A study of thyroglobulin and peroxidase activity in the thyroid tissue of patients with non-endemic non-toxic nodular goitre

1991 ◽  
Vol 80 (4) ◽  
pp. 301-307 ◽  
Author(s):  
T. Mories ◽  
J. M. Miralles ◽  
A. Reglero ◽  
S. Felipe ◽  
J. J. Corrales ◽  
...  
Keyword(s):  
Peroxidase Activity ◽  
Thyroid Tissue ◽  
Enzymic Activity ◽  
Thyroid Peroxidase ◽  
Carbohydrate Composition ◽  
Nodular Goitre ◽  
Hormone Synthesis ◽  
Control Subjects ◽  
The Mean ◽  
Second Peak

1. A study was made of the activity of the enzyme thyroid peroxidase and of the concentration, carbohydrate composition and the degree of iodination of thyroglobulin in the thyroid glands of 60 patients with non-endemic non-toxic goitre in the nodular phase and in those of 25 control subjects. 2. Thyroid peroxidase activity was determined by the guaiacol assay and was significantly higher in patients with non-endemic non-toxic goitre than in control subjects (3.60 ± 2.51 and 2.07 ± 1.08 μmol of guaiacol oxidized min−1 g−1 of tissue, respectively; ranges 0.16–10.57 and 0.52–4.85 μmol of guaiacol oxidized min−1 g−1 of tissue, respectively; P <0.05). 3. Thyroglobulin was purified by precipitation with ammonium sulphate and Sephadex G-200 gel filtration. Two protein peaks were obtained which were identified as thyroglobulin and measured by radioimmunoassay. The concentration of thyroglobulin in the first peak was 98.94 (SD 84.87, range 0.60–455.54) mg/g of tissue for the patients with non-endemic, non-toxic goitre and 51.41 (SD 28.34, range 14.99–106.39) mg/g of tissue for the control subjects (P <0.01). The second peak showed 1.26 (SD 1.27, range 0.09–6.50) mg of thyroglobulin/mg of tissue for the group with non-endemic non-toxic goitre and 0.51 (SD 0.25, range 0.15–0.98 mg of thyroglobulin/mg of tissue) for the control subjects (P <0.01). 4. The carbohydrate composition of thyroglobulin was determined by acid hydrolysis and colorimetry, evaluating the levels of hexoses, hexosamines and sialic acid. The degree of glycosylation was significantly higher in thyroglobulin from patients with non-endemic non-toxic goitre (mean 16.46%, SD 5.68%, range 8.33–37.3% for the first peak, and mean 16.11%, SD 4.85%, range 5.30–33.10% for the second peak) than that from control subjects (mean 9.62%, SD 1.23%, range 7.56–12.02% for the first peak, and mean 8.68%, SD 0.99%, range 7.24–11.09% for the second peak). The values for each of the carbohydrates were significantly higher in the thyroglobulin from patients with non-endemic non-toxic goitre than in the control subjects, and there was also a positive correlation between them, except for the hexoses and hexosamines in the second peak of the thyroglobulin from the control subjects. 5. The thyroglobulin of the group with non-endemic non-toxic goitre was significantly less iodinated (mean 0.055%, SD 0.038%, range 0.021–0.161% in the first peak, and mean 0.30%, SD 0.22%, range 0.10–0.93% in the second peak) than that of the control subjects (mean 0.32%, SD 0.16%, range 0.07–0.64% in the first peak, and mean 0.77%, SD 0.17%, range 0.37–1.27% in the second peak). 6. A significant negative correlation was observed between the degree of thyroglobulin iodination and thyroid peroxidase activity in control subjects; however, this was not found in patients with non-endemic non-toxic goitre. The mean level of peroxidase activity in the latter group was 26.71% above what would be expected for the mean degree of thyroglobulin iodination found, indicating that other additional factors may govern the increase in enzymic activity. 7. Such findings point to the existence of an alteration in thyroglobulin that may decrease the efficiency of the protein for normal hormone synthesis, and this may be one of the reasons for the development and/or maintenance of non-endemic non-toxic goitre.

