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JILL BROWN
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D. S. MUNRO
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SUMMARY

A new in vitro assay for thyroid-stimulating hormone (TSH) is described. The parameter of TSH action is the discharge of radioactive iodine from mouse thyroid glands labelled with 131I in vivo. The assay is sensitive to human TSH and gave consistent results during 1 yr. without seasonal variation. A potent preparation of long-acting thyroid stimulator gave a dose-response line parallel with human TSH. Fresh human serum was toxic to the assay preparation so that circulating TSH levels cannot be measured.

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P. S. HOPKINS
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A. L. C. WALLACE
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G. D. THORBURN
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SUMMARY

A radioimmunoassay technique for measuring the thyrotrophin (TSH) concentration of sheep and cattle plasma is described. The sensitivity of the assay allowed the measurement of 1–50 ng TSH/ml unextracted plasma. Cross-reaction with ovine luteinizing hormone, prolactin and growth hormone was very low. The average recovery of added TSH was 103 ± 4·1 (s.e.m.)% and the between-assay coefficient of variation was 13·8%.

The normal plasma TSH levels of sheep and cattle were approximately 2·5 ng/ml (5 mu. bovine TSH/100 ml). Foetal sheep had plasma TSH concentrations of approximately 3·2 ng/ml during the last 20 days of gestation. Levels of TSH in the circulation decreased abruptly after hypophysectomy of the foetal lamb and a decline in the plasma thyroxine (T4) concentrations was also apparent within 24 h of the operation. However, thyroidectomy of adult and foetal sheep did not increase plasma TSH concentrations until almost all the T4 had been cleared from the circulation.

The injection of T4 into thyroidectomized sheep rapidly reduced plasma TSH concentrations to normal values. However, the continued injection of T4 did not further reduce TSH concentration. The injection of T4 or triiodothyronine into normal sheep was also without effect on plasma TSH concentrations.

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D. F. SALAMAN
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SUMMARY

The changes in plasma concentration and anterior pituitary content of thyrotrophic hormone (TSH) after thyroidectomy in the rat were followed by means of an in vitro assay method. A triphasic change in plasma TSH was demonstrated which consisted of a threefold rise by the 2nd day, a fall to the normal range by the 5th day, and a gradual rise from the 10th day, which continued for at least 6 weeks.

The initial rise in plasma TSH was accompanied by a fall in the pituitary TSH store after 5 days to 7 % of the normal value; the store then remained low for the next 6 weeks.

Thyroxine (as measured by protein-bound 131I) disappeared from the circulation after thyroidectomy at a rate compatible with the observed rate of rise of plasma TSH; 20 % remained after 2 days.

The replacement of thyroid hormone by exogenous thyroxine in thyroidectomized rats resulted in 4 days in a decline in plasma TSH concentration to a subnormal value. During the next 3 days the blood level of TSH rose to 400 % of the control level. Thyroxine administration caused a large increase in the pituitary store of TSH.

The results indicate that circulating thyroxine influences primarily the rate of release of TSH from the anterior pituitary, and that a slower effect on the synthesis of TSH may be indirect and secondary to changes in the TSH content of the pituitary gland.

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S. P. BIDEY
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N. J. MARSHALL
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R. P. EKINS
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Slice preparations of normal human thyroid tissue have been used to investigate the effect of normal immunoglobulin G (IgG) on thyrotrophin (TSH)-induced accumulation of cyclic AMP. Incubation of slices in the presence of both TSH and normal IgG for 20 min reduced the stimulation of cyclic AMP accumulation elicited by TSH alone by approximately 30%. However, preincubation of slices with IgG for 100 min before addition of TSH virtually abolished the response to TSH. The latter effect of normal IgG was reversible, and removal of IgG before exposure to TSH allowed an unimpaired cyclic AMP response to TSH. The implications of these observations with respect to the application of this system to the functional bio-detection of thyroid-stimulating antibodies in IgG fractions from thyrotoxic sera are discussed.

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Kerstin Krause
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Stefan Karger
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Sien-Yi Sheu Division of Endocrinology, Institute of Pathology and Neuropathology, Institute of Pathology, Department of Surgery, Department of Internal Medicine, University of Leipzig, Ph.-Rosenthal-Str. 27, D-04103 Leipzig, Germany

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Thomas Aigner Division of Endocrinology, Institute of Pathology and Neuropathology, Institute of Pathology, Department of Surgery, Department of Internal Medicine, University of Leipzig, Ph.-Rosenthal-Str. 27, D-04103 Leipzig, Germany

