The presence of autoantibodies directed to thyroid plasma membrane antigens in sera of patients with thyroid disorders, estimated by the reaction with labelled protein A

1984 ◽  
Vol 105 (4) ◽  
pp. 500-504 ◽  
Author(s):  
Andrzej Gardas ◽  
Barbara Czarnocka ◽  
Janusz Nauman
Keyword(s):  
Plasma Membrane ◽  
Lupus Erythematosus ◽  
Plasma Membranes ◽  
Binding Capacity ◽  
Protein A ◽  
Graves Disease ◽  
Nodular Goitre ◽  
Simple Obesity ◽  
Membrane Antigens ◽  
Toxic Nodular Goitre

Abstract. The presence of antithyroid plasma membrane antibodies (ATMA) has been detected in 97% of patients with untreated hyperthyroid Graves' disease, 85% of methimazole treated hyperthyroid Graves' disease, 25% of Hashimoto's thyroiditis and 6.9% of patients with toxic nodular goitre. The ATMA index was negative in all healthy blood donors, in patients with non-toxic nodular goitre, with the thyrocardiac syndrome and with simple obesity. Studies of patients with non-thyroid autoimmune diseases revealed that ATMA is positive in 11% of patients with scleroderma, 17.6% of systemic lupus erythematosus and 16% of rheumatoid arthritis. The amount of immunoglobulin bound to thyroid plasma membranes after pre-incubation with serum from patients with Graves' disease varied from 4.2 to 25.2 pmoles per mg of membrane protein; these values are several times higher than the maximal binding capacity for thyrotrophin which is 1.28 pmole/mg protein. In the majority of the cases studied TSH did not significantly inhibit IgG bound from thyroid plasma membranes. Significant amounts of IgG were displaced by an excess of TSH only in three cases with untreated hyperthyroid Graves' disease.

Enzyme-linked immunosorbent assay of autoantibodies reacting with thyroid plasma membrane antigens in sera of patients with autoimmune thyroid diseases

1986 ◽  
Vol 113 (2) ◽  
pp. 255-260 ◽  
Author(s):  
Andrzej Gardas ◽  
Kathleen L. Rives
Keyword(s):  
Plasma Membrane ◽  
Immunosorbent Assay ◽  
Lupus Erythematosus ◽  
Antithyroid Drug ◽  
Cross Reactivity ◽  
Enzyme Linked Immunosorbent Assay ◽  
Autoimmune Thyroid Diseases ◽  
Nodular Goitre ◽  
Membrane Antigens ◽  
Toxic Nodular Goitre

Abstract. A sensitive and specific enzyme-linked immunosorbent assay (ELISA) for the detection of autoantibodies reacting with thyroid plasma membrane antigens has been established. Autoantibodies reacting with thyroid plasma membrane antigens were detected by the ELISA in 95% of untreated hyperthyroid Graves', 68% of antithyroid drug-treated Graves' up to four months of the therapy, in 62% of Hashimoto's thyroiditis and in 8.9% of toxic nodular goitre. The ELISA was negative in 100% healthy blood donors, 100% non-toxic nodular goitre, in 12 patients with rheumatoid arthritis, 18 patients with scleroderma and 94% of patients with systemic lupus erythematosus. The mean value of autoantibodies titre was higher in untreated hyperthyroid Graves' (1:84 000) and lowest in positive patients with autoimmune disease of non-thyroid origin (1:4000). The cross-reactivity of antimicrosomal antigen antibodies was below 10%; there was no influence of antithyroglobulin antibodies on the ELISA; and most of the autoantibodies react with plasma membrane antigens different from the TSH binding sites.

Simple and sensitive method for estimation of antithyroid plasma membrane antibodies in the serum of patients with autoimmune thyroid diseases; comparison with other assays

1984 ◽  
Vol 105 (4) ◽  
pp. 492-499 ◽  
Author(s):  
Andrzej Gardas ◽  
Barbara Czarnocka ◽  
Marta Faryna ◽  
Grazyna Adler ◽  
Alexandra Lewartowska ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Plasma Membranes ◽  
Blood Donors ◽  
Protein A ◽  
Mean Value ◽  
Adenyl Cyclase ◽  
Graves Disease ◽  
Autoimmune Thyroid Diseases ◽  
Autoimmune Thyroid ◽  
Index Estimation

Abstract. The ability of protein A from Staphylococcus aureus to interact with Fc fragments of IgG was used to estimate the antithyroid plasma membrane antibodies in sera of patients with Graves' disease. The results were expressed as an antithyroid plasma membrane antibodies (ATMA) index. The ATMA index estimated in 60 healthy blood donors varied from 0.57 to 1.28, with a mean value of 0.99, sd Ø 0.20. The ATMA index in hyperthyroid untreated Graves' disease varied from 1.80 to 8.0, with a mean value of 4.7. Autoantibody binding to thyroid plasma membranes could be inhibited by (Fab)2 fragments obtained from the serum of patients with Graves' disease but not by (Fab)2 fragments obtained from the serum of healthy blood donors. The influence of rabbit antithyroglobulin and antimicrosomal antibodies on the ATMA index estimation has been evaluated. The ATMA index estimation was compared with the thyrotrophin binding inhibiting immunoglobulins (TBII) index and with the adenyl cyclase stimulating activity of immunoglobulins obtained from 92 hyperthyroid Graves' patients. The ATMA index was positive in 97%, the TBII index in 62% and TSI in 35% of cases. This method using protein A could also be used for estimation of ATMA in other autoimmune thyroid disorders.

