Effect of lithium on thyrotropin-stimulated adenylate cyclase activity in the human thyroid

1989 ◽  
Vol 17 (1) ◽  
pp. 87-87
Author(s):  
MICHAEL S. WRAGG ◽  
SHEILA MACNEIL
Keyword(s):  
Adenylate Cyclase ◽  
Cyclase Activity ◽  
Adenylate Cyclase Activity ◽  
Human Thyroid

Epidermal growth factor receptors and adenylate cyclase activity in human thyroid tissues

1990 ◽  
Vol 14 (3) ◽  
pp. 410-417 ◽  
Author(s):  
Quan-Yang Duh ◽  
Allan E. Siperstein ◽  
Rebecca A. Miller ◽  
Joan J. Sancho ◽  
Michael J. Demeure ◽  
...  
Keyword(s):  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Adenylate Cyclase ◽  
Growth Factor Receptors ◽  
Cyclase Activity ◽  
Adenylate Cyclase Activity ◽  
Human Thyroid ◽  
Epidermal Growth Factor Receptors ◽  
Epidermal Growth

scholarly journals Calcium and calmodulin in the regulation of human thyroid adenylate cyclase activity

1985 ◽  
Vol 225 (3) ◽  
pp. 581-589 ◽  
Author(s):  
T Lakey ◽  
S Mac Neil ◽  
H Humphries ◽  
S W Walker ◽  
D S Munro ◽  
...  
Keyword(s):  
Adenylate Cyclase ◽  
Metal Ion ◽  
Cyclase Activity ◽  
Adenylate Cyclase Activity ◽  
Human Thyroid ◽  
Dependent Manner ◽  
Biphasic Response ◽  
Thyroid Stimulating Immunoglobulins ◽  
Wide Range ◽  
Dose Dependent

TSH (thyrotropin)-stimulated human thyroid adenylate cyclase has a biphasic response to Ca2+, being activated by submicromolar Ca2+ (optimum 22nM), with inhibition at higher concentrations. Calmodulin antagonists caused an inhibition of TSH-stimulated adenylate cyclase in a dose-dependent manner. Inhibition of TSH-and TSIg-(thyroid-stimulating immunoglobulins)-stimulated activity was more marked than that of basal, NaF- or forskolin-stimulated activity. This inhibition was not due to a decreased binding of TSH to its receptor. Addition of pure calmodulin to particulate preparations of human non-toxic goitre which had not been calmodulin-depleted had no effect on adenylate cyclase activity. EGTA was ineffective in removing calmodulin from particulate preparations, but treatment with the tervalent metal ion La3+ resulted in a loss of up to 98% of calmodulin activity from these preparations. Addition of La3+ directly to the adenylate cyclase assay resulted in a partial inhibition of TSH- and NaF-stimulated activity, with 50% inhibition produced by 5.1 microM and 4.0 microM-La3+ respectively. Particulate preparations with La3+ showed a decrease of TSH- and NaF-stimulated adenylate cyclase activity (approx. 40-60%). In La3+-treated preparations there was a decrease in sensitivity of TSH-stimulated adenylate cyclase to Ca2+ over a wide range of Ca2+ concentrations, but most markedly in the region of the optimal stimulatory Ca2+ concentration. In particulate preparations from which endogenous calmodulin had been removed by La3+ treatment, the addition of pure calmodulin caused an increase (73 +/- 22%; mean +/- S.E.M., n = 8) in TSH-stimulated thyroid adenylate cyclase activity. This was seen in 8 out of 13 experiments.

Human Thyroid Cancer: Membrane Thyrotropin Binding and Adenylate Cyclase Activity

1980 ◽  
Vol 51 (4) ◽  
pp. 915-920 ◽  
Author(s):  
PIERRE CARAYON ◽  
COLETTE THOMAS-MORVAN ◽  
ELIAS CASTANAS ◽  
MAURICE TUBIANA
Keyword(s):  
Thyroid Cancer ◽  
Adenylate Cyclase ◽  
Cyclase Activity ◽  
Adenylate Cyclase Activity ◽  
Human Thyroid

Inhibition of adenylate cyclase activity of human thyroid membranes by gangliosides

1984 ◽  
Vol 770 (2) ◽  
pp. 142-147 ◽  
Author(s):  
G Dacremont ◽  
M De Baets ◽  
J.M Kaufman ◽  
A Elewaut ◽  
A Vermeulen
Keyword(s):  
Adenylate Cyclase ◽  
Cyclase Activity ◽  
Adenylate Cyclase Activity ◽  
Human Thyroid

Prostacyclin Stimulation of Adenylate Cyclase Activity in Human Thyroid Membranes

1986 ◽  
Vol 18 (09) ◽  
pp. 625-629 ◽  
Author(s):  
K. Kasai ◽  
M. Hiraiwa ◽  
Y. Suzuki ◽  
N. Banba ◽  
T. Emoto ◽  
...  
Keyword(s):  
Adenylate Cyclase ◽  
Cyclase Activity ◽  
Adenylate Cyclase Activity ◽  
Human Thyroid ◽  
Stimulation Of

EFFECTS OF HUMAN THYROID-STIMULATING HORMONE AND IMMUNOGLOBULINS ON ADENYLATE CYCLASE ACTIVITY AND THE ACCUMULATION OF CYCLIC AMP IN HUMAN THYROID MEMBRANES AND SLICES

1978 ◽  
Vol 79 (1) ◽  
pp. 121-130 ◽  
Author(s):  
S. D. HOLMES ◽  
SUSAN M. DIRMIKIS ◽  
T. J. MARTIN ◽  
D. S. MUNRO
Keyword(s):  
Cyclic Amp ◽  
Adenylate Cyclase ◽  
Thyroid Stimulating Hormone ◽  
Cyclase Activity ◽  
Adenylate Cyclase Activity ◽  
Maximum Response ◽  
Human Thyroid ◽  
Tissue Slices ◽  
Long Acting ◽  
Stimulating Hormone

The activation of adenylate cyclase and the accumulation of cyclic AMP resulting from the action of human thyroid-stimulating hormone (TSH), long-acting thyroid stimulator (LATS) or LATS-protector (LATS-P) have been investigated in preparations of human thyroid membranes and slices. Human TSH significantly increased adenylate cyclase activity in membranes from non-toxic goitres whereas LATS and LATS-P had no consistent effect. However, pre-incubation of goitrous membranes with LATS–immunoglobulin G inhibited the effect of TSH on adenylate cyclase. When thyroid membranes were prepared from the glands of patients with Graves's disease neither TSH nor thyroid-stimulating immunoglobulins (TSIg) stimulated adenylate cyclase significantly. Whether from non-toxic goitres or thyrotoxic tissue, the concentration of TSH needed to induce half of the maximum response was lower in thyroid slices than in membranes. Both LATS and LATS-P significantly stimulated the accumulation of cyclic AMP in slices of goitrous tissue but thyrotoxic tissue slices did not respond. In goitrous slices, submaximum concentrations of TSH and TSIg caused additive responses in the accumulation of cyclic AMP but TSIg did not increase the maximum response to TSH.

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