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Romy Kursawe
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Oliver Gimm Division of Endocrinology, Institute of Pathology and Neuropathology, Institute of Pathology, Department of Surgery, Department of Internal Medicine, University of Leipzig, Ph.-Rosenthal-Str. 27, D-04103 Leipzig, Germany

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Kurt-Werner Schmid Division of Endocrinology, Institute of Pathology and Neuropathology, Institute of Pathology, Department of Surgery, Department of Internal Medicine, University of Leipzig, Ph.-Rosenthal-Str. 27, D-04103 Leipzig, Germany

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Henning Dralle Division of Endocrinology, Institute of Pathology and Neuropathology, Institute of Pathology, Department of Surgery, Department of Internal Medicine, University of Leipzig, Ph.-Rosenthal-Str. 27, D-04103 Leipzig, Germany

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Dagmar Fuhrer
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/ml ascorbic acid (all from Sigma–Aldrich), 5 μg/ml transferrin (Calbiochem, Darmstadt, Germany) and 5 mU/ml bovine thyrotrophin (TSH) (Sigma–Aldrich). FTC-133 cells were maintained in DMEM containing 10% calf serum and 1% penicillin–streptomycin (Invitrogen

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C. A. Ollis
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A. Fowles
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B. L. Brown
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D. S. Munro
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S. Tomlinson
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ABSTRACT

Confluent monolayer cultures of human thyroid cells secreted low levels of immunoassayable triiodothyronine (T3) and this process could be stimulated by TSH in a concentration-dependent manner. The characteristics of the response to TSH were related to the age of the thyroid cell culture both in terms of the relative sensitivity to TSH and the quantity of T3 released. Cells which had been in culture for 2–3 days (primary cultures) secreted high levels of T3 under unstimulated and TSH-stimulated conditions with a median effective dose (ED50) for TSH of 0·030 mu. TSH/ml. However, cells which had been subcultured and consequently had been in culture for a longer period of 6–7 days secreted lower levels of T3 under basal and stimulated conditions. This was approximately 30% of that released from primary cultures with an ED50 for TSH of 0·1 mu. TSH/ml. Reorganization of human thyroid cells into follicular structures was seen during growth with TSH but these cultures showed little response to subsequent acute stimulation by TSH; the return of a diminished, less sensitive response to TSH was seen after a recovery period of 8 h. The time-course of T3 release was dependent on the TSH concentration with low TSH concentrations stimulating T3 secretion after increased incubation periods. Human thyroid cells had lost the ability to concentrate and organify free iodide after several days in culture but were still secreting T3. This indicates the presence of intracellular stores of T3 which are released on stimulation with TSH, rather than new synthesis of T3.

J. Endocr. (1985) 104, 285–290

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C. P. Verschueren
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G. R. Rutteman
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J. H. Vos
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J. E. Van Dijk
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T. W. A. de Bruin
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ABSTRACT

Thyrotrophin (TSH) is the conditional growth factor of thyroid epithelial cells. Abnormalities in TSH-receptor binding such as a low receptor number or low binding affinity may be a marker of thyroid carcinoma or metastases, or may exhibit a relationship with the functional variability of such tissues. The dog was used as a model to characterize TSH-receptor binding in normal thyroid tissues, naturally occurring thyroid neoplasms and distant metastases. In normal dog thyroid tissues, specific 125I-labelled TSH binding ranged from 2·7 to 15·5%, and low cross-reactivity with bovine LH (0·023%) was observed. One class of TSH-binding sites was found in eight normal thyroid tissues and 22 thyroid carcinomas; two normal thyroid tissues and one tumour exhibited two classes of binding sites. The concentration of binding sites was lower in the five carcinomas with reduced pertechnetate uptake (0·09 pmol/mg protein) than in the five thyroid neoplasms with increased uptake (0·19 pmol/mg) (P= 0·055). Compared with the original carcinoma tissues, TSH binding revealed a reduced binding affinity in eight out of eleven metastases. Two metastases showed a complete absence of TSH binding, suggesting that they were not dependent on TSH for growth. We conclude that one class of TSH-binding site is predominant in normal dog thyroid tissues and dog thyroid carcinomas. TSH could therefore contribute, at least in theory, to further growth of primary dog thyroid carcinomas. Secondly, assays measuring TSH binding may not be able to discriminate between malignant and benign dog thyroid tumours. TSH receptor number or affinity may be related to the functional variability of thyroid neoplasms. The absence of TSH binding in some metastases demonstrated that this characteristic can be acquired during the natural history of a differentiated thyroid carcinoma.

