Abstract
The lipid-binding protein (LBP) family is conserved from Caenorhabditis elegans to mammals and essential for fatty acid homeostasis. RNAi-mediated knockdown of nine C. elegans lbp family members revealed that lbp-5 regulates fat accumulation. C. elegans LBP-5 bound directly to various fatty acids with varying affinities. lbp-5 expression in nhr-49(nr2041) worms was much lower than in N2 worms. Nhr-49 transcriptional activity also decreased with lbp-5 deletion, suggesting that they may work together as functional partners in fat metabolism. In support of this notion, LBP-5 translocated into nuclei, where it appeared to influence C. elegans NHR-49 target genes involved in energy metabolism. Interestingly, LBP-5 is required for stearic acid-induced transcription of NHR-49 target genes. Thus, this knowledge could help identify therapeutic targets to treat obesity and diseases associated with nematode-host interactions.
| Original language | English |
|---|---|
| Pages (from-to) | 28111-28118 |
| Number of pages | 8 |
| Journal | Journal of Biological Chemistry |
| Volume | 286 |
| Issue number | 32 |
| DOIs | |
| Publication status | Published - 2011 Aug 12 |
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All Science Journal Classification (ASJC) codes
- Biochemistry
- Molecular Biology
- Cell Biology
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Novel functions of lipid-binding protein 5 in Caenorhabditis elegans fat metabolism. / Xu, Mo; Joo, Hyoe Jin; Paik, Young-Ki.
In: Journal of Biological Chemistry, Vol. 286, No. 32, 12.08.2011, p. 28111-28118.Research output: Contribution to journal › Article
TY - JOUR
T1 - Novel functions of lipid-binding protein 5 in Caenorhabditis elegans fat metabolism
AU - Xu, Mo
AU - Joo, Hyoe Jin
AU - Paik, Young-Ki
PY - 2011/8/12
Y1 - 2011/8/12
N2 - The lipid-binding protein (LBP) family is conserved from Caenorhabditis elegans to mammals and essential for fatty acid homeostasis. RNAi-mediated knockdown of nine C. elegans lbp family members revealed that lbp-5 regulates fat accumulation. C. elegans LBP-5 bound directly to various fatty acids with varying affinities. lbp-5 expression in nhr-49(nr2041) worms was much lower than in N2 worms. Nhr-49 transcriptional activity also decreased with lbp-5 deletion, suggesting that they may work together as functional partners in fat metabolism. In support of this notion, LBP-5 translocated into nuclei, where it appeared to influence C. elegans NHR-49 target genes involved in energy metabolism. Interestingly, LBP-5 is required for stearic acid-induced transcription of NHR-49 target genes. Thus, this knowledge could help identify therapeutic targets to treat obesity and diseases associated with nematode-host interactions.
AB - The lipid-binding protein (LBP) family is conserved from Caenorhabditis elegans to mammals and essential for fatty acid homeostasis. RNAi-mediated knockdown of nine C. elegans lbp family members revealed that lbp-5 regulates fat accumulation. C. elegans LBP-5 bound directly to various fatty acids with varying affinities. lbp-5 expression in nhr-49(nr2041) worms was much lower than in N2 worms. Nhr-49 transcriptional activity also decreased with lbp-5 deletion, suggesting that they may work together as functional partners in fat metabolism. In support of this notion, LBP-5 translocated into nuclei, where it appeared to influence C. elegans NHR-49 target genes involved in energy metabolism. Interestingly, LBP-5 is required for stearic acid-induced transcription of NHR-49 target genes. Thus, this knowledge could help identify therapeutic targets to treat obesity and diseases associated with nematode-host interactions.
UR - http://www.scopus.com/inward/record.url?scp=80051516676&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=80051516676&partnerID=8YFLogxK
U2 - 10.1074/jbc.M111.227165
DO - 10.1074/jbc.M111.227165
M3 - Article
VL - 286
SP - 28111
EP - 28118
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
SN - 0021-9258
IS - 32
ER -