Please use this identifier to cite or link to this item: https://doi.org/10.1371/journal.pone.0004104
Title: Nematode homologue of PQBP1, a mental retardation causative gene, is involved in lipid metabolism
Authors: Takahashi K.
Yoshina S.
Masashi M.
Ito W.
Inoue T. 
Shiwaku H.
Arai H.
Mitani S.
Okazawa H.
Keywords: binding protein
fatty acid
polyglutamate binding protein
protein PQBP1
short hairpin RNA
triacylglycerol
unclassified drug
Caenorhabditis elegans protein
carrier protein
hybrid protein
nuclear protein
PQBP1 protein, human
adipocyte
article
Caenorhabditis elegans
cell proliferation
controlled study
evolutionary homology
gene expression
gene function
gene repression
in vivo study
intestine cell
larval stage
lipid analysis
lipid metabolism
mutant
nonhuman
protein defect
protein function
transgenics
animal
Caenorhabditis elegans
cell culture
cytology
genetics
histology
human
intestine
metabolism
physiology
syndrome
transgenic animal
white adipose tissue
X linked mental retardation
Caenorhabditis elegans
Mammalia
Nematoda
Adipocytes
Adipose Tissue, White
Animals
Animals, Genetically Modified
Caenorhabditis elegans
Caenorhabditis elegans Proteins
Carrier Proteins
Cells, Cultured
Humans
Intestines
Lipid Metabolism
Mental Retardation, X-Linked
Nuclear Proteins
Recombinant Fusion Proteins
Syndrome
Issue Date: 2009
Citation: Takahashi K., Yoshina S., Masashi M., Ito W., Inoue T., Shiwaku H., Arai H., Mitani S., Okazawa H. (2009). Nematode homologue of PQBP1, a mental retardation causative gene, is involved in lipid metabolism. PLoS ONE 4 (1) : e4104. ScholarBank@NUS Repository. https://doi.org/10.1371/journal.pone.0004104
Abstract: Background: PQBP1 is a causative gene for X-linked mental retardation (MR) whose patients frequently show lean body. C. elegans has a strictly conserved homologue gene of PQBP1, T21D12.3. Methodology and Principal Findings: We generated Venus-transgenic and T21D12.3-mutant nematodes to analyze developmental expression patterns and in vivo functions of the nematode PQBP1 homologue protein (pqbp-1.1). During development, pqbp-1.1 is expressed from cell proliferation stage to larva stage. In larva, intestinal cells show the highest expression of pqbp-1.1, while it decreases in adult worms. The mutants of pqbp-1.1 show a decrease of the lipid content in intestinal cells. Especially, incorporation of fatty acid into triglyceride is impaired. ShRNA-mediated repression of PQBP1 also leads to reduction of lipid content in mammalian primary white adipocytes. Conclusion/Significance: These results suggest that pqbp-1.1 is involved in lipid metabolism of intestinal cells. Dysfunction of lipid metabolism might underlie lean body, one of the most frequent symptoms associating with PQBP1-linked MR patients. � 2009 Takahashi et al.
Source Title: PLoS ONE
URI: https://scholarbank.nus.edu.sg/handle/10635/161845
ISSN: 19326203
DOI: 10.1371/journal.pone.0004104
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