Document Detail


Retinoic acid is a potential dorsalising signal in the late embryonic chick hindbrain.
MedLine Citation:
PMID:  18093305     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
BACKGROUND: Human retinoic acid teratogenesis results in malformations of dorsally derived hindbrain structures such as the cerebellum, noradrenergic hindbrain neurons and the precerebellar system. These structures originate from the rhombic lip and adjacent dorsal precursor pools that border the fourth ventricle roofplate. While retinoic acid synthesis is known to occur in the meninges that blanket the hindbrain, the particular sensitivity of only dorsal structures to disruptions in retinoid signalling is puzzling. We therefore looked for evidence within the neural tube for more spatiotemporally specific signalling pathways using an in situ hybridisation screen of known retinoic acid pathway transcripts.
RESULTS: We find that there are highly restricted domains of retinoic acid synthesis and breakdown within specific hindbrain nuclei as well as the ventricular layer and roofplate. Intriguingly, transcripts of cellular retinoic acid binding protein 1 are always found at the interface between dividing and post-mitotic cells. By contrast to earlier stages of development, domains of synthesis and breakdown in post-mitotic neurons are co-localised. At the rhombic lip, expression of the mRNA for retinoic acid synthesising and catabolising enzymes is spatially highly organised with respect to the Cath1-positive precursors of migratory precerebellar neurons.
CONCLUSION: The late developing hindbrain shows patterns of retinoic acid synthesis and use that are distinct from the well characterised phase of rostrocaudal patterning. Selected post-mitotic populations, such as the locus coeruleus, appear to both make and break down retinoic acid suggesting that a requirement for an autocrine, or at least a highly localised paracrine signalling network, might explain its acute sensitivity to retinoic acid disruption. At the rhombic lip, retinoic acid is likely to act as a dorsalising factor in parallel with other roofplate signalling pathways. While its precise role is unclear, retinoic acid is potentially well placed to regulate temporally determined cell fate decisions within the rhombic lip precursor pool.
Authors:
Leigh J Wilson; Anna Myat; Aadhar Sharma; Malcolm Maden; Richard J T Wingate
Related Documents :
9724745 - Epidermal trans-urocanic acid and the uv-a-induced photoaging of the skin.
1346245 - Induction of peroxisomal beta-oxidation genes by retinoic acid in cultured rat hepatocy...
10813875 - Spectroscopic and dynamic studies of the epidermal chromophores trans-urocanic acid and...
7064705 - Functional and morphological findings of endolymphatic sac.
23549985 - Effects of exogenous thiocyanate on mineral nutrients, antioxidative responses and free...
24778725 - A novel family of (1-aminoalkyl)(trifluoromethyl)- and -(difluoromethyl)phosphinic acid...
Publication Detail:
Type:  Journal Article     Date:  2007-12-19
Journal Detail:
Title:  BMC developmental biology     Volume:  7     ISSN:  1471-213X     ISO Abbreviation:  BMC Dev. Biol.     Publication Date:  2007  
Date Detail:
Created Date:  2008-03-11     Completed Date:  2008-03-26     Revised Date:  2014-02-19    
Medline Journal Info:
Nlm Unique ID:  100966973     Medline TA:  BMC Dev Biol     Country:  England    
Other Details:
Languages:  eng     Pagination:  138     Citation Subset:  IM    
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Descriptor/Qualifier:
Animals
Aryl Hydrocarbon Hydroxylases / biosynthesis
Body Patterning*
Chick Embryo
Gene Expression Regulation, Developmental
Immunohistochemistry
In Situ Hybridization
Retinal Dehydrogenase / biosynthesis
Retinol-Binding Proteins / biosynthesis
Rhombencephalon / embryology*,  metabolism
Signal Transduction*
Tretinoin / metabolism*
Grant Support
ID/Acronym/Agency:
G9900989//Medical Research Council
Chemical
Reg. No./Substance:
0/Retinol-Binding Proteins; 5688UTC01R/Tretinoin; EC 1.14.14.1/Aryl Hydrocarbon Hydroxylases; EC 1.14.14.1/cytochrome P-450 CYP1B1; EC 1.2.1.36/Retinal Dehydrogenase
Comments/Corrections

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


Previous Document:  Measuring the effect of intimate partner violence on health-related quality of life: a qualitative f...
Next Document:  Identifying protein complexes directly from high-throughput TAP data with Markov random fields.