryos resulting from treatment with LiCl, and the expression of Xwnt-4 is suppressed in UV-ventralized embryos that lack anterior neural tissue. These results suggested that expression of Xwnt-4 is dependent on the induction of neural tissue. This idea was tested using induction experiments with dorsal or ventral ectoderm from a stage 10 embryo, recombined with dorsal marginal zone mesoderm from the same embryo. Recombinant tissue and ectoderm alone were cultured until stage 14, when Xwnt-4 expression was assayed using Northern analysis. In the recombinant assay, Xwnt-4 expression does not occur in the uninduced ectoderm but is expressed in both the dorsal and ventral recombinants. Xwnt-4 expression in neural ectoderm was confirmed in isolated, induced neural ectoderm, dissected away from the dorsal mesoderm, in a stage 12.5 embryo. Whole-mount in situ hybridization confirmed the dissection studies and demonstrated that Xwnt-4 transcripts are expressed in the dorsal midline of the midbrain, hindbrain and the floor plate of the neural tube. Collectively, the data indicate that Xwnt-4 is a unique member of the Wnt family whose expression is dependent on neural induction. The specific pattern of expression following neural induction suggests that Xwnt-4 plays a role in the early patterning events responsible in the formation of the nervous system in Xenopus.

A posteriorising factor, retinoic acid, reveals that anteroposterior patterning controls the timing of neuronal differentiation in Xenopus neuroectoderm

Development ◽  
1996 ◽  
Vol 122 (11) ◽  
pp. 3409-3418 ◽  
Author(s):  
N. Papalopulu ◽  
C. Kintner
Keyword(s):  
Retinoic Acid ◽  
Neuronal Differentiation ◽  
Neural Tissue ◽  
Neural Plate ◽  
Neural Tube Closure ◽  
Proneural Gene ◽  
Anteroposterior Patterning ◽  
Neural Genes ◽  
Tube Closure

During early development of the Xenopus central nervous system (CNS), neuronal differentiation can be detected posteriorly at neural plate stages but is delayed anteriorly until after neural tube closure. A similar delay in neuronal differentiation also occurs in the anterior neural tissue that forms in vitro when isolated ectoderm is treated with the neural inducer noggin. Here we examine the factors that control the timing of neuronal differentiation both in embryos and in neural tissue induced by noggin (noggin caps). We show that the delay in neuronal differentiation that occurs in noggin caps cannot be overcome by inhibiting the activity of the neurogenic gene, X-Delta-1, which normally inhibits neuronal differentiation, suggesting that it represents a novel level of regulation. Conversely, we show that the timing of neuronal differentiation can be changed from late to early after treating noggin caps or embryos with retinoic acid (RA), a putative posteriorising agent. Concommittal with changes in the timing of neuronal differentiation, RA suppresses the expression of anterior neural genes and promotes the expression of posterior neural genes. The level of early neuronal differentiation induced by RA alone is greatly increased by the additional expression of the proneural gene, XASH3. These results indicate that early neuronal differentiation in neuralised ectoderm requires posteriorising signals, as well as signals that promote the activity of proneural genes such as XASH3. In addition, these result suggest that neuronal differentiation is controlled by anteroposterior (A-P) patterning, which exerts a temporal control on the onset of neuronal differentiation.

scholarly journals XASH genes promote neurogenesis in Xenopus embryos

Development ◽  
1994 ◽  
Vol 120 (12) ◽  
pp. 3649-3655 ◽  
Author(s):  
B. Ferreiro ◽  
C. Kintner ◽  
K. Zimmerman ◽  
D. Anderson ◽  
W.A. Harris
Keyword(s):  
Neural Development ◽  
Neural Induction ◽  
Neural Tissue ◽  
Neural Plate ◽  
Binding Partner ◽  
Helix Loop Helix ◽  
Neural Genes ◽  
Dorsal Ectoderm ◽  
Bhlh Transcription Factors ◽  
Beta Tubulin Gene

Neural development in Drosophila is promoted by a family of basic helix-loop-helix (bHLH) transcription factors encoded within the Achaete Scute-Complex (AS-C). XASH-3, a Xenopus homolog of the Drosophila AS-C genes, is expressed during neural induction within a portion of the dorsal ectoderm that gives rise to the neural plate and tube. Here, we show that XASH-3, when expressed with the promiscuous binding partner XE12, specifically activates the expression of neural genes in naive ectoderm, suggesting that XASH-3 promotes neural development. Moreover, XASH-3/XE12 RNA injections into embryos lead to hypertrophy of the neural tube. Interestingly, XASH-3 misexpression does not lead to the formation of ectopic neural tissue in ventral regions, suggesting that the domain of XASH proneural function is restricted in the embryo. In contrast to the neural inducer noggin, which permanently activates the NCAM gene, the activation of neural genes by XASH-3/XE12 is not stable in naive ectoderm, yet XASH-3/XE12 powerfully and stably activates NCAM, Neurofilament and type III beta-tubulin gene expression in noggin-treated ectoderm. These results show that the XASH-3 promotes neural development, and suggest that its activity depends on additional factors which are induced in ectoderm by factors such as noggin.

