Literature DB >> 181307

The different modes of action of thyrotropin and prostaglandin E1 on cyclic adenosine 3',5'-monophosphate synthesis in human thyroid, as studied by sequential stimulations.

N Takasu, S Sato, T Yamada, M Makiuchi, R Furihata.   

Abstract

PGE1 was equally effective in increasing 3H-cyclic AMP in normal and in toxic thyroids, whereas TSH was less effective but over a longer time in the toxic thyroids. Stimulation by a large second dose of TSH could not be elicited after prior stimulation by large doses of TSH. Similar results were obtained with regard to the effect of PGE1. However, stimulation by a large dose of PGE1 was still effective after the slices became refractory to TSH. Similarly, stimulation by a large dose of TSH was still effective after the slices became refractory to PGE1. It is suggested that the site and/or mode of action of TSH is quite different from that of PGE1.

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Year:  1976        PMID: 181307     DOI: 10.1055/s-0028-1093661

Source DB:  PubMed          Journal:  Horm Metab Res        ISSN: 0018-5043            Impact factor:   2.936


  4 in total

1.  The adenylate cyclase-cyclic AMP-phosphodiesterase system in pathological human thyroid.

Authors:  V Macchia; E Mandato; C Carella; G Pisano; G Biscaglia
Journal:  J Endocrinol Invest       Date:  1978-10       Impact factor: 4.256

2.  TSH-responsive adenylate cyclase activity in thyroid tissue from patients with Graves' disease.

Authors:  C M Rotella; P Fani; A L Tanini; P Cicchi; R S Toccafondi; P Arcangeli
Journal:  J Endocrinol Invest       Date:  1979 Jan-Mar       Impact factor: 4.256

3.  Cyclic AMP as the second hormonal messenger in the in vitro folliculogenesis of the foetal thyroid gland of the rat.

Authors:  P Pic; L Remy; E Mazzella; S Rua
Journal:  Cell Tissue Res       Date:  1983       Impact factor: 5.249

4.  Decrease of prostaglandin I2 binding sites in thyroid cancer.

Authors:  I Virgolini; M Hermann; H Sinzinger
Journal:  Br J Cancer       Date:  1988-11       Impact factor: 7.640

  4 in total

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