Presence of high affinity receptor for interleukin-1 (IL-1) on cultured porcine thyroid cells.
Using 125I-interleukin-1 beta (125I-IL-1 beta) as a ligand, a specific receptor of high affinity dissociation constant (1.1 +/- 0.2 x 10(-10) M) with binding sites (350 +/- 40/cell) for interleukin-1 beta (IL-1 beta) has been demonstrated on cultured porcine thyroid cells. IL-1 alpha almost equally cross-reacted with the receptor (Kd = 1.2 +/- 0.3 x 10(-10) M and 350 +/- 50 binding sites/cell). TSH, IL-2 and other peptide hormones did not inhibit the binding of 125I-IL-1 beta to thyroid cells. Crosslinking study revealed a major band (approximately 95 kD) with a corrected molecular mass of approximately 78 kD. Moreover, both IL-1 beta and IL-1 alpha stimulated prostaglandin E2 production of cultured porcine thyroid cells, although the potency of IL-1 alpha was slightly greater than that of IL-1 beta. These results suggest that IL-1 may be involved in the regulation of thyroid cell function.
Kasai
K
K
Department of Endocrinology, Internal Medicine, Dokkyo University School of Medicine, Tochigi, Japan.
Hiraiwa
M
M
Emoto
T
T
Kuroda
H
H
Hattori
Y
Y
Mochizuki
Y
Y
Nakamura
T
T
Shimoda
S
S
D000818:Animals; D002478:Cells, Cultured; D007700:Kinetics; D008970:Molecular Weight; D011971:Receptors, Immunologic / Q000032:analysis / Q000378:metabolism*; D017472:Receptors, Interleukin-1; D013552:Swine; D013961:Thyroid Gland / Q000166:cytology / Q000378:metabolism*; D013997:Time Factors
D011971:Receptors, Immunologic; D017472:Receptors, Interleukin-1