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Thyrotropin receptor processing and interaction with thyrotropin.

T Akamizu1, S Kosugi, L D Kohn

  • 1Laboratory of Biochemistry and Metabolism, National Institute of Diabetes and Digestive and Kidney Diseases National Institutes of Health, Bethesda, MD 20892.

Biochemical and Biophysical Research Communications
|June 29, 1990
PubMed
Summary
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Researchers created nonglycosylated thyrotropin receptors in vitro that bind thyrotropin. A signal peptide was found to be critical for post-translational processing by specific membranes, but not for thyrotropin binding.

Area of Science:

  • Molecular biology
  • Biochemistry
  • Endocrinology

Background:

  • The thyrotropin receptor (TSHR) plays a crucial role in thyroid hormone regulation.
  • Understanding TSHR's post-translational modifications is essential for comprehending its function.

Purpose of the Study:

  • To investigate the in vitro synthesis and characteristics of the rat thyrotropin receptor.
  • To identify the role of a signal peptide in TSHR processing and thyrotropin binding.

Main Methods:

  • In vitro transcription/translation of rat TSHR cDNA.
  • Binding assays with thyrotropin.
  • Incubation with canine pancreatic microsomal membranes.
  • Endoglycosidase H digestion.
  • Analysis of deletion mutants.

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Main Results:

  • Nonglycosylated TSHR proteins were synthesized in vitro, with one approximating the predicted 87 kDa size.
  • These proteins demonstrated the ability to bind thyrotropin.
  • Canine pancreatic microsomal membranes facilitated modification of putative glycosylation sites, confirmed by endoglycosidase H digestion.
  • A hydrophobic signal peptide was identified as critical for post-translational processing by these membranes, but not for thyrotropin binding.

Conclusions:

  • The study successfully synthesized functional, albeit nonglycosylated, thyrotropin receptors in vitro.
  • A specific signal peptide is essential for proper post-translational modification of TSHR by microsomal membranes.
  • This signal peptide's role is distinct from the direct binding of thyrotropin to the receptor.