Inhibition by immunoglobulin G of synthesis of thyroid hormone in thyroid cultures from hypothyroid patients with goitrous Hashimoto's thyroiditis

1990 ◽  
Vol 123 (5) ◽  
pp. 511-518 ◽  
Author(s):  
Jaeduk Noh ◽  
Noboru Hamada ◽  
Hifumi Saito ◽  
Midori Yoshimoto ◽  
Hiroyuki Iwasaki ◽  
...  
Keyword(s):  
Thyroid Hormone ◽  
Peroxidase Activity ◽  
Immunoglobulin G ◽  
Hashimoto’S Thyroiditis ◽  
Thyroid Tissue ◽  
Hashimoto's Thyroiditis ◽  
Thyroid Peroxidase ◽  
Hormone Synthesis ◽  
Microsomal Antibody ◽  
Hypothyroid Patients

Abstract. Recently, thyroid microsomal antigen was identified as thyroid peroxidase, and thyroid microsomal antibody was found to inhibit thyroid peroxidase activity in vitro. We investigated the possibility that anti-microsomal antibody inhibits the iodination of tyrosine, in vivo. Immunoglobulin G with or without anti-microsomal antibody from hypothyroid patients with goitrous Hashimoto's thyroiditis inhibited thyroid hormone synthesis in cultured slices of normal human thyroid tissue. IgGs with anti-microsomal antibody inhibited 125I thyroidal uptake and thyroid hormone synthesis stimulated by TSH more than normal IgG did. However, the same results were obtained with IgGs without anti-microsomal antibody. This effect did not involve anti-microsomal antibody, anti-thyroglobulin antibody, TSH-binding inhibitor immunoglobulin, thyroid stimulation-blocking immunoglobulin, or the cAMP level of the thyroid tissue. The ratio of organic I to inorganic I with stimulation by TSH in slices incubated with IgG from hypothyroid patients with goitrous Hashimoto's thyroiditis or normal IgG was not significantly different, but was significantly higher in slices incubated with methylmercaptoimidazole. Therefore, IgG from hypothyroid patients with goitrous Hashimoto's thyroiditis mainly suppressed 125I thyroidal uptake, rather than inhibiting thyroid peroxidase activity. In addition, this IgG was present in the serum of 11 of the 12 hypothyroid patients with Hashimoto's thyroiditis studied. This IgG may be involved in the mechanism that causes hypothyroidism in some patients with goitrous Hashimoto's disease.

scholarly journals Subcellular structure of bovine thyroid gland. The localization of the peroxidase activity in bovine thyroid

1978 ◽  
Vol 174 (3) ◽  
pp. 939-949 ◽  
Author(s):  
M J S De Wolf ◽  
A R Lagrou ◽  
H J J Hilderson
Keyword(s):  
Peroxidase Activity ◽  
Buoyant Density ◽  
Thyroid Tissue ◽  
Guaiacol Peroxidase ◽  
Subcellular Structure ◽  
The Third ◽  
Bovine Thyroid ◽  
Two Peaks ◽  
Second Peak ◽  
Membranous Material

1. After differential pelleting of bovine thyroid tissue the highest relative specific activities for plasma membrane markers are found in the L fraction whereas those for peroxidase activities (p-phenylenediamine, guaiacol and 3,3′-diaminobenizidine tetrachloride peroxidases) are found in the M fraction. 2. When M + L fractions were subjected to buoyant-density equilibration in a HS zonal rotor all peroxidases show different profiles. The guaiacol peroxidase activity always follows the distribution of glucose 6-phosphatase. 3. When a Sb fraction is subjected to Sepharose 2B chromatography three major peaks are obtained. The first, eluted at the void volume, consists of membranous material and contains most of the guaiacol peroxidase activity. Most of the protein (probably thyroglobulin) is eluted with the second peak. Solubilized enzymes are recovered in the third peak. 4. p-Phenylenediamine peroxidase activity penetrates into the gel on polyacrylamidegel electrophoresis, whereas guaiacol peroxidase activity remains at the sample zone. 5. DEAE-Sephadex A-50 chromatography resolves the peroxidase activities into two peaks, displaying different relative amounts of the different enzymic activities in each peak. 6. The peroxidase activities may be due to the presence of different proteins. A localization of guaiacol peroxidase in rough-endoplasmic-reticulum membranes (or in membranes related to them) seems very likely.

scholarly journals Increased Expression of the Na+/I− Symporter in Cultured Human Thyroid Cells Exposed to Thyrotropin and in Graves’ Thyroid Tissue*

1997 ◽  
Vol 82 (10) ◽  
pp. 3331-3336 ◽  
Author(s):  
Tsukasa Saito ◽  
Toyoshi Endo ◽  
Akio Kawaguchi ◽  
Masato Ikeda ◽  
Minoru Nakazato ◽  
...  
Keyword(s):  
Thyroid Tissue ◽  
Human Thyroid ◽  
Thyroid Peroxidase ◽  
Graves Disease ◽  
Intracellular Camp ◽  
Normal Thyroid Tissue ◽  
Thyroid Cells ◽  
Normal Thyroid ◽  
Hormone Synthesis ◽  
Messenger Ribonucleic Acid

