Biochemical roles of the oligosaccharide chains in thyrostimulin, a heterodimeric hormone of glycoprotein hormone subunits alpha2 (GPA2) and beta5 (GPB5)

Yoshiki Okajima, Hiroshi Nagasaki, Chizuko Suzuki, Hidetaka Suga, Nobuaki Ozaki, Hiroshi Arima, Yoji Hamada, Olivier Civelli, Yutaka Oiso

Research output: Contribution to journalArticlepeer-review

21 Citations (Scopus)

Abstract

Thyrostimulin is a heterodimeric hormone composed of GPA2 and GPB5, and shares the thyroid-stimulating hormone receptor (TSHR). Thyrostimulin has three N-linked oligosaccharide chains, two in GPA2 and one in GPB5. The roles of these N-linked oligosaccharides in secretion, heterodimer formation and signal transduction were analyzed. Recombinant GPA2s lacking either of the two oligosaccharides were obtained from conditioned medium, whereas dual site-disrupted GPA2 and the GPB5 mutant were not expressed in either the conditioned medium or cell lysate. The binding between GPA2 and GPB5 was weaker than that between TSH subunits GPA1 and TSHβ. Neither of the oligosaccharides in GPA2 had significant effects on heterodimerization. Disruption of either of the oligosaccharides in GPA2 significantly decreased receptor activation, suggesting their critical role in receptor activation.

Original languageEnglish
Pages (from-to)62-67
Number of pages6
JournalRegulatory Peptides
Volume148
Issue number1-3
DOIs
Publication statusPublished - 05-06-2008
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Physiology
  • Endocrinology
  • Clinical Biochemistry
  • Cellular and Molecular Neuroscience

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