TY - JOUR
T1 - Biochemical roles of the oligosaccharide chains in thyrostimulin, a heterodimeric hormone of glycoprotein hormone subunits alpha2 (GPA2) and beta5 (GPB5)
AU - Okajima, Yoshiki
AU - Nagasaki, Hiroshi
AU - Suzuki, Chizuko
AU - Suga, Hidetaka
AU - Ozaki, Nobuaki
AU - Arima, Hiroshi
AU - Hamada, Yoji
AU - Civelli, Olivier
AU - Oiso, Yutaka
N1 - Funding Information:
We thank Ms. Michiko Yamada for her excellent technical assistance. This paper was supported in part by grants-in-aid from the Ministry of Education, Culture, Science, and Technology of Japan (#19590245-00).
PY - 2008/6/5
Y1 - 2008/6/5
N2 - 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.
AB - 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.
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U2 - 10.1016/j.regpep.2008.03.002
DO - 10.1016/j.regpep.2008.03.002
M3 - Article
C2 - 18433898
AN - SCOPUS:44349121122
SN - 0167-0115
VL - 148
SP - 62
EP - 67
JO - Regulatory Peptides
JF - Regulatory Peptides
IS - 1-3
ER -