Endocrinol Japon

1977

DOI: 10.1507/endocrj1954.24.277

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Effect of LATS, TSH and cholera toxin on the thyroid gland in nude mice.

¹

,

Takashi Hachiya

²

,

Tadayoshi Miyazaki

³

et al.

Abstract: SynopsisThree thyroid stimulators; LATS, TSH, and cholera toxin, have been tested by bioassay using congenitally athymic homozygous mice (nu/nu), nude mice and control littermates (nu/+) possessing normal thymic function. nu/+ Animals showed a response to LATS similarly to normal white mice of the ddN strain. The assay response to LATS in nu/nu animals was about half that in normal mice. TSH also showed a less stimulating action in nude mice.Cholera toxin made a long acting response similarly to LATS. The resp… Show more

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Radioreceptor Assay1

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Cited by 11 publications

(3 citation statements)

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“…Mullin et al (1976) reported that cholera toxin stimulated adenyl cyclase and also bound with the same receptor of TSH in the thyroid. In the previous paper we demonstrated the thyroid stimulating action of cholera toxin (Ochi et al, 1977) and in the present experiment we confirmed an evidence for the binding of both cholera toxin and TSH to the same receptor.…”

Section: Discussionsupporting

confidence: 89%

An attempt to analyze various thyroid stimulators by the receptor assay using hTSH radioimmunoassay.

¹

,

²

,

³

et al. 1979

Endocrinol Japon

Self Cite

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No abstract

“…Mullin et al (1976) reported that cholera toxin stimulated adenyl cyclase and also bound with the same receptor of TSH in the thyroid. In the previous paper we demonstrated the thyroid stimulating action of cholera toxin (Ochi et al, 1977) and in the present experiment we confirmed an evidence for the binding of both cholera toxin and TSH to the same receptor.…”

Section: Discussionsupporting

confidence: 89%

An attempt to analyze various thyroid stimulators by the receptor assay using hTSH radioimmunoassay.

¹

,

²

,

³

et al. 1979

Endocrinol Japon

Self Cite

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No abstract

“…TSAb assay and TSBAb assay using porcine thyroid cells were performed as previously described (11). T4 production activity using mouse bioassay was measured according to the method of McKenzie as previously described (12). Test sera Sera from Graves' disease with abnormally negative TRAb activity (untreated and during treatment) were used.…”

mentioning

confidence: 99%

Precise Determination of TSH Receptor Antibody Activity in Serum Containing Bovine TSH (bTSH) Binding Antibody by Absorption Using Denatured bTSH or Sheep FSH

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,

et al. 1996

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A previous report demonstrated that sera with bovine TSH (bTSH) binding antibody showed abnormally negative TSH receptor antibody (TRAb) activity in the standard TRAb assay method. The corrected TRAb activity calculated by the determination of the nonspecific binding of the labeled bTSH for each test serum [NSB(T)] resulted in positive TRAb activity. However, the precise calculation was difficult because NSB(T) level was significantly higher than the nonspecific binding in normal pool serum [NSB(N)] level. In the present experiment the determination of the TRAb activity was performed after absorption of bTSH binding antibodies by the heat-denatured bTSH to obtain more precise TRAb activity. In addition, absorption by sheep FSH (sFSH) was performed because almost all bTSH binding antibodies showed specific binding to the alpha-subunit of mammalian pituitary glycoprotein hormones in our previous study. Three days absorption of test serum using 1 mU of the heat-denatured bTSH (100 degrees C for 1 h) or 5 mU of sFSH was chosen as optimal because NSB(T) decreased remarkably to NSB(N) levels. The corrected TRAb determined after these absorptions decreased significantly compared to the corrected TRAb activity without the absorption. When the complete absorption of bTSH binding antibody was performed by the decrease of the NSB(T) level to the NSB(N) level, the TRAb activity determined by these two different absorptions was almost similar (difference was less than 10%). However, it was difficult to obtain the precise TRAb activity in the cases with extremely high bTSH binding antibody, because the NSB(T) level was higher than the NSB(N) level by the incomplete absorption of bTSH binding antibody.

