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|Title:||Two very long chain fatty acid acyl-CoA synthetase genes, acs-20 and acs-22, have roles in the cuticle surface barrier in Caenorhabditis elegans||Authors:||Kage-Nakadai E.
|Keywords:||fatty acid transporter 4
long chain fatty acid coenzyme A ligase
very long chain fatty acid
acs 20 gene
acs 22 gene
transmission electron microscopy
Coenzyme A Ligases
Fatty Acid Transport Proteins
|Issue Date:||2010||Citation:||Kage-Nakadai E., Kobuna H., Kimura M., Gengyo-Ando K., Inoue T., Arai H., Mitani S. (2010). Two very long chain fatty acid acyl-CoA synthetase genes, acs-20 and acs-22, have roles in the cuticle surface barrier in Caenorhabditis elegans. PLoS ONE 5 (1) : e8857. ScholarBank@NUS Repository. https://doi.org/10.1371/journal.pone.0008857||Abstract:||In multicellular organisms, the surface barrier is essential for maintaining the internal environment. In mammals, the barrier is the stratum corneum. Fatty acid transport protein 4 (FATP4) is a key factor involved in forming the stratum corneum barrier. Mice lacking Fatp4 display early neonatal lethality with features such as tight, thick, and shiny skin, and a defective skin barrier. These symptoms are strikingly similar to those of a human skin disease called restrictive dermopathy. FATP4 is a member of the FATP family that possesses acyl-CoA synthetase activity for very long chain fatty acids. How Fatp4 contributes to skin barrier function, however, remains to be elucidated. In the present study, we characterized two Caenorhabditis elegans genes, acs-20 and acs-22, that are homologous to mammalian FATPs. Animals with mutant acs-20 exhibited defects in the cuticle barrier, which normally prevents the penetration of small molecules. acs-20 mutant animals also exhibited abnormalities in the cuticle structure, but not in epidermal cell fate or cell integrity. The acs-22 mutants rarely showed a barrier defect, whereas acs-20;acs-22 double mutants had severely disrupted barrier function. Moreover, the barrier defects of acs-20 and acs-20;acs-22 mutants were rescued by acs-20, acs-22, or human Fatp4 transgenes. We further demonstrated that the incorporation of exogenous very long chain fatty acids into sphingomyelin was reduced in acs-20 and acs-22 mutants. These findings indicate that C. elegans Fatp4 homologue(s) have a crucial role in the surface barrier function and this model might be useful for studying the fundamental molecular mechanisms underlying human skin barrier and relevant diseases. � 2010 Kage-Nakadai et al.||Source Title:||PLoS ONE||URI:||https://scholarbank.nus.edu.sg/handle/10635/161821||ISSN:||19326203||DOI:||10.1371/journal.pone.0008857|
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