scholarly journals Establishing embryonic territories in the context of Wnt signaling

2020 ◽  
Vol 52 ◽  
Author(s):  
Ian Velloso ◽  
Lorena A. Maia ◽  
Nathalia G. Amado ◽  
Alice H. Reis ◽  
Xi He ◽  
...  
Keyword(s):  
Wnt Pathway ◽  
Neural Induction ◽  
Neural Tissue ◽  
Research Groups ◽  
Major Player ◽  
History Of ◽  
Neural Ectoderm ◽  
Trunk Organizer ◽  
Early Gastrula ◽  
Developmental Windows

This review highlights the work that my research group has been developing, together with international collaborators, during the last decade. Since we were able to establish Xenopus laevis experimental model in Brazil we have been focused on understanding early embryonic patterns regarding neural induction and axes establishment. In this context, Wnt pathway appears as a major player and has been much explored by us and other research groups. Here we chose to review three published works that we consider landmarks within the history of our research on the developmental biology field and the neural induction and patterning modern findings. We intend to show how our series of discoveries, when painted together, tells a story that covers crucial developmental windows of early differentiation paths of anterior neural tissue. Being those: 1. Establishing Head organizer in contrast to trunk organizer at early gastrula; 2. deciding between neural ectoderm and epidermis ectoderm at the blastula/gastrula stages, and 3. the gathering of prechordal unique properties at late gastrula/early neurula.

Characterization of a Mode of Specific Binding of Fibrin Monomer through its Amino-Terminal Domain by Macrophages and Macrophage Cell-Lines

1990 ◽  
Vol 63 (02) ◽  
pp. 193-203 ◽  
Author(s):  
John R Shainoff ◽  
Deborah J Stearns ◽  
Patricia M DiBello ◽  
Youko Hishikawa-Itoh
Keyword(s):  
Peritoneal Macrophages ◽  
Affinity Binding ◽  
Macrophage Cell ◽  
High Affinity Binding ◽  
Amino Terminal ◽  
High Affinity ◽  
Terminal Domain ◽  
Weak Binding ◽  
Amino Terminal Domain

SummaryThe studies reported here probe the existence of a receptor-mediated mode of fibrin-binding by macrophages that is associated with the chemical change underlying the fibrinogen-fibrin conversion (the release of fibrinopeptides from the amino-terminal domain) without depending on fibrin-aggregation. The question is pursued by 1) characterization of binding in relation to fibrinopeptide content of both the intact protein and the CNBr-fragment comprising the amino-terminal domain known as the NDSK of the protein, 2) tests of competition for binding sites, and 3) photo-affinity labeling of macrophage surface proteins. The binding of intact monomers of types lacking either fibrinopeptide A alone (α-fibrin) or both fibrinopeptides A and B (αβ-fibrin) by peritoneal macrophages is characterized as proceeding through both a fibrin-specific low density/high affinity (BMAX ≃ 200–800 molecules/cell, KD ≃ 10−12 M) interaction that is not duplicated with fibrinogen, and a non-specific high density/low affinity (BMAX ≥ 105 molecules/cell, KD ≥ 10−6 M) interaction equivalent to the weak binding of fibrinogen. Similar binding characteristics are displayed by monocyte/macrophage cell lines (J774A.1 and U937) as well as peritoneal macrophages towards the NDSK preparations of these proteins, except for a slightly weaker (KD ≃ 10−10 M) high-affinity binding. The high affinity binding of intact monomer is inhibitable by fibrin-NDSK, but not fibrinogen-NDSK. This binding appears principally dependent on release of fibrinopeptide-A, because a species of fibrin (β-fibrin) lacking fibrinopeptide-B alone undergoes only weak binding similar to that of fibrinogen. Synthetic Gly-Pro-Arg and Gly-His-Arg-Pro corresponding to the N-termini of to the α- and the β-chains of fibrin both inhibit the high affinity binding of the fibrin-NDSKs, and the cell-adhesion peptide Arg-Gly-Asp does not. Photoaffinity-labeling experiments indicate that polypeptides with elec-trophoretically estimated masses of 124 and 187 kDa are the principal membrane components associated with specifically bound fibrin-NDSK. The binding could not be up-regulated with either phorbol myristyl acetate, interferon gamma or ADP, but was abolished by EDTA and by lipopolysaccharide. Because of the low BMAX, it is suggested that the high-affinity mode of binding characterized here would be too limited to function by itself in scavenging much fibrin, but may act cooperatively with other, less limited modes of fibrin binding.

scholarly journals Role of Amino-Terminal Domain in the Assembly Mechanism of Kainate-Subtype Glutamate Receptor Ion Channels

2014 ◽  
Vol 106 (2) ◽  
pp. 151a
Author(s):  
Sagar Chittori ◽  
Janesh Kumar ◽  
Suvendu Lomash ◽  
Huaying Zhao ◽  
Peter Schuck ◽  
...  
Keyword(s):  
Ion Channels ◽  
Glutamate Receptor ◽  
Amino Terminal ◽  
Terminal Domain ◽  
Assembly Mechanism ◽  
Amino Terminal Domain
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