Abstract：
:Specific binding sites for atrial natriuretic peptide (ANP) were identified and characterized in primary cultures of human thyroid cells. Saturation analysis using [125I] alpha rat ANP as the ligand showed a single class of high affinity binding (Kd = 0.2 nM) which was inhibited by atriopeptin I and the alpha -human form of ANP, but not by a C-terminal fragment 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, thyro-globulin secretion was significantly reduced in the presence of 0.01 nM ANP and was maximally reduced (to 25% of control value) with 10 nM ANP. Cyclic GMP production was increased threefold in the presence of 100 nM ANP, but was unchanged with lower doses (0.01 and 0.1 nM) of the peptide. The finding of receptors in thyroid follicular cells suggests a hitherto unrecognized role of ANP in the thyroid gland.
journal_name
Life Scijournal_title
Life sciencesauthors
Sellitti DF,Tseng YC,Wartofsky Ldoi
10.1016/0024-3205(89)90172-0subject
Has Abstractpub_date
1989-01-01 00:00:00pages
793-801issue
9eissn
0024-3205issn
1879-0631pii
0024-3205(89)90172-0journal_volume
45pub_type
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