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Related Experiment Videos

Alternative splicing generates messages encoding rat c-erbA proteins that do not bind thyroid hormone.

T Mitsuhashi1, G E Tennyson, V M Nikodem

  • 1Clinical Endocrinology Branch, National Institute of Diabetes, Digestive and Kidney Diseases, Bethesda, MD 20892.

Proceedings of the National Academy of Sciences of the United States of America
|August 1, 1988
PubMed
Summary

Two novel rat brain thyroid hormone receptor (rTR alpha) variants, vI and vII, are abundantly expressed but do not bind thyroid hormones. Alternative splicing explains their prevalence and resolves discrepancies in receptor expression studies.

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Area of Science:

  • Molecular Biology
  • Endocrinology
  • Genetics

Background:

  • Thyroid hormone receptors (TRs) regulate gene expression.
  • Previous studies indicated high levels of rat brain thyroid hormone receptor alpha (rTR alpha) mRNA.
  • Discrepancies existed between reported mRNA abundance and measured receptor protein levels.

Purpose of the Study:

  • To investigate the molecular basis for discrepancies in rat brain thyroid hormone receptor expression.
  • To characterize novel variant cDNAs of rat brain thyroid hormone receptor alpha (rTR alpha).
  • To elucidate the functional implications of these variants.

Main Methods:

  • cDNA sequencing of rTR alpha variants vI and vII.
  • Gene sequencing of the 3' end of rTR alpha transcripts.

Related Experiment Videos

  • RNA transfer blot analysis.
  • In vitro translation and ligand binding assays.

    • Main Results:

    • Two variant rTR alpha cDNAs (vI and vII) were identified with sequence differences primarily at the 3' end.
    • Alternative splicing of primary transcripts from the same gene generates the 3' heterogeneity.
    • Variant mRNAs (rTR alpha vI and vII) are abundantly expressed in rat brain, while rTR alpha mRNA is less abundant.
    • In vitro translated rTR alpha vI and vII proteins did not bind thyroid hormones specifically.
    • Variant mRNAs are also found in kidney, heart, spleen, and liver at lower levels.

    Conclusions:

    • Alternative splicing generates distinct rTR alpha mRNA variants in rat brain.
    • The high abundance of non-ligand-binding rTR alpha variants explains previously observed discrepancies in receptor expression.
    • These variants possess intact DNA-binding domains, suggesting potential roles in modulating thyroid hormone action.