TY - JOUR
T1 - Demonstration of receptors for parathyroid hormone on cultured rabbit costal chondrocytes
AU - Enomoto, Motomi
AU - Kinoshita, Akihiro
AU - Pan, Hai Ou
AU - Suzuki, Fujio
AU - Yamamoto, Itsuo
AU - Takigawa, Masaharu
N1 - Funding Information:
Acknowledgments: We thank Mrs. Elizabeth Ichihara for assistance in the preparation of this manuscript and Miss Noriko Yoneda for secretarial assistance. This work was supported in part by Grants-in-Aid for Scientific Research and Developmental Scientific Research from the Ministry of Education, Science and Culture of Japan, and grants from the Kowa Life Science Foundation and the Osaka Anti-Cancer Society.
PY - 1989/8/15
Y1 - 1989/8/15
N2 - Parathyroid hormone (PTH) receptors on cultured rabbit costal chondrocytes were demonstrated using HPLC-purified, radioiodinated [Nle8,-Nle18,Tyr34]bovine PTH-(1-34)amide. PTH binding was found to be specific for PTH agonists and antagonists and dependent on the time and temperature of incubation. Both growth cartilage (GC) cells and resting cartilage (RC) cells were shown to have a single class of saturable, high affinity PTH binding sites with a dissociation constant of 0.6-0.7 nM. However, the numbers of receptors per cell were approximately 49,000 on GC cells and 19,000 on RC cells. After crosslinking the receptors on these cells with the radioligand, one, major 125I-labeled band of 76 kDa was separated by SDS-PAGE.
AB - Parathyroid hormone (PTH) receptors on cultured rabbit costal chondrocytes were demonstrated using HPLC-purified, radioiodinated [Nle8,-Nle18,Tyr34]bovine PTH-(1-34)amide. PTH binding was found to be specific for PTH agonists and antagonists and dependent on the time and temperature of incubation. Both growth cartilage (GC) cells and resting cartilage (RC) cells were shown to have a single class of saturable, high affinity PTH binding sites with a dissociation constant of 0.6-0.7 nM. However, the numbers of receptors per cell were approximately 49,000 on GC cells and 19,000 on RC cells. After crosslinking the receptors on these cells with the radioligand, one, major 125I-labeled band of 76 kDa was separated by SDS-PAGE.
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U2 - 10.1016/0006-291X(89)90804-8
DO - 10.1016/0006-291X(89)90804-8
M3 - Article
C2 - 2548491
AN - SCOPUS:0024414238
SN - 0006-291X
VL - 162
SP - 1222
EP - 1229
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
IS - 3
ER -