Abstract The Na+/I− symporter (NIS) is important in hormone synthesis in the thyroid gland. NIS activity, as reflected by I− uptake, was increased by TSH (1 mU/mL) or forskolin (10μ mol/L) in primary cultured human thyroid cells. Northern blot analysis revealed that incubation of these cells with TSH or forskolin for 24 h increased the abundance of NIS messenger ribonucleic acid (mRNA) 2.3- and 2.5-fold, respectively. Immunoblot analysis revealed 2.7- and 2.4-fold increases, respectively, in the amount of NIS protein after 48 h, suggesting that elevated levels of intracellular cAMP induced the expression of NIS in human thyrocytes. We then studied the levels of NIS mRNA and protein in Graves’ thyroid tissue and found that the amount of NIS mRNA in thyroid tissue from individuals with Graves’ disease (n = 5) was 3.8 times that in normal thyroid tissue (n = 5). The abundance of NIS mRNA was significantly correlated with that of thyroid peroxidase or thyroglobulin mRNAs, but not with that of TSH receptor mRNA, in the Graves’ and normal thyroid tissue specimens. The amount of NIS protein was also increased 3.1-fold in Graves’ thyroid tissue compared with that in normal thyroid tissue. The increased expression of NIS may thus contribute to the development of Graves’ disease.

EFFECT OF TSH ON cAMP AND cGMP LEVELS IN THYROID CANCERS, ADENOMAS AND NORMAL HUMAN THYROID TISSUE

1978 ◽  
Vol 87 (1) ◽  
pp. 106-113 ◽  
Author(s):  
Colette Thomas-Morvan
Keyword(s):  
Thyroid Tissue ◽  
Camp Level ◽  
Human Thyroid ◽  
Cgmp Level ◽  
Camp Content ◽  
Thyroid Cancers ◽  
Hormone Synthesis ◽  
Normal Tissues ◽  
Human Thyroid Tissue ◽  
The Mean

ABSTRACT The effect of TSH (50 mU/ml) alone or in combination with theophylline (10 mm) on the cAMP level in human thyroid tissue after a 10 min incubation has been studied in 8 normal tissues, 7 adenomas and 10 thyroid cancers (8 differentiated and 1 anaplastic). Our results have shown the lack of responsiveness to TSH in the 2 anaplastic carcinomas studied, as well as in 4 cases among the 8 differentiated cancers studied. In thyroid adenomas, on the contrary, the cAMP increase in response to TSH was close to that observed in normal tissues. In these adenomas, the mean basal cAMP level (0.43 ± 0.07 pmol/mg tissue) was not statistically different from that in normal tissues (0.36 ± 0.06), while in thyroid cancers the mean basal cAMP level (0.93 ± 0.26) was significantly greater than that in normal tissues (P < 0.05). The cGMP level was measured in the same conditions in 7 normal thyroid tissues and 8 thyroid cancers (7 differentiated and 1 anaplastic). The mean basal cGMP level in these cancers (9 ± 1 fmol/mg tissue) was not statistically different from that in normal tissues (12 ± 2). In response to TSH, no increase of cGMP level was observed in cancers, or in the normal tissues. The disorders of hormone synthesis previously seen in human thyroid cancers did not appear related to a decreased cAMP content, but might be due to a lack of responsiveness to TSH in undifferentiated cancers and in some cases of differentiated carcinomas.

scholarly journals Association of Duoxes with Thyroid Peroxidase and Its Regulation in Thyrocytes

2010 ◽  
Vol 95 (1) ◽  
pp. 375-382 ◽  
Author(s):  
Yue Song ◽  
Jean Ruf ◽  
Philippe Lothaire ◽  
Didier Dequanter ◽  
Guy Andry ◽  
...  
Keyword(s):  
Thyroid Hormone ◽  
Protein Kinase ◽  
Plasma Membranes ◽  
Cell Damage ◽  
Thyroid Tissue ◽  
Human Thyroid ◽  
Thyroid Peroxidase ◽  
Thyroid Cells ◽  
Hormone Synthesis ◽  
Thyroid Hormone Synthesis

