scholarly journals Pronephric Duct

2020 ◽  
Author(s):  
Keyword(s):  
Pronephric Duct

scholarly journals Cadherin-17 is required to maintain pronephric duct integrity during zebrafish development

2002 ◽  
Vol 115 (1-2) ◽  
pp. 15-26 ◽  
Author(s):  
Julia Horsfield ◽  
Anassuya Ramachandran ◽  
Katja Reuter ◽  
Edward LaVallie ◽  
Lisa Collins-Racie ◽  
...  
Keyword(s):  
Zebrafish Development ◽  
Pronephric Duct

Axolotl pronephric duct cell migration is sensitive to phosphatidylinositol-specific phospholipase C

Development ◽  
1989 ◽  
Vol 105 (1) ◽  
pp. 1-7 ◽  
Author(s):  
S.L. Zackson ◽  
M.S. Steinberg
Keyword(s):  
Alkaline Phosphatase ◽  
Cell Migration ◽  
Phospholipase C ◽  
Slow Release ◽  
Surface Protein ◽  
Duct Cell ◽  
Ambystoma Mexicanum ◽  
Pronephric Duct ◽  
A Cell ◽  
Fissure Formation

On the basis of its distribution pattern in embryos of the axolotl (Ambystoma mexicanum), we recently identified alkaline phosphatase as a molecule potentially involved in guiding the migration of the pronephric duct. Alkaline phosphatase is a cell surface protein anchored to cell membranes via a covalent linkage to a phosphatidylinositol glycan (PI-G). The enzyme phosphatidylinositol-specific phospholipase C (PIPLC) specifically releases from cell surfaces molecules anchored by the PI-G linkage. In order to test the possibility that a PI-G anchored protein is involved in directing pronephric duct cell migration, PIPLC was applied to axolotl embryos. The enzyme was introduced into embryos through the use of a novel slow-release bead material, hydrolysed polyacrylamide. PIPLC blocked pronephric duct cell migration without interfering with somite fissure formation, a concurrent, neighbouring morphogenetic cell rearrangement which occurs with little if any alkaline phosphatase present. In addition, alkaline phosphatase activity was markedly diminished in the vicinity of the implanted beads. These observations suggest that at least one protein anchored to the cell membrane by a PI-G linkage, possibly alkaline phosphatase, is involved in guiding or promoting pronephric duct cell migration.

scholarly journals Expression analysis of Rab11 during zebrafish embryonic development

2019 ◽  
Author(s):  
Haijun Zhang ◽  
Yu Gao ◽  
Zhangji Dong ◽  
Wenjin Hao ◽  
Dong Liu ◽  
...  
Keyword(s):  
Nervous System ◽  
Embryonic Development ◽  
Expression Analysis ◽  
Expression Patterns ◽  
Rab Gtpase ◽  
Rab Proteins ◽  
Pharyngeal Arches ◽  
Pronephric Duct ◽  
Phylogeny Analysis ◽  
The Central Nervous System

Abstract Background: Rab proteins are GTPases responsible for intracellular vesicular trafficking regulation. Rab11 proteins, members of the Rab GTPase family, are known to regulate vesicular recycling during embryonic development. In zebrafish, there are 3 rab11 paralogues, known as rab11a, rab11ba and rab11bb, sharing high identity with each other. However, the expression analysis of rab11 is so far lacking. Results: Here, by phylogeny analysis, we found the three rab11 genes are highly conserved especially for their GTPase domains. We examined the expression patterns of rab11a, rab11ba and rab11bb using RT-PCR and in situ hybridization. We found that all the three genes were highly enriched in the central nervous system, but in different areas of the brain. Apart from brain, rab11a was also expressed in caudal vein, pronephric duct, proctodeum, pharyngeal arches and digestive duct, rab11ba was detected to express in muscle, and rab11bb was expressed in kidney, fin and spinal cord. Different from rab11a and rab11ba, which both have maternal expressions in embryos, rab11bb only expresses during 24hpf to 96hpf. Conclusions: Our results suggest that rab11 genes play important but distinct roles in the development of the nervous system in zebrafish. The findings could provide new evidences for better understanding the functions of rab11 in the development of zebrafish embryos.

Integrin alpha 6 expression is required for early nervous system development in Xenopus laevis

Development ◽  
1996 ◽  
Vol 122 (8) ◽  
pp. 2539-2554 ◽  
Author(s):  
T.E. Lallier ◽  
C.A. Whittaker ◽  
D.W. DeSimone
Keyword(s):  
Nervous System ◽  
Early Development ◽  
System Development ◽  
Cranial Nerves ◽  
Nervous System Development ◽  
Neural Plate ◽  
Pronephric Duct ◽  
Axial Defects ◽  
Integrin Alpha 6

The integrin alpha 6 subunit pairs with both the beta 1 and beta 4 subunits to form a subfamily of laminin receptors. Here we report the cDNA cloning and primary sequence for the Xenopus homologue of the mammalian integrin alpha 6 subunit. We present data demonstrating the spatial and temporal expression of alpha 6 mRNA and protein during early development. Initially, alpha 6 transcripts are expressed in the dorsal ectoderm and future neural plate at the end of gastrulation. Later in development, alpha 6 mRNAs are expressed in a variety of neural derivatives, including the developing sensory placodes (otic and olfactory) and commissural neurons within the neural tube. Integrin alpha 6 is also expressed in the elongating pronephric duct as well as a subset of the rhombencephalic neural crest, which will form the Schwann cells lining several cranial nerves (VII, VIII and X). In vivo expression of an alpha 6 antisense transcript in the animal hemisphere leads to a reduction in alpha 6 protein expression, a loss of adhesion to laminin, and severe defects in normal development. In 35% of cases, reduced levels of alpha 6 expression result in embryos that complete gastrulation normally but arrest at neurulation prior to the formation of the neural plate. In an additional 22% of cases, embryos develop with severe axial defects, including complete loss of head or tail structures. In contrast, overexpression of the alpha 6 subunit by injection of full-length mRNA has no apparent effect on embryonic development. Co-injection of antisense and sense plasmid constructs results in a partial rescue of the antisense-generated phenotypes. These data indicate that the integrin alpha 6 subunit is critical for the early development of the nervous system in amphibians.

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