FURTHER STUDIES ON THE RATE OF DISAPPEARANCE OF LABELLED THYROXINE FROM THE INTRAVASCULAR COMPARTMENT OF MAN, WITH REFERENCE TO THE ROLE OF THYROXINE BINDING PROTEINS

1967 ◽  
Vol 55 (3) ◽  
pp. 497-521 ◽  
Author(s):  
Brian R. Webster ◽  
Amy Britton ◽  
Robert Volpé ◽  
Calvin Ezrin
Keyword(s):  
Binding Sites ◽  
Radioactive Iodine ◽  
Binding Capacity ◽  
Normal Subjects ◽  
Graves Disease ◽  
List Type ◽  
Half Time ◽  
Nodular Goitre ◽  
Toxic Nodular Goitre

ABSTRACT The disappearance of an intravenously injected tracer dose of 131I-labelled L-thyroxine from the circulation has been followed for 70 minutes. We have confirmed that the most significant separation between euthyroid subjects and patients with hyperthyroidism or myxoedema is given by the single exponential slope of the regression of blood radioactivity occurring between 20 and 50 minutes after T4* injection. This slope is referred to as the acute T4* half-time. When there is no alteration in total TBG the acute T4* half-time is closely related to the plasma BEI concentration. Increase in the latter due to Graves' disease, toxic nodular goitre, or exogenous administration of thyroxine or desiccated thyroid, results in a comparable acceleration in the acute T4* half-time compared to the value in euthyroid control subjects. Conversely patients with a low BEI due to primary or radioactive iodine induced myxoedema all have a significantly slow acute T4* half-time compared to normal subjects. There was no specific abnormality in the handling of thyroxine by patients with Graves' disease in contrast to the earlier findings of Lennon et al. (1961). Hypermetabolism per se does not affect the acute T4* half-time. The administration of pharmacological doses of triiodothyronine, unlike similar doses of thyroxine, failed to affect the acute T4* half-time. The acute T4* half-time is consistently related in an inverse manner to the concentration of unsaturated thyroxine-binding sites in association with TBG. These data show no such correlation between TBPA binding and the acute T4 half-time. Synthetic oestrogen, by increasing the unsaturated thyroxine-binding capacity of TBG, produces a profound slowing of the acute T4* halftime.

Agonist-induced internalisation of the angiotensin II-binding sites from plasma membranes of isolated rat hepatocytes

1997 ◽  
Vol 152 (3) ◽  
pp. 407-412 ◽  
Author(s):  
M Montiel ◽  
M C Caro ◽  
E Jiménez
Keyword(s):  
Plasma Membrane ◽  
Angiotensin Ii ◽  
Binding Sites ◽  
Plasma Membranes ◽  
Binding Capacity ◽  
Rat Hepatocytes ◽  
Receptor Complex ◽  
Ang Ii ◽  
Isolated Rat Hepatocytes ◽  
Isolated Rat

Angiotensin II (Ang II) provokes rapid internalisation of its receptor from plasma membranes in isolated rat hepatocytes. After 10 min stimulation with Ang II, plasma membrane lost about 60% of its 125I-Ang II-binding capacity. Internalisation was blocked by phenylarsine oxide (PhAsO), whereas okadaic acid, which markedly reduced the sustained phase of calcium mobilization, did not have a preventive effect on Ang II–receptor complex sequestration. These data suggest that Ang II receptor internalisation is probably independent of a phosphorylation/dephosphorylation cycle of critical serine/threonine residues in the receptor molecule. To establish a relationship between sequestration of the Ang II receptor and the physical properties of the Ang II-binding sites, 125I-Ang II–receptor complex profiles were analysed by isoelectric focusing. In plasma membrane preparations two predominant Ang II-binding sites, migrating to pI 6·8 and 6·5 were found. After exposure to Ang II, cells lost 125I-Ang II-binding capacity to the Ang II–receptor complex migrating at pI 6·8 which was prevented in PhAsO-treated cells. Pretreatment of hepatocytes with okadaic acid did not modify Ang II–receptor complex profiles, indicating that the binding sites corresponding to pI 6·5 and pI 6·8 do not represent a phosphorylated and/or non-phosphorylated form of the Ang II receptor. The results show that the Ang II–receptor complex isoform at pI 6·8 represents a functional form of the type-1 Ang II receptor. Further studies are necessary to identify the Ang II-related nature of the binding sites corresponding to pI 6·5. Journal of Endocrinology (1997) 152, 407–412

scholarly journals Integrin-associated protein: a 50-kD plasma membrane antigen physically and functionally associated with integrins.

