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J. Biol. Chem., Vol. 269, Issue 39, 24459-24465, Sep, 1994
BP Eliceiri and DD Brown
Greater than 90% of the endogenous thyroid hormone receptor proteins TR
alpha and TR beta in tissues of Xenopus laevis comigrate with their
respective in vitro synthesized counterparts, and these major components
are not phosphorylated detectably. Maternally inherited TR alpha protein is
stable through early embryogenesis during a time in which there is no
detectable TR alpha mRNA synthesis. At stage 35 when TR alpha mRNA is first
detectable, the inherited TR alpha protein is present at about 100
molecules/cell. TR alpha protein subsequently increases to levels of about
1500 and 6000 molecules/cell in tail and head regions, respectively, in
stage 52 tadpoles. Even though TR alpha mRNA gradually increases during
metamorphosis (from stage 52 to 62), TR alpha protein remains constant,
suggesting strongly that post- transcriptional events control the ultimate
levels of TR alpha protein. In contrast, there is no detectable TR beta
protein (less than 100 molecules/cell) throughout embryogenesis until stage
52. Both TR beta mRNA and protein rise along with the increase in
endogenous thyroid hormone, reaching a maximum at the climax of
metamorphosis, when TR beta protein exceeds TR alpha protein in
concentration. As with TR alpha protein, TR beta protein in tail is
consistently about one-fourth that of TR beta protein in the head region.
The number of TR alpha protein molecules in extracts of premetamorphic
tadpoles and cultured cells grown in the absence of thyroid hormone fully
accounts for all of the sites to which 125I-T3 bind. We interpret this to
mean that TR alpha protein must be a necessary, if not sufficient,
component in the pathway toward metamorphosis triggered by thyroid hormone
and required for the phenomenon of competence in tissues and cells.
Quantitation of endogenous thyroid hormone receptors alpha and beta during embryogenesis and metamorphosis in Xenopus laevis
Carnegie Institution of Washington, Baltimore, Maryland 21210.
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