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Thyrotropin-releasing hormone (TRH) and phorbol myristate acetate decrease TRH receptor messenger RNA in rat

J Fujimoto1, R E Straub, M C Gershengorn

  • 1Department of Medicine, New York Hospital, Cornell University Medical College, New York 10021.

Insights

Thyrotropin-releasing hormone (TRH) transiently decreases thyrotropin-releasing hormone receptor (TRH-R) mRNA levels in GH3 cells. Protein kinase C activation by phorbol myristate acetate (PMA) mimics this effect, which is blocked by H-7.

Area of Science:

  • Endocrinology
  • Molecular Biology
  • Cell Signaling

Background:

  • Thyrotropin-releasing hormone (TRH) down-regulates its own receptors (TRH-Rs) on pituitary tumor cells.
  • TRH-R mRNA levels decrease before TRH-R density reduction.
  • TRH signaling involves calcium and diacylglycerol pathways, activating protein kinases.

Purpose of the Study:

  • Investigate the mechanism of TRH-induced TRH-R downregulation.
  • Determine the role of protein kinase C (PKC) in TRH-R mRNA regulation.
  • Examine the effects of TRH, calcium, PMA, and H-7 on TRH-R mRNA levels.

Main Methods:

  • GH3 cells were treated with TRH, elevated cytoplasmic Ca2+, PMA, or H-7.
  • TRH-R mRNA levels were quantified using Northern analysis and nuclease protection assays.
  • Probes were generated from mouse pituitary TRH-R cDNA.

Main Results:

  • TRH (1 μM) caused a transient decrease in TRH-R mRNA (20-45% of control by 3-6 h).
  • Elevated cytoplasmic Ca2+ had no effect on TRH-R mRNA levels.
  • PMA (1 μM) mimicked TRH's effect on TRH-R mRNA, while H-7 blocked both TRH and PMA effects.

Conclusions:

  • TRH-induced TRH-R downregulation involves a decrease in TRH-R mRNA.
  • Protein kinase C activation, not calcium elevation, mediates TRH's effect on TRH-R mRNA.
  • PKC plays a crucial role in regulating TRH-R mRNA levels in GH3 cells.

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