Guanyl nucleotide regulatory proteins in neoplastic and normal human thyroid tissue

1988 ◽  
Vol 12 (4) ◽  
pp. 538-544 ◽  
Author(s):  
O. H. Clark ◽  
E. T. Gum ◽  
A. E. Siperstein ◽  
P. L. Gerend
Keyword(s):  
Thyroid Tissue ◽  
Regulatory Proteins ◽  
Human Thyroid ◽  
Human Thyroid Tissue ◽  
Normal Human

Regulation of Cyclic Nucleotide and Prostaglandin Formation in Normal Human Thyroid Tissue and in Autonomous Nodules*

1980 ◽  
Vol 50 (4) ◽  
pp. 776-785 ◽  
Author(s):  
J. VAN SANDE ◽  
J. MOCKEL ◽  
J. M. BOEYNAEMS ◽  
P. DOR ◽  
G. ANDRY ◽  
...  
Keyword(s):  
Cyclic Nucleotide ◽  
Thyroid Tissue ◽  
Human Thyroid ◽  
Human Thyroid Tissue ◽  
Normal Human

IODOTHYRONINE CONTENT OF HUMAN THYROID ALBUMIN

1976 ◽  
Vol 81 (2) ◽  
pp. 288-297
Author(s):  
Colette Thomas-Morvan
Keyword(s):  
Thyroid Hormones ◽  
Gel Electrophoresis ◽  
Thyroid Tissue ◽  
Iodine Concentration ◽  
Human Thyroid ◽  
Human Thyroid Tissue ◽  
Normal Human ◽  
The Difference ◽  
Radioactive Measurement

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.

Vascularization of Normal Human Thyroid Tissue Transplanted to Nude Mice

Pathobiology ◽  
1987 ◽  
Vol 55 (2) ◽  
pp. 104-114
Author(s):  
Johan Mölne ◽  
Erik Jörtsö ◽  
Staffan Smeds ◽  
Lars E. Ericson
Keyword(s):  
Nude Mice ◽  
Thyroid Tissue ◽  
Human Thyroid ◽  
Human Thyroid Tissue ◽  
Normal Human

INHIBITION BY NORMAL IMMUNOGLOBULINS OF THYROTROPHIN-STIMULATED PRODUCTION OF CYCLIC AMP IN SLICES OF NORMAL HUMAN THYROID

1980 ◽  
Vol 87 (2) ◽  
pp. 271-277 ◽  
Author(s):  
S. P. BIDEY ◽  
N. J. MARSHALL ◽  
R. P. EKINS
Keyword(s):  
Cyclic Amp ◽  
Immunoglobulin G ◽  
Thyroid Tissue ◽  
Human Thyroid ◽  
Human Thyroid Tissue ◽  
Thyroid Stimulating Antibodies ◽  
Cyclic Amp Accumulation ◽  
Normal Human ◽  
Stimulation Of

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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