ACS-22, a protein homologous to mammalian fatty acid transport protein 4, is essential for the control of the toxicity and translocation of multi-walled carbon nanotubes in Caenorhabditis elegans. Issue 5 (8th January 2016)
- Record Type:
- Journal Article
- Title:
- ACS-22, a protein homologous to mammalian fatty acid transport protein 4, is essential for the control of the toxicity and translocation of multi-walled carbon nanotubes in Caenorhabditis elegans. Issue 5 (8th January 2016)
- Main Title:
- ACS-22, a protein homologous to mammalian fatty acid transport protein 4, is essential for the control of the toxicity and translocation of multi-walled carbon nanotubes in Caenorhabditis elegans
- Authors:
- Zhi, Lingtong
Fu, Wei
Wang, Xiong
Wang, Dayong - Abstract:
- Abstract : ACS-22 plays an essential role in regulating toxicity and translocation of MWCNTs. Abstract : Biodistribution and translocation are important for the generation of the toxicity of multi-walled carbon nanotubes (MWCNTs) in organisms. However, we know little about the molecular mechanisms of MWCNT translocation. In Caenorhabditis elegans, the acs-22 gene encodes a protein homologous to mammalian FATP4 (fatty acid transport protein 4). In this study, we employed a C. elegans in vivo assay system to investigate the possible function of ACS-22 in regulating the toxicity and translocation of MWCNTs. Prolonged exposure to MWCNTs significantly decreased transcriptional expression of the acs-22 gene. Loss-of-function mutation of the acs-22 gene strengthened MWCNT toxicity to the functions of both primary targeted organs such as intestine and secondary targeted organs such as neurons and reproductive organs; however, overexpression of the acs-22 gene reduced the toxicity of MWCNTs to the functions of both primary and secondary targeted organs. Loss-of-function mutation of the acs-22 gene enhanced the distribution and translocation of MWCNTs in both primary and secondary targeted organs, whereas overexpression of the acs-22 gene inhibited the distribution of MWCNTs in primary targeted organs and prevented translocation of MWCNTs into secondary targeted organs. Moreover, our results demonstrated the important function of ACS-22 in intestine to be in limiting the toxicity andAbstract : ACS-22 plays an essential role in regulating toxicity and translocation of MWCNTs. Abstract : Biodistribution and translocation are important for the generation of the toxicity of multi-walled carbon nanotubes (MWCNTs) in organisms. However, we know little about the molecular mechanisms of MWCNT translocation. In Caenorhabditis elegans, the acs-22 gene encodes a protein homologous to mammalian FATP4 (fatty acid transport protein 4). In this study, we employed a C. elegans in vivo assay system to investigate the possible function of ACS-22 in regulating the toxicity and translocation of MWCNTs. Prolonged exposure to MWCNTs significantly decreased transcriptional expression of the acs-22 gene. Loss-of-function mutation of the acs-22 gene strengthened MWCNT toxicity to the functions of both primary targeted organs such as intestine and secondary targeted organs such as neurons and reproductive organs; however, overexpression of the acs-22 gene reduced the toxicity of MWCNTs to the functions of both primary and secondary targeted organs. Loss-of-function mutation of the acs-22 gene enhanced the distribution and translocation of MWCNTs in both primary and secondary targeted organs, whereas overexpression of the acs-22 gene inhibited the distribution of MWCNTs in primary targeted organs and prevented translocation of MWCNTs into secondary targeted organs. Moreover, our results demonstrated the important function of ACS-22 in intestine to be in limiting the toxicity and translocation of MWCNTs. Therefore, our data suggest an essential role of ACS-22 in regulating the toxicity and translocation of MWCNTs in nematodes. Our results will provide important clues for further examination of the molecular mechanisms of translocation of MWCNTs in organisms. … (more)
- Is Part Of:
- RSC advances. Volume 6:Issue 5(2016)
- Journal:
- RSC advances
- Issue:
- Volume 6:Issue 5(2016)
- Issue Display:
- Volume 6, Issue 5 (2016)
- Year:
- 2016
- Volume:
- 6
- Issue:
- 5
- Issue Sort Value:
- 2016-0006-0005-0000
- Page Start:
- 4151
- Page End:
- 4159
- Publication Date:
- 2016-01-08
- Subjects:
- Chemistry -- Periodicals
540.5 - Journal URLs:
- http://pubs.rsc.org/en/Journals/JournalIssues/RA ↗
http://www.rsc.org/ ↗ - DOI:
- 10.1039/c5ra23543j ↗
- Languages:
- English
- ISSNs:
- 2046-2069
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 8036.750300
British Library DSC - BLDSS-3PM
British Library STI - ELD Digital store - Ingest File:
- 674.xml