Journal of Endocrinology (1992) 132, 461–468

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Maria H Warner Clinical Biochemistry, University of Edinburgh, The Royal Infirmary of Edinburgh, 51 Little France Crescent, Edinburgh EH16 4SA, UK

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Geoffrey J Beckett Clinical Biochemistry, University of Edinburgh, The Royal Infirmary of Edinburgh, 51 Little France Crescent, Edinburgh EH16 4SA, UK

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thyrotrophin (TSH), thyroxine (T 4 ) and T 3 . Thyroid function testing becomes problematic when the tests are performed in patients who have any significant co-existing illness (organic or psychiatric), since the illness per se may give rise to changes in

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Emmely M de Vries Department of Endocrinology and Metabolism, Academic Medical Center, University of Amsterdam, Meibergdreef 9, 1105 AZ Amsterdam, The Netherlands

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Eric Fliers Department of Endocrinology and Metabolism, Academic Medical Center, University of Amsterdam, Meibergdreef 9, 1105 AZ Amsterdam, The Netherlands

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Anita Boelen Department of Endocrinology and Metabolism, Academic Medical Center, University of Amsterdam, Meibergdreef 9, 1105 AZ Amsterdam, The Netherlands

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) concentrations, increased serum reverse T 3 (rT 3 ) concentrations and unaltered or inappropriately low serum thyroid-stimulating hormone (TSH), indicating profoundly altered negative feedback in the pituitary and hypothalamus ( Docter et al . 1993 ). The

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C Giuliani Unit of Endocrinology, Department of Medicine and Sciences of Aging, University ‘G D’Annunzio’ and Aging Research Center, Ce.S.I., ‘Gabriele D’Annunzio’ University Foundation, Campus Universitario, via Colle dell’Ara, 66013 Chieti, Italy
Arthur G Janes Cancer Center and Richard J Solove Research Institute, Ohio State University, Columbus, Ohio 43210, USA
Unit of Immuno-oncology Aging Research Center, Ce.S.I., ‘Gabriele D’Annunzio’ University Foundation, Chieti-Pescara, Italy
Experimental Immunology Branch, National Cancer Institute, National Institutes of Health, Bethesda, Maryland 20892, USA
Edison Biotechnology Institute and Department of Biomedical Sciences, College of Osteopathic Medicine, Ohio University, Athens, Ohio 45701, USA

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M Saji Unit of Endocrinology, Department of Medicine and Sciences of Aging, University ‘G D’Annunzio’ and Aging Research Center, Ce.S.I., ‘Gabriele D’Annunzio’ University Foundation, Campus Universitario, via Colle dell’Ara, 66013 Chieti, Italy
Arthur G Janes Cancer Center and Richard J Solove Research Institute, Ohio State University, Columbus, Ohio 43210, USA
Unit of Immuno-oncology Aging Research Center, Ce.S.I., ‘Gabriele D’Annunzio’ University Foundation, Chieti-Pescara, Italy
Experimental Immunology Branch, National Cancer Institute, National Institutes of Health, Bethesda, Maryland 20892, USA
Edison Biotechnology Institute and Department of Biomedical Sciences, College of Osteopathic Medicine, Ohio University, Athens, Ohio 45701, USA

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I Bucci Unit of Endocrinology, Department of Medicine and Sciences of Aging, University ‘G D’Annunzio’ and Aging Research Center, Ce.S.I., ‘Gabriele D’Annunzio’ University Foundation, Campus Universitario, via Colle dell’Ara, 66013 Chieti, Italy
Arthur G Janes Cancer Center and Richard J Solove Research Institute, Ohio State University, Columbus, Ohio 43210, USA
Unit of Immuno-oncology Aging Research Center, Ce.S.I., ‘Gabriele D’Annunzio’ University Foundation, Chieti-Pescara, Italy
Experimental Immunology Branch, National Cancer Institute, National Institutes of Health, Bethesda, Maryland 20892, USA
Edison Biotechnology Institute and Department of Biomedical Sciences, College of Osteopathic Medicine, Ohio University, Athens, Ohio 45701, USA

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G Fiore Unit of Endocrinology, Department of Medicine and Sciences of Aging, University ‘G D’Annunzio’ and Aging Research Center, Ce.S.I., ‘Gabriele D’Annunzio’ University Foundation, Campus Universitario, via Colle dell’Ara, 66013 Chieti, Italy
Arthur G Janes Cancer Center and Richard J Solove Research Institute, Ohio State University, Columbus, Ohio 43210, USA
Unit of Immuno-oncology Aging Research Center, Ce.S.I., ‘Gabriele D’Annunzio’ University Foundation, Chieti-Pescara, Italy
Experimental Immunology Branch, National Cancer Institute, National Institutes of Health, Bethesda, Maryland 20892, USA
Edison Biotechnology Institute and Department of Biomedical Sciences, College of Osteopathic Medicine, Ohio University, Athens, Ohio 45701, USA