Abstract Context: Thyroid hormone synthesis requires H2O2 produced by dual oxidases (Duoxes) and thyroperoxidase (TPO). Defects in this system lead to congenital hypothyroidism. H2O2 damage to the thyrocytes may be a cause of cancer. Objective: The objective of the study was to investigate whether Duox and TPO, the H2O2 producer and consumer, might constitute a complex in the plasma membrane of human thyroid cells, thus maximizing efficiency and minimizing leakage and damage. Design: The interaction between Duox and TPO was studied by coimmunoprecipitation and Western blotting of plasma membranes from incubated follicles prepared from freshly resected human thyroid tissue from patients undergoing thyroidectomy, and COS-7 cells transiently transfected with the entire Duoxes or truncated [amino (NH2) or carboxyl (COOH) terminal]. Results: The following results were reached: 1) Duox and TPO from membranes are coprecipitated, 2) this association is up-regulated through the Gq-phospholipase C-Ca2+-protein kinase C pathway and down-regulated through the Gs-cAMP-protein kinase A pathway, 3) H2O2 increases the association of Duox1 and Duox2 to TPO in cells and in membranes, and 4) truncated NH2- or COOH-terminal Duox1 and Duox2 proteins show different binding abilities with TPO. Conclusion: Coimmunoprecipitations show that Duox and TPO locate closely in the plasma membranes of human thyrocytes, and this association can be modulated by H2O2, optimizing working efficiency and minimizing H2O2 spillage. This association could represent one part of a postulated pluriprotein complex involved in iodination. This suggests that defects in this association could impair thyroid hormone synthesis and lead to thyroid insufficiency and cell damage.

Peroxidase activity and thyroglobulin iodination activity of thyroid peroxidase in non-functioning thyroid tumours

1988 ◽  
Vol 118 (1) ◽  
pp. 147-153 ◽  
Author(s):  
Hirokatsu Yoshimura ◽  
Kunihiko Ito ◽  
Osamu Tarutani ◽  
Toichiro Hosoya
Keyword(s):  
Peroxidase Activity ◽  
Thyroid Tissue ◽  
Assay Method ◽  
Considerable Proportion ◽  
Thyroid Peroxidase ◽  
Oxidation Activity ◽  
Rapid Assay ◽  
Iodide Transport ◽  
Iodide Oxidation ◽  
Transport Defect

Abstract. Both lesion (L) and adjacent normal (N) thyroid tissue from 48 patients with non-functioning adenomas and adenomatous goitres were assayed for peroxidase activity by the 'mini' assay method employing guaiacol or iodide as the second substrate. A considerable proportion of thyroids (46% of adenomas and 22% of adenomatous goitres) demonstrated no iodide oxidation activity in L although they had guaiacol oxidation activity, and these were grouped as subgroups A. The rest of these non-functioning tumours, termed subgroups B, had both guaiacol and iodide oxidation activity which was higher (3.0–4.6 times in guaiacol assay and 7.3–14.1 times in iodide assay) in L than in N. These data indicate that the non-functioning in subgroups A may be due to a lack of iodide oxidation activity and that some other defects such as an iodide transport defect may be involved in subgroups B. Furthermore, a precise and rapid assay method for thyroglobulin iodination activity of thyroid peroxidase was developed, with modifications of previous methods. On the basis of this method, we found that there is a good correlation (r = 0.94) between iodide oxidation assay and thyroglobulin iodination assay, leading to the conclusion that thyroglobulin iodination assay can be replaced by iodide oxidation assay.

Platelet Hypersensitivity in Acute Malaria (Plasmodium falciparum) Infection in Man

1981 ◽  
Vol 46 (02) ◽  
pp. 547-549 ◽  
Author(s):  
E M Essien ◽  
M I Ebhota
Keyword(s):  
Plasmodium Falciparum ◽  
Malaria Infection ◽  
Light Transmission ◽  
Human Platelet ◽  
Platelet Rich Plasma ◽  
Wave Pattern ◽  
Falciparum Infection ◽  
Secondary Wave ◽  
Control Subjects ◽  
The Mean

SummaryDuring acute malaria infection, platelets in human platelet-rich plasma are hypersensitive to the addition of ADP between 1.0 uM and 5.0 uM, or adrenaline 0.11 uM as aggregating agents. The mean maximum aggregation amplitude (as % of light transmission) obtained from 8 subjects in response to added ADP (1.0 uM), 39.8 ± 27 (1SD), was significantly greater than the value in 6 controls (5.2±6.7 (1SD); t = 3, 51 P <0.005). A similar pattern of response was obtained with higher ADP concentrations (2.4,4.5 or 5.0 uM) in 22 patients and 20 control subjects (89.9±14.9% vs 77.8±16.5% (1SD) t = 2.45, P <0.02). Addition of 4.5 uM ADP to patient PRP usually evoked only a single aggregation wave (fused primary and secondary waves) while the typical primary and secondary wave pattern was usually obtained from controls.Mean plasma B-thromboglobulin (BTG) concentration in 7 patients (208.3 ± 15.6 ng/ml) was significantly higher than the value in 6 control subjects (59.2±15.7 ng/ml; t = 13.44, P <0.002).

