PubMed Health⌕ Search

PubMed · 15063092

Deletion of the Pemt gene increases progenitor cell mitosis, DNA and protein methylation and decreases calretinin expression in embryonic day 17 mouse hippocampus.

Abstract

Choline is a required nutrient and is derived from the diet as well as from de novo synthesis catalyzed by phosphatidylethanolamine N-methyltransferase (PEMT). We previously reported that choline availability during pregnancy alters mitosis and neuronal protein expression during fetal brain development in wild-type mice and rats, and that Pemt-/- mice become choline deficient. In this study, we examined brain development in these knockout mice. Pregnant Pemt-/- and wild-type mice were fed AIN-76A diet until gestation day 17 (E17) when the fetal brains were harvested. Phosphorylation of histone H3 (a measure of mitosis) and calretinin (a GABAergic neuronal marker) were assessed in hippocampal regions. We observed increased numbers of phosphorylated histone H3 positive cells in the Pemt-/- mice (up 54% compared to wild-type mice; p<0.01). We also found decreased calretinin labeling in Pemt-/- (down to 43% compared to wild-type mice; p<0.01). Thus, there was increased stem cell proliferation in the neuroepithelium and decreased GABAergic neuronal differentiation of these animals on E17. These results are opposite to what would have been expected in choline-deficient mice. The concentrations of S-adenosylmethionine (up 21%; p<0.05) and methylation of DNA (up 46%) and proteins (up 12%; p<0.01) in hippocampus were significantly increased in Pemt-/- mice, suggesting that increased S-adenosylmethionine availability may mediate the observed developmental changes. This is the first report of altered brain development in Pemt-/- mice.

Explore related subjects

Keep this discovery

Explore connections, maps & timelines

BibTeXRIS

Xiaonan Zhu, Mei-Heng Mar, Jiannan Song, Steven H Zeisel. 2004-04-19. Deletion of the Pemt gene increases progenitor cell mitosis, DNA and protein methylation and decreases calretinin expression in embryonic day 17 mouse hippocampus.. https://doi.org/10.1016/j.devbrainres.2004.01.004

Cite the original work for its findings. Save a collection to share your selection of sources.

KEEP EXPLORING

Related citations

Pangenome-wide identification and expression analysis of the chalcone synthase (CHS) gene family in five yellowhorn spp.

Chalcone synthase (CHS) is a pivotal enzyme in flavonoid biosynthesis involved in plant development, defense, and secondary metabolism. Xanthoceras sorbifolium (yellowhorn) is a medicinal and ornamental species with high resistance to environmental stresses, but its CHS gene family remains uncharacterized. We performed a pangenome-wide identification of CHS genes across five yellowhorn genomes (Xzs4, Xwf8, Xjg, Xg11, and Xzg2). Across the five yellowhorn genomes, 27 CHS genes were identified and classified into four core pangenes, present in all five genomes, and two dispensable genes, present only in a subset of genomes. Phylogenetic analysis grouped these genes into three major clades, and chromosomal mapping and duplication analyses identified four tandemly duplicated gene pairs under purifying selection. The analyses of conserved structural features, including protein motifs and exon-intron organization, together with promoter cis-regulatory elements and gene ontology annotation, further indicated the potential involvement of CHS genes in flavonoid biosynthesis and stress-responsive mechanisms. Gene expression profiling identified significant upregulation of Xg11_CHS1 and Xg11_CHS3 under cold and drought stress, with tissue-specific expression patterns. These findings provide valuable insights into the evolution, functional diversification, and stress-responsive roles of the CHS gene family, identifying candidate genes for future studies targeting stress tolerance and flavonoid biosynthesis in yellowhorn.

Acyltransferases↗

Poly(3-hydroxyalkanoate) polymerase synthesis and in vitro activity in recombinant Escherichia coli and Pseudomonas putida.

We tested the synthesis and in vitro activity of the poly(3-hydroxyalkanoate) (PHA) polymerase 1 from Pseudomonas putida GPo1 in both P. putida GPp104 and Escherichia coli JMU193. The polymerase encoding gene phaC1 was expressed using the inducible PalkB promoter. It was found that the production of polymerase could be modulated over a wide range of protein levels by varying inducer concentrations. The optimal inducer dicyclopropylketone concentrations for PHA production were at 0.03% (v/v) for P. putida and 0.005% (v/v) for E. coli. Under these concentrations the maximal polymerase level synthesized in the E. coli host (6% of total protein) was about three- to fourfold less than that in P. putida (20%), whereas the maximal level of PHA synthesized in the E. coli host (8% of total cell dry weight) was about fourfold less than that in P. putida (30%). In P. putida, the highest specific activity of polymerase was found in the mid-exponential growth phase with a maximum of 40 U/g polymerase, whereas in E. coli, the maximal specific polymerase activity was found in the early stationary growth phase (2 U/g polymerase). Our results suggest that optimal functioning of the PHA polymerase requires factors or a molecular environment that is available in P. putida but not in E. coli.

Acyltransferases↗

Resveratrol glucoside (Piceid) synthesis in seeds of transgenic oilseed rape (Brassica napus L.).

Resveratrol is a phytoalexin produced in various plants like wine, peanut or pine in response to fungal infection or UV irradiation, but it is absent in members of the Brassicaceae. Moreover, resveratrol and its glucoside (piceid) are considered to have beneficial effects on human health, known to reduce heart disease, arteriosclerosis and cancer mortality. Therefore, the introduction of the gene encoding stilbene synthase for resveratrol production in rapeseed is a tempting approach to improve the quality of rapeseed products. The stilbene synthase gene isolated from grapevine (Vitis vinifera L.) was cloned under control of the seed-specific napin promotor and introduced into rapeseed (Brassica napus L.) by Agrobacterium-mediated co-transformation together with a ds-RNA-interference construct deduced from the sequence of the key enzyme for sinapate ester biosynthesis, UDP-glucose:sinapate glucosyltransferase (BnSGT1), assuming that the suppression of the sinapate ester biosynthesis may increase the resveratrol production in seeds through the increased availability of the precursor 4-coumarate. Resveratrol glucoside (piceid) was produced at levels up to 361 microg/g in the seeds of the primary transformants. This value exceeded by far piceid amounts reported from B. napus expressing VST1 in the wild type sinapine background. There was no significant difference in other important agronomic traits, like oil, protein, fatty acid and glucosinolate content in comparison to the control plants. In the third seed generation, up to 616 microg/g piceid was found in the seeds of a homozygous T3-plant with a single transgene copy integrated. The sinapate ester content in this homozygous T3-plant was reduced from 7.43 to 2.40 mg/g. These results demonstrate how the creation of a novel metabolic sink could divert the synthesis towards the production of piceid rather than sinapate ester, thereby increasing the value of oilseed products.

Acyltransferases↗