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M Liberatore Unit of Endocrinology, Department of Medicine and Sciences of Aging, University ‘G D’Annunzio’ and Aging Research Center, Ce.S.I., ‘Gabriele D’Annunzio’ University Foundation, Campus Universitario, via Colle dell’Ara, 66013 Chieti, Italy
Arthur G Janes Cancer Center and Richard J Solove Research Institute, Ohio State University, Columbus, Ohio 43210, USA
Unit of Immuno-oncology Aging Research Center, Ce.S.I., ‘Gabriele D’Annunzio’ University Foundation, Chieti-Pescara, Italy
Experimental Immunology Branch, National Cancer Institute, National Institutes of Health, Bethesda, Maryland 20892, USA
Edison Biotechnology Institute and Department of Biomedical Sciences, College of Osteopathic Medicine, Ohio University, Athens, Ohio 45701, USA

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D S Singer Unit of Endocrinology, Department of Medicine and Sciences of Aging, University ‘G D’Annunzio’ and Aging Research Center, Ce.S.I., ‘Gabriele D’Annunzio’ University Foundation, Campus Universitario, via Colle dell’Ara, 66013 Chieti, Italy
Arthur G Janes Cancer Center and Richard J Solove Research Institute, Ohio State University, Columbus, Ohio 43210, USA
Unit of Immuno-oncology Aging Research Center, Ce.S.I., ‘Gabriele D’Annunzio’ University Foundation, Chieti-Pescara, Italy
Experimental Immunology Branch, National Cancer Institute, National Institutes of Health, Bethesda, Maryland 20892, USA
Edison Biotechnology Institute and Department of Biomedical Sciences, College of Osteopathic Medicine, Ohio University, Athens, Ohio 45701, USA

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F Monaco Unit of Endocrinology, Department of Medicine and Sciences of Aging, University ‘G D’Annunzio’ and Aging Research Center, Ce.S.I., ‘Gabriele D’Annunzio’ University Foundation, Campus Universitario, via Colle dell’Ara, 66013 Chieti, Italy
Arthur G Janes Cancer Center and Richard J Solove Research Institute, Ohio State University, Columbus, Ohio 43210, USA
Unit of Immuno-oncology Aging Research Center, Ce.S.I., ‘Gabriele D’Annunzio’ University Foundation, Chieti-Pescara, Italy
Experimental Immunology Branch, National Cancer Institute, National Institutes of Health, Bethesda, Maryland 20892, USA
Edison Biotechnology Institute and Department of Biomedical Sciences, College of Osteopathic Medicine, Ohio University, Athens, Ohio 45701, USA

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L D Kohn Unit of Endocrinology, Department of Medicine and Sciences of Aging, University ‘G D’Annunzio’ and Aging Research Center, Ce.S.I., ‘Gabriele D’Annunzio’ University Foundation, Campus Universitario, via Colle dell’Ara, 66013 Chieti, Italy
Arthur G Janes Cancer Center and Richard J Solove Research Institute, Ohio State University, Columbus, Ohio 43210, USA
Unit of Immuno-oncology Aging Research Center, Ce.S.I., ‘Gabriele D’Annunzio’ University Foundation, Chieti-Pescara, Italy
Experimental Immunology Branch, National Cancer Institute, National Institutes of Health, Bethesda, Maryland 20892, USA
Edison Biotechnology Institute and Department of Biomedical Sciences, College of Osteopathic Medicine, Ohio University, Athens, Ohio 45701, USA

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G Napolitano Unit of Endocrinology, Department of Medicine and Sciences of Aging, University ‘G D’Annunzio’ and Aging Research Center, Ce.S.I., ‘Gabriele D’Annunzio’ University Foundation, Campus Universitario, via Colle dell’Ara, 66013 Chieti, Italy
Arthur G Janes Cancer Center and Richard J Solove Research Institute, Ohio State University, Columbus, Ohio 43210, USA
Unit of Immuno-oncology Aging Research Center, Ce.S.I., ‘Gabriele D’Annunzio’ University Foundation, Chieti-Pescara, Italy
Experimental Immunology Branch, National Cancer Institute, National Institutes of Health, Bethesda, Maryland 20892, USA
Edison Biotechnology Institute and Department of Biomedical Sciences, College of Osteopathic Medicine, Ohio University, Athens, Ohio 45701, USA

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that regulate cell growth and function – thyroid-stimulating hormone (TSH), hydrocortisone, insulin, insulin-like growth factor (IGF)-I and iodide – coordinately and specifically decrease MHC class I expression ( Saji et al. 1992 a , 1992 b , 1997

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