Kaolin-Activated Euglobulin Lysis Time (KELT)

1979 ◽  
Author(s):  
H Greig
Keyword(s):  
No Value ◽  
Clinical Assessment ◽  
Fibrinolytic Activity ◽  
Factor Xii ◽  
Plasminogen Activation ◽  
Normal Range ◽  
Control Subjects ◽  
Lysis Time ◽  
Euglobulin Lysis Time ◽  
The Mean

The most commonly used test for clinical assessment of fibrinolytic activity is the Euglobulin Lysis Time (ELT). However the normal range is very wide, the long times are inconvenient and detection of inhibition is impossible. An attempt has been made to utilise the acceleration of the ELT when kaolin is present, to devise a test with shorter times, a narrower normal range, and better precision. The Euglobulin lysis time was carried out by a modification of the method of NILSSON and OLOW, after precipitation of the euglobulin in the absence of kaolin (ELT) and in the presence of 1 mg. kaolin/ml. plasma (KELT). In 14 control subjects the mean, SD, and range for the ELT were 168.6’, 54.6’, 84-290’; the corresponding values for the KELT were 60.3’, 8.3’ and 46-74’. However, it was found that there was no correlation between the ELT value and the corresponding KELT (’r’ = -0.021); on the contrary, the longer the ELT, the greater the shortening produced by kaolin and there is a direct correlation between the ELT and the shortening of the lysis time by kaolin; ’r’ = 0.988. It is concluded that the KELT has no value as a clinical measure of fibrinolytic activity; further, the results suggest that kaolin may remove an inhibitor(s) of plasminogen activation as well as initiating Factor XII - mediated plasminogen activation.

scholarly journals Prevalence of Prediabetes and Type 2 Diabetes Mellitus in Football Players: A Novel Multi Football Clubs Cross Sectional Study

2021 ◽  
Vol 18 (4) ◽  
pp. 1763
Author(s):  
Sultan Ayoub Meo ◽  
Abdulelah Adnan Abukhalaf ◽  
Ali Abdullah Alomar ◽  
Omar Mohammed Alessa ◽  
Omar Yassin Sumaya ◽  
...  
Keyword(s):  
Diabetes Mellitus ◽  
Type 2 Diabetes ◽  
Type 2 Diabetes Mellitus ◽  
Elite Athlete ◽  
Population Based ◽  
Football Players ◽  
Preventive Strategy ◽  
Control Subjects ◽  
The Mean

Sports offer great benefits, improving health and reducing the risk of illnesses. This study’s aim was to investigate the prevalence of prediabetes and type 2 diabetes mellitus in football players compared to population based non-elite athlete control subjects. Initially 1100 male volunteers, (550) football players, and (550) population based non-elite athlete control subjects were interviewed. After socio-demographic and medical history analysis, 756 (378) nonsmoker male football players and (378) nonsmoker male control subjects were recruited. The control subjects were not involved in regular sports activities such as football, volleyball, badminton, cricket, hockey, and swimming. Participants with a known history of anemia, blood diseases, diabetes mellitus, and malignancy were excluded from the study. The mean age of football players was 31.80 ± 5.46 years, Body Mass Index (BMI) was 26.40 ± 2.08 (kg/m2), and the mean age of control subjects was 32.32 ± 4.37 years, and BMI was 26.66 ± 1.87 (kg/m2). The selected football players have been playing football for about 2 h a day, 3 days per week, and so the total mean duration of playing football was 1.08 years. American Diabetes Association (ADA) based criteria on Glycated Hemoglobin (HbA1c) was used to investigate prediabetes and type 2 diabetes mellitus. In football players the prevalence of prediabetes was 30 (7.93%) and type 2 diabetes mellitus (T2DM) was 6 (1.59%) compared to population based matched non-elite athlete control subjects where the prediabetes was 71 (18.78%) and T2DM was 89 (23.54%) (p = 0.001). Among football players there was a 7-fold decrease in T2DM compared to control subjects. Football recreational activities markedly reduce the prevalence of prediabetes and T2DM. The study findings demonstrate the benefits of football and other such sport activities and emphasize the urgent need for promoting football based physical activities as a physiological preventive strategy against the globally growing diabetes epidemic.

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