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At least 109 records · Page 6Linked to original sources
PubMed1986

[Serum thyroglobulin in the diagnosis of metastases of differentiated thyroid cancer. Effect of suppressive thyroid hormone substitution on the diagnostic accuracy of thyroglobulin values].

The diagnostic accuracy of serum thyroglobulin (S-TG) determination as measured under endogenous thyrotropin(TSH)stimulation (ETS) has been investigated in 372 patients with completed therapy for differentiated thyroid cancer. In 51 of these (13.7%) S-TG could be detected by means of the IRMA-technique. In 34 S-TG determination was additionally performed during suppressive thyroxine therapy (SSH): S-TG in SSH was significantly lower as compared with S-TG in ETS (p less than 0.001). In seven cases with proven metastases S-TG values were pushed below the minimal detection level by SSH. Tumor manifestations with suppressible S-TG were significantly smaller (mean = 5 ccm, range 1-25 ccm) than those with non-suppressible S-TG (mean = 90 ccm, range 11-125 ccm, p less than 0.005) and displayed a papillary histology. There was a moderate correlation between S-TG concentration and tumor volume (r = 0.71; p less than 0.001). 21% (n = 66) of patients with undetectable S-TG in ETS showed 131I-uptake in the thyroid region; 2% (n = 7) had proven metastases. Sensitivity of S-TG determination for the detection of metastases amounted to 82.5% in ETS and 53.3% in SST, specificity was 94.6% in ETS and 99.7% in SST. It is concluded that small metastases of papillary thyroid carcinomas may escape S-TG screening more readily than follicular carcinoma metastases when S-TG concentrations are measured during thyroxine treatment.

Adenocarcinoma↗
PubMedDate not supplied

[Thyroglobulin biosynthesis and the content of thyroglobulin polyribosomes of the thyroid gland cells in the normal state and in various types of thyroid pathology].

The content of polyribosomes in human thyroid cells was studied in health and different forms of thyroid pathology. In thyroid pathology, thyroglobulin (TG) polyribosome content in thyroid cells diminished in the following order: diffuse toxic goiter greater than mixed euthyroid goiter greater than nodular toxic goiter greater than Hashimoto's goiter and complete absence of TG synthesizing polyribosomes in thyroid cancer and congenital goiter cells. No correlation was revealed between polyribosome TG content and thyroid function. It is inferred that impairment of TG biosynthesis in thyroid diseases is related to the decreased content of polyribosome TG in thyroid cells.

Humans↗
PubMed1983

Thyroid autoantibody synthesis by cultures of thyroid and peripheral blood lymphocytes. II. Effect of thyroglobulin on thyroglobulin antibody synthesis.

The influence of antigen (thyroglobulin, Tg) on Tg antibody synthesis has been investigated using cultures of Hashimoto thyroid and peripheral blood lymphocytes. In cultures of thyroid lymphocytes, Tg antibody synthesis was stimulated by a 24h pulse of Tg (10-100 micrograms/ml) and similar results were obtained using spleen lymphocytes from BALB/c mice immunized with human Tg. In contrast, Tg antibody synthesis by Hashimoto peripheral blood lymphocytes was not affected by similar concentrations of Tg (1-240 micrograms/ml) in the presence or absence of pokeweed mitogen (PWM). However, peripheral blood lymphocytes from two out of nine patients produced increased levels of Tg antibody in the presence of very low concentrations of Tg (50 ng/ml). This increase in Tg antibody production was accompanied by a rise in total IgG synthesis indicating that the response to Tg was polyclonal. On the basis of other unusual features of the lymphocyte cultures from these two patients including a relatively small response to PWM and evidence of circulating plasma cells, it is suggested that sufficient numbers of lymphocytes responsive to Tg are only released into the circulation during active phases of the disease process.

Adult↗
PubMed1984

Injection of mouse thyroglobulin and/or adult thymectomy do not break tolerance to thyroglobulin during the lupus like graft versus host disease in mice.

In a previous paper (Gleichmann, van Elven & van der Veen, 1982), it had been reported that, in contrast to lupus like autoantibodies such as anti-DNA, autoantibodies to mouse thyroglobulin (MTg) were not detectable in serum of F1 mice suffering from a lupus like graft versus host disease (GVHD) (GVH F1). In the present paper, possible explanations for this restricted autoantibody formation during the potent allogeneic stimulation were investigated. The main question was whether the natural level of circulating MTg was too low to induce the formation of anti-MTg antibodies in GVH F1 mice. Existence, in the F1 mice studied, of B cells capable of producing anti-MTg antibodies was demonstrated by injection of lipopolysaccharide (LPS) and exogeneous MTg. However, MTg injected into various F1 mice at the onset of the GVH reaction (GVHR) failed to overcome the lack of antibody formation to MTg even though the GVHR led to a severe lupus like disease. Furthermore, adult thymectomy (ATx) of either the recipients, the donors, or both also did not break tolerance to MTg during the GVHR, irrespective of administration of exogeneous MTg. Thus, neither intravenous injection of MTg nor ATx, designed to remove T suppressor (TS) cells, is adequate to enable an autoantibody response to MTg during lupus like GVHD. Hence, the non-specific T cell help that causes lupus like GVHD seems to be intrinsically insufficient to trigger the Tg reactive B cells. We suggest that globular proteins, such as Tg, require specific T cell help. In the presence of only non-specific T help, self-antigens such as DNA seem to be more apt than globular proteins to provide an effective signal 1 to the corresponding autoreactive B cells.

Animals↗
PubMed1980

Radioimmunoassay of human thyroglobulin with use of "thyroglobulin-free" plasma prepared by ultracentrifugation as diluent.