1990 ◽  
Vol 111 (6) ◽  
pp. 2785-2794 ◽  
Author(s):  
E Brown ◽  
L Hooper ◽  
T Ho ◽  
H Gresham
Keyword(s):  
Signal Transduction ◽  
Plasma Membrane ◽  
Synthetic Peptides ◽  
Plasma Membranes ◽  
Protein A ◽  
Hematopoietic Cells ◽  
Cell Types ◽  
Cell Biol ◽  
Leukocyte Response ◽  
Stimulation Of

Phagocytosis by monocytes or neutrophils can be enhanced by interaction with several proteins or synthetic peptides containing the Arg-Gly-Asp sequence. Recently we showed that an mAb, B6H12, specifically inhibited this enhancement of neutrophil phagocytosis by inhibiting Arg-Gly-Asp binding to the leukocyte response integrin (Gresham, H. D., J. L. Goodwin, P. M. Allen, D. C. Anderson, and E. J. Brown. 1989. J. Cell Biol. 108:1935-1943). Now, we have purified the antigen recognized by B6H12 to homogeneity. Surprisingly, it is a 50-kD molecule that is expressed on the plasma membranes of all hematopoietic cells, including erythrocytes, which express no known integrins. On platelets and placenta, but not on erythrocytes, this protein is associated with an integrin that can be recognized by an anti-beta 3 antibody. In addition, both the anti-beta 3 and several mAbs recognizing the 50-kD protein inhibit Arg-Gly-Asp stimulation of phagocytosis. These data demonstrate an association between integrins and the 50-kD protein on several cell types. For this reason, we call it Integrin-associated Protein (IAP). We hypothesize that IAP may play a role in signal transduction for enhanced phagocytosis by Arg-Gly-Asp ligands.

scholarly journals The influence of non-radioactive iodine (127I) on the outcome of radioiodine (131I) therapy in patients with Graves’ disease and toxic nodular goitre

2011 ◽  
Vol 14 (1) ◽  
pp. 9-15 ◽  
Author(s):  
Franciszek Rogowski ◽  
Saeid Abdelrazek ◽  
Piotr Szumowski ◽  
Anna Zonenberg ◽  
Adam Parfienczyk ◽  
...  
Keyword(s):  
Radioactive Iodine ◽  
131I Therapy ◽  
Graves Disease ◽  
Nodular Goitre ◽  
Toxic Nodular Goitre

Antithyroid drugs as a factor influencing the outcome of radioiodine therapy in Graves' disease and toxic nodular goitre?

2001 ◽  
Vol 28 (9) ◽  
pp. 1360-1364 ◽  
Author(s):  
C. Körber ◽  
P. Schneider ◽  
N. Körber-Hafner ◽  
H. Hänscheid ◽  
C. Reiners
Keyword(s):  
Radioiodine Therapy ◽  
Antithyroid Drugs ◽  
Graves Disease ◽  
Nodular Goitre ◽  
Toxic Nodular Goitre

D-Glucose uptake and insulin binding by the human adipose cell plasma membrane as a function of its polypeptide composition

1977 ◽  
Vol 55 (2) ◽  
pp. 126-133 ◽  
Author(s):  
Bluma G. Brenner ◽  
Shiro Ozaki ◽  
Norman Kalant ◽  
Arthur Kahlenberg
Keyword(s):  
Plasma Membrane ◽  
Glucose Uptake ◽  
Plasma Membranes ◽  
Binding Capacity ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Insulin Binding ◽  
Partial Purification ◽  
Scatchard Analysis ◽  
Molecular Weight Range

A preparation of plasma membranes isolated from human omental lipocytes is composed of about 15 major polypeptide components including three major glycoproteins with an apparent molecular weight range from 100 000 to 23 000, as determined by sodium dodecyl sulfate – polyacrylamide gel electrophoresis. Extraction of this membrane preparation with sodium iodide or 2,3-dimethylmaleic anhydride solubilized 50 and 70% of the membrane protein, respectively, resulting from the extensive extraction of protein from all but two of the major membrane polypeptide components. This removal of protein did not affect the membrane's stereospecific D-glucose-uptake activity but did reduce its total specific [l25I]insulin-binding activity by 46–67%. The binding of [125I]insulin to its specific receptor on lipocyte plasma membranes was detected at physiologic concentrations of the hormone and could be competitively displaced by increasing concentrations of native insulin. The kinetic behaviour of this reaction was approximated by Scatchard analysis, and both the affinity and binding capacity of the plasma membrane for insulin were increased at lower temperatures.These results suggest that D-glucose transport in human adipose tissue is mediated by an intrinsic component of the hydrophobic structure of the lipocyte plasma membrane, and represent a partial purification of this component. In addition, these studies demonstrate and characterize the binding of insulin to the plasma membrane isolated from human lipocytes. A quantitative study of this binding reaction may provide further understanding of the mechanisms underlying the decreased insulin responsiveness characteristic of human diabetes.

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