Title : Introduction of human apolipoprotein E4 "domain interaction" into mouse apolipoprotein E.

Pub. Date : 2001 Sep 25

PMID : 11553788






4 Functional Relationships(s)
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1 Replacing Thr-61 in mouse apoE with arginine converted the binding preference from HDL to very low density lipoproteins in vitro, suggesting that apoE4 domain interaction could be introduced into mouse apoE in vivo. Arginine apolipoprotein E Homo sapiens
2 Heterozygous Arg-61/wild-type apoE mice displayed two phenotypes found in human apoE4/E3 heterozygotes: preferential binding to lower density lipoproteins and reduced abundance of Arg-61 apoE in the plasma, reflecting its more rapid catabolism. Arginine apolipoprotein E Homo sapiens
3 Heterozygous Arg-61/wild-type apoE mice displayed two phenotypes found in human apoE4/E3 heterozygotes: preferential binding to lower density lipoproteins and reduced abundance of Arg-61 apoE in the plasma, reflecting its more rapid catabolism. Arginine apolipoprotein E Homo sapiens
4 The Arg-61 apoE mouse model will allow the effects of apoE4 domain interaction in lipoprotein metabolism, atherosclerosis, and neurodegeneration to be determined. Arginine apolipoprotein E Homo sapiens