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Receptors for atrial natriuretic peptide (ANP) and regulation of thyroglobulin secretion by ANP in human thyroid cells

Journal Article · · Life Sciences; (USA)
; ;  [1]
  1. Uniformed Services Univ. of the Health Sciences, Bethesda, MD (USA) Walter Reed Army Medical Center, Washington, DC (USA)

Specific binding sites for atrial natriuretic peptide (ANP) were identified and characterized in primary cultures of human thyroid cells. Saturation analysis using ({sup 125}I) {alpha} rat (1-28) ANP as the ligand showed a single class of high affinity binding which was inhibited by atriopeptin I and the {alpha} -human form of ANP, but not by a C-terminal fragment (13-28) of the peptide. The number of ANP binding sites in these cultures was not altered by the thyroid hormone concentration of the medium. In a dose-response experiment, thyroglobulin secretion was significantly reduced in the presence of 0.01 nM ANP and was maximally reduced with 10 nM ANP. Cyclic GMP production was increased threefold in the presence of 100 nM ANP, but was unchanged with lower doses of the peptides. The finding of receptors in thyroid follicular cells suggests a hitherto unrecognized role of ANP in the thyroid gland.

OSTI ID:
7067244
Journal Information:
Life Sciences; (USA), Journal Name: Life Sciences; (USA) Vol. 45:9; ISSN 0024-3205; ISSN LIFSA
Country of Publication:
United States
Language:
English