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Tissue-specific posttranslational modification allows functional targeting of thyrotropin.

Keisuke Ikegami1, Xiao-Hui Liao2, Yuta Hoshino1

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Summary

Tissue-specific glycosylation prevents functional crosstalk between pituitary TSH variants. Differently glycosylated thyroid-stimulating hormone (TSH) forms distinct circulating complexes, ensuring targeted physiological regulation.

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Area of Science:

  • Endocrinology
  • Glycobiology
  • Molecular Biology

Background:

  • Thyroid-stimulating hormone (TSH), also known as thyrotropin, is a pituitary glycoprotein crucial for thyroid hormone production.
  • Distinct TSH populations, pars distalis-TSH (PD-TSH) and pars tuberalis-TSH (PT-TSH), exert differential functions on the thyroid and hypothalamus, respectively.
  • The mechanism preventing functional crosstalk between these TSH variants remained unclear.

Purpose of the Study:

  • To elucidate how tissue-specific TSH variants avoid functional crosstalk.
  • To investigate the role of glycosylation in regulating TSH bioactivity and targeting.

Main Methods:

  • Analysis of N-glycan structures of PD-TSH and PT-TSH.
  • Investigation of circulating TSH complex formation (macro-TSH).
  • Assessment of TSH bioactivity and metabolic fate based on glycosylation patterns.

Main Results:

  • PD-TSH exhibits sulfated biantennary N-glycans, leading to rapid hepatic metabolism.
  • PT-TSH possesses sialylated multibranched N-glycans, forming inactive macro-TSH complexes with immunoglobulin or albumin in circulation.
  • Tissue-specific glycosylation dictates TSH bioactivity and prevents unintended thyroid stimulation by PT-TSH.

Conclusions:

  • Glycosylation is a key mechanism for preventing functional crosstalk between TSH variants.
  • Differential glycosylation ensures that PD-TSH regulates thyroid function while PT-TSH modulates hypothalamic pathways.
  • This study highlights the critical role of glycosylation in maintaining the specificity of signaling molecules within the body.