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

研究成果: Article査読

24 被引用数 (Scopus)

抄録

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.

本文言語English
ページ(範囲)62-67
ページ数6
ジャーナルRegulatory Peptides
148
1-3
DOI
出版ステータスPublished - 05-06-2008
外部発表はい

All Science Journal Classification (ASJC) codes

  • 生化学
  • 生理学
  • 内分泌学
  • 臨床生化学
  • 細胞および分子神経科学

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