In Vivo Effects of Cytokines, Growth Factors, TSH and Antithyroid Drugs on Xenotransplanted Human Thyroid Tissue of Graves’ Disease

Author(s):  
P. M. Schumm-Draeger ◽  
B. O. Boehm ◽  
H. J. C. Wenisch ◽  
K. Schöffling
1986 ◽  
Vol 113 (3) ◽  
pp. 335-339
Author(s):  
S. de Rave ◽  
H. M.J. Goldschmidt ◽  
Y. T.J. Somers-Pijnenburg ◽  
B. Bravenboer ◽  
J. H. M. Lockefeer

Abstract. The central role of Thyroid Stimulating Immunoglobulins (TSI) in the pathogenesis of the hyperthyroidism of Graves' disease has become generally accepted and a wide variety of assays for the detection of these antibodies has been developed. The dependence on the availability of human thyroid tissue makes most of these assays unsuitable for routine clinical use, a problem circumvented by the use of nonhuman thyroid tissue in some TSI assays. We therefore compared porcine and human thyroid tissue in a TSI assay based on in vitro cAMP generation. No major differences in within and between run variation were found and, with some notable exceptions, a reasonable correlation could be demonstrated between the results in both assays (R = 0.89, P < 0.001). However, the sensitivity of the porcine TSI assay is only 60% of the estimated sensitivity of the human TSI assay. In spite of the practical advantages this porcine TSI assay, and possibly also other TSI assays using non-human thyroid tissue, cannot totally replace human TSI assays. The value of these assays in predicting the outcome of medical treatment of Graves' disease remains to be established.


1987 ◽  
Vol 65 (4) ◽  
pp. 197-201 ◽  
Author(s):  
P. -M. Schumm-Draeger ◽  
R. Senekowitsch ◽  
F. -D. Maul ◽  
H. J. C. Wenisch ◽  
C. R. Pickardt ◽  
...  

1976 ◽  
Vol 81 (2) ◽  
pp. 288-297
Author(s):  
Colette Thomas-Morvan

ABSTRACT Stable thyroid hormones (T4 and T3)1) have been demonstrated in pure albumin isolated from normal human thyroid tissue iodinated in vivo. Five samples of albumin were separated from other thyroid proteins by acrylamide gel electrophoresis. After pronase hydrolysis, the content of Thyroid hormones was measured chemically (T4 + T3) as well as by competitive radioactive measurement (T4) and radioimmunoassay (T3). The purity of the albumin and validity of these measurements were confirmed by different techniques. The synthesis of thyroid hormones is not therefore a property unique to Tg and may occur in albumin. However the amount of iodothyronines in the albumin (average 0.004 residue per molecule) is much less than that found in Tg (0.5 residue per molecule). In the albumin as in Tg the number of hormone residues per molecule is proportional to the number of atoms of iodine. At an equivalent iodine concentration, the albumin seems capable of forming the thyroid hormones as well as Tg. The difference between these two proteins, in their capacity to synthesize thyroid hormones, seems to depend on their capacity for iodination. This difference of iodination does not seem to be linked with the number of tyrosyl residues, but might be related to the position of these residues.


Author(s):  
Petra-Maria Schumm-Draeger ◽  
Hans-Peter Fortmeyer ◽  
Hubertus Johannes Christoph Wenisch ◽  
Claudia Müller ◽  
Klaus Henning Usadel

1986 ◽  
Vol 113 (1_Suppl) ◽  
pp. S48-S49
Author(s):  
P.-M. SCHUMM-DRAEGER ◽  
H.J.C. WENISCH ◽  
F.D. MAUL ◽  
C. TIMM

Sign in / Sign up

Export Citation Format

Share Document