Jul 4, 2002

The half-life of the transcript encoding the folate receptor alpha in KB cells is reduced by cytosolic proteins expressed in folate-replete and not in folate-depleted cells

Gene
Easwara SadasivanSheldon P Rothenberg

Abstract

The KB cell, a transformed human cell line, constitutively expresses a high level of the glycosylphosphatidylinositol (GPI) anchored folate receptor protein alpha (FR alpha) and thereby can grow in medium containing <1 nM folate. When transferred from a folate-replete (FR) medium to one folate-deficient (FD), intracellular folate diminishes about 50-fold and expression of the FR alpha increases 6-fold. This up-regulation is mediated by a 4.5-fold increase in the initial transcription rate and a 2.4-fold prolongation of the mRNA half-life that together provide a higher level of the steady-state mRNA abundance. An RNA gel -shift assay of a 5' region of the mRNA that includes all of the non-coding and 24 nt of coding sequence, and a 3' region comprised only of coding sequence, identified unique complexes with cytosolic proteins from the FR-KB cells that were not observed with the cytosol from FD-KB cells. It appears, therefore, that expression of these folate-dependent cytosolic trans-active proteins function to maintain a shorter half-life of the mRNA in the FR-KB cells by binding to 5' and 3' cis elements, reducing the stability of this transcript.

Mentioned in this Paper

Hormone Receptors, Cell Surface
Complex (molecular entity)
Protoplasm
Transcription, Genetic
Folate Receptor 1
Human Cell Line
Folate
Folic Acid Measurement
Northern Blot
Metaplastic Cell Transformation

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