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Point mutations alter regulation of folate receptor expression

, : Point mutations alter regulation of folate receptor expression. FASEB Journal 17(4-5): Abstract No 191 17, March

The folate receptor (FR) is a high affinity receptor that transports folates into cells expressing this protein. In a previous study of FR regulation, endogenous levels of this receptor significantly increased as growth decreased. Conversely, FR introduced by stable transfection, decreased as growth slowed. Sequence analysis of the FR cDNA has since revealed two point mutations which altered amino acids 144 and 201. Of specific interest was the 201 mutation, which deleted one of the three known glycosylation sites. To test the possibility that these mutations altered the regulation of the transfected FR, the response of the wild-type FR (FRwt) and the FR with only the 201 mutation (FR201), to changing growth rates were examined. In addition, the effect of a mutation at position 67 (FR67), which previously had been reported to create a dominant-negative FR on receptor levels, was also analyzed. The transfected FRwt behaved in a similar fashion as the endogenous receptor, while FR201 mimicked the results found previously for FR144/201. The combination of mutations 67 and 201 (FR67/201) resulted in no detectable binding, although protein was expressed as detected by Western blotting. These results suggest that core glycosylation at amino acid 201 significantly alters regulation of protein levels. Furthermore, a change at position 67 in combination with 201 severely comprises the ability of the receptor to bind folate.


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