B6;129P2-Pemt^tm1J/J

Stock number: 003187
Product name: Pempt2-
Research areas: Cancer Research, Cardiovascular Research, Metabolism Research

Description

These Pemt knock-out mice exhibit a lack of phosphatidylethanolamine N-methyltransferase (PEMT) activity.

Detailed description

Mice homozygous for the Pemt^tm1J are viable and fertile. Pemt encodes an enzyme that converts phosphatidylethanolamine to phosphatidylcholine. Homozygotes completely lack PEMT activity and are no longer able to catalyze this reaction. Homozygotes are indistinguishable from controls in terms of development, behavior, and fecundity. Hepatocyte morphology, plasma lipid levels, and bile composition are normal. However, feeding homozygotes a choline deficient (CD) diet causes rapid onset of a severe liver pathology. Mice lose weight, develop grossly enlarged and pale colored livers, develop bright yellow plasma, and their gall bladders become engorged. In addition, a 50% decrease in liver phosphatidylcholine concentration and greater than 90% decrease in plasma triacylglyceride and cholesterol levels is observed in homozygotes on the CD-deficient diet.

Development

A sequence-replacement type gene targeting vector was constructed from a 6-kb BamHI subclone of gamma clone 3 containing exon 2 of the mouse Pemt2 gene. A cassette containing a neomycin-resistance gene (neo) driven by the Pgk promoter was inserted at unique XhoI and BclI sites in the subclone, replacing the majority of exon 2, including the translation start site, and the extreme 5' end of intron 1.

Allele

Symbol: Pemt^tm1J
Name: targeted mutation 1, Jackson
MGI accession ID: MGI:1857394
Generation method: Targeted
Attributes: Null/Knockout
Synonyms: Pempt2-; Pemt-
Marker symbol: Pemt
Marker name: phosphatidylethanolamine N-methyltransferase
Marker synonyms: PEAMT; Pempt; Pempt2; PEMT2; PHOMETH; PLMT; PNMT
Chromosome: 11
Strain of origin: 129P2/OlaHsd
Molecular note: A PGK neomycin cassette replaces the majority of exon 2, including the translation start site and the extreme 5' end of the intron. Lack of protein in homozygous mutant mice was demonstrated by immunoblot assays on liver homogenates, using a rat antibody from the C terminal end of the protein. Enzymatic activity was also abolished in homozygous mutant animals.