Horm Metab Res 1990; 22(2): 75-79
DOI: 10.1055/s-2007-1004855
Originals Basic

© Georg Thieme Verlag, Stuttgart · New York

Presence of High Affinity Receptor for Interleukin-1 (IL-1) on Cultured Porcine Thyroid Cells

K. Kasai, M. Hiraiwa, T. Emoto, H. Kuroda, Y. Hattori, Y. Mochizuki, T. Nakamura, S.-I. Shimoda
  • Department of Endocrinology, Internal Medicine, Dokkyo University School of Medicine, Mibu, Tochigi, Japan
Further Information

Publication History

1988

1989

Publication Date:
14 March 2008 (online)

Summary

Using 125I-interleukin-1β (125I-IL-1β) as a ligand, a specific receptor of high affinity dissociation constant (1.1 ± 0.2 × 10-10 M) with binding sites (350 ± 40/cell) for interleukin-1β (IL-1β) has been demonstrated on cultured porcine thyroid cells. IL-1α Almost equally cross-reacted with the receptor (Kd = 1.2 ± 0.3 × 10-10 M and 350 ± 50 binding sites/cell). TSH, IL-2 and other peptide hormones did not inhibit the binding of 125I-IL-1β to thyroid cells.

Crosslinking study revealed a major band (∼ 95 kD) with a corrected molecular mass of ∼ 78 kD. Moreover, both IL-1β and IL-1α stimulated prostaglandin E2 production of cultured porcine thyroid cells, although the potency of IL-1α was slightly greater than that of IL-1β. These results suggest that IL-1 may be involved in the regulation of thyroid cell function.