“…TR-ab activity was expressed as bTSH amounts diluted with pooled normal human serum (bTSH equiv¬ alents in 0.05 ml of test serum). LATS activity was mea¬ sured as previously described (25). Thyroid-stimulating activity of TS-ab and TSH-blocking activity of TSB-ab were assayed by cAMP production using cultured porcine thyroid cells (26).…”

Section: Radioreceptor Assaymentioning

confidence: 99%

Different binding of stimulatory-type and blocking-type TSH receptor antibody with guinea-pig testis membrane

¹

,

Ochi²,

et al. 1991

Acta Endocrinologica

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A receptor assay using [125I]bTSH-binding to guinea-pig testis membrane was developed. Unlabelled hCG and FSH inhibited [125I]bTSH binding. In patients with Graves' disease and in untreated hyperthyroid patients, almost all long-acting thyroid stimulators and thyroid-stimulating antibodies, respectively did not inhibit [125I]bTSH binding, which on the other hand was inhibited by thyroid stimulation blocking antibodies in patients with primary hypothyroidism. When the inhibitory effect on the binding of [125I]hCG and 125I-synthetic \g=a\-subunit peptide (\g=a\26-46) of hCG to testis membrane was examined, bTSH resulted in a significant inhibition. However, all three kinds of TSH receptor antibodies had no inhibitory effect. This study demonstrated 1. interaction of \g=a\-subunitof TSH and hCG with the testicular receptor; 2. binding of thyroid stimulation-blocking antibody and lack of binding of thyroid-stimulating antibody to the testicular TSH receptor in spite of binding of these TSH receptor antibodies to the thyroidal TSH receptor, and 3. lack of binding of thyroid-stimulating antibody and thyroid stimulation-blocking antibody to the testicular gonadotropin receptor.TSH receptors have been demonstrated in mem¬ branes from extrathyroid tissues (1-4). TSH, LH, FSH and hCG consist of a common ct-subunit and a hormone specific ß-subunit. Available data sug¬ gest that the ci-subunit part of pituitary glycoprotein hormones such as FSH, LH, TSH and hCG may play an important role in recognition and binding to receptor. The binding of [12oI]bovine TSH (bTSH) to its receptor was attributed to the ct-subunit (1,4-10). On the other hand, an inhibi¬ tory effect of bTSH on [125I]hCG binding to its receptor (testis or ovary) has been demonstrated (6,11,12).Long-acting thyroid stimulator (LATS) and thy¬ roid-stimulating antibody (TS-ab) have been shown to compete with TSH for binding to TSH receptor (13-16). Thyroid stimulation-blocking antibody (TSB-ab) have also a blocking action on TSH by its direct binding to the TSH receptor (17)(18)(19). How¬ ever, it has never been clear how these thyroid stimu¬ lators (TSH, LATS, TS-ab) and TSB-ab can bind to the same binding site in the receptor.In the present study binding characteristics of TSH receptor antibody (TR-ab) such as LATS, TSab, TSB-ab to the testicular TSH receptor were examined. Materials and Methods Materials and MethodsCrude bTSH (1 IU/mg protein) was obtained from Sigma Chemical Co (St. Louis, MO). Crude FSH (HMG, 75 IU/mg protein) was obtained from Nikken Co (Tokyo, Japan). The purified hCG (9000 IU/mg protein) and crude hCG preparation (1000 IU/mg protein) were ob¬ tained from UCB-Bioproducts (Brüssel, Belgium) and Mochida Co (Tokyo), respectively. Synthetic a-subunk peptide (a 26-46, Leu-Gln-CysMet-Gly-Cys-Cys-Phe-Ser-Arg-Ala-Tyr-Pro-Thr-Pro-LeuArg-Ser-Lys-Lys-Thr (NH2)) of hCG was synthesized by Curare Co Ltd (Osaka, Japan) (20,21).

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