Demonstration of receptors for parathyroid hormone on cultured rabbit costal chondrocytes.
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.
Enomoto
M
M
Department of Biochemistry and Calcified-Tissue Metabolism, Faculty of Dentistry, Osaka University, Japan.
Kinoshita
A
A
Pan
H O
HO
Suzuki
F
F
Yamamoto
I
I
Takigawa
M
M
D000818:Animals; D001667:Binding, Competitive; D002356:Cartilage / Q000166:cytology / Q000378:metabolism*; D002455:Cell Division; D002478:Cells, Cultured; D007700:Kinetics; D008970:Molecular Weight; D010281:Parathyroid Hormone / Q000378:metabolism*; D011817:Rabbits; D011956:Receptors, Cell Surface / Q000378:metabolism*; D018016:Receptors, Parathyroid Hormone
D010281:Parathyroid Hormone; D011956:Receptors, Cell Surface; D018016:Receptors, Parathyroid Hormone