We describe the preparation and evaluation of a new diluent for use in preparing standard curves for the radioimmunoassay of human thyroglobulin (TG). This diluent, "TG-free human plasma, allows measurement of TG in lower concentrations than with previous assay systems because the components of the standards are more similar to those of the samples. TG-free plasma was prepared by a modification of the differential centrifugation method of Edelhoch (J. Biol. Chem. 235:1326, 1960). Standard curves prepared by use of TG-free plasma and plasma obtained from thyroidectomized patients were identical. In our assay, plasma from patients who had undergone total thyroidectomy produced no displacement when 25 to 100 microL of plasma was assayed. Twenty-five normal subjects all had detectable TG concentrations, ranging from 4.0 to 25.7 microgram/L. Only 27 of 2000 determinations performed by this new method had undetectable values and 26 of these were from patients with total or near-total thyroidectomies. TG concentration determined by this assay may be more sensitive for finding recurrent thyroid malignancy.

Animals↗
PubMed1994

[Chemical iodination of hormonogenic tyrosine residues of human thyroglobulin is critical for the production of anti-thyroglobulin autoantibody and for the induction of experimental autoimmune thyroiditis in mice].

There is evidence from animal models that the iodine content of thyroglobulin (Tg) may influence its antigenicity in thyroid autoimmunity. To elucidate the effect of iodination of hormonogenic sites of human Tg (hTg) on its autoantigenicity, a synthetic peptide (TB: hTg 2546-2571), containing two hormonogenic tyrosine residues of hTg, and a chemically-iodinated peptide (TB-I) were prepared. We immunized C3H/He (H-2k) mice, a high responder strain to Tg, and BALB/c (H-2d), a low responder strain, with TB or TB-I plus lipopolysaccharide. Lymph node cells from the two strains immunized with TB or TB-I proliferated in response to both TB and TB-I. Anti-Tg autoantibodies were detected in both strains when immunized with TB-I, while immunization with TB failed to produce anti-Tg antibodies. Furthermore, one of the C3H/He mice immunized with TB-I developed diffuse thyroiditis, but BALB/c mice did not. These findings indicate that the iodination of the hormonogenic tyrosine residues of hTg, in other words, the synthesis of mono- and di-iodotyrosine (MIT and DIT) residues, is necessary for the production of anti-Tg autoantibodies in high and low responder mice and for the induction of autoimmune thyroiditis in high responder mice.

Amino Acid Sequence↗
PubMed1993

Recognition of triiodothyronine-containing epitopes in canine thyroglobulin by circulating thyroglobulin autoantibodies.

Serum triiodothyronine autoantibody (T3 AA), triiodothyronine (T3), and thyroxine (T4) concentrations were determined in 45 canine sera containing substantial amounts of thyroglobulin autoantibodies (Tg AA); sera also were assayed to investigate the ability of free T3 to inhibit Tg AA binding to canine Tg. Serum T3 AA concentrations defined 2 groups of sera; 28 sera had low T3 AA concentration (< or = 20 ng/ml) and 17 sera had high T3 AA concentration (> or = 250 ng/ml). Direct linear correlation between T3 AA concentration and apparent serum T3 concentration was observed (r = 0.75). Serum with low T3 AA concentration had apparent T3 concentration that was significantly (P < 0.01) lower than that in serum with high T3 AA concentration. Mean serum T4 concentration was not significantly different between serum with low or high T3 AA concentration. Mean Tg AA activity was significantly (P < 0.05) lower in serum with low T3 AA concentration than in serum with high T3 AA concentration. Addition of free T3 to serum significantly (P < 0.05) decreased detectable activity of Tg AA in both groups of sera. However, significant difference in magnitude of the reduction was not observed between sera with low or high T3 AA concentration. Results indicate that a fraction of Tg AA recognizes T3-containing epitopes in Tg. Increased prevalence of T3 AA for serum with high Tg AA activity indicates that T3 AA may be another valid indicator of lymphocytic thyroiditis. These antibodies may be generated against the hormonogenic epitopes of Tg.

Animals↗
PubMed1996

ELISA for thyroglobulin in serum: recovery studies to evaluate autoantibody interference and reliability of thyroglobulin values.

An ELISA for measuring thyroglobulin (Tg) in serum was developed with polyclonal antibodies to Tg on the solid phase and two monoclonal antibodies to Tg as the second antibodies. The assay has a detection limit of 1 microgram/L, a within-run imprecision (CV) of <7%, and a between-run CV of < 10%. Parallelism of the assay was shown in dilution studies, in which the percent observed/expected values for n = 5 autoantibody-containing samples gave a mean of 99% (SD 13.1 %); for n = 5 samples with undetectable autoantibody concentrations, the mean was 103% (SD 11.8%). The correlation of the ELISA with an RIA for Tg in 46 normal samples was ELISA = 1.11(RIA) + 0.52, S y/x = 2.23, SD intercept = 0.54, SD slope = 0.03, range = 0 to 53 micrograms/L, r = 0.980. Comparison of the ELISA with a reference laboratory RIA for 29 clinical samples gave a correlation of: ELISA = 1.53(RIA) - 0.48, S y/x = 9.00, SD intercept = 2.19, SD slope = 0.10, range = 0 to 98 micrograms/L, r = 0.950. To provide additional information concerning the reliability of the Tg measurement in samples containing autoantibodies to Tg, we developed a procedure for determining the percent recovery. A percent recovery greater than or equal to 80% indicates minimal interference by autoantibodies in this assay. The assay is straightforward to perform, results can be posted within 8 h, and the routinely good recovery of Tg in the presence of Tg autoantibodies indicates minimal autoantibody interference in this assay.

Adult↗