scholarly journals The Mechanism of the Calorigenic Action of Thyroid Hormone

1971 ◽  
Vol 57 (6) ◽  
pp. 710-722 ◽  
Author(s):  
Faramarz Ismail-Beigi ◽  
Isidore S. Edelman
Keyword(s):  
Plasma Membrane ◽  
Oxygen Consumption ◽  
Thyroid Hormone ◽  
Thyroid Hormones ◽  
Atpase Activity ◽  
Energy Utilization ◽  
Total Oxygen ◽  
Liver Plasma Membrane ◽  
Hormone Stimulation ◽  
Stimulation Of

In an earlier study, we proposed that thyroid hormone stimulation of energy utilization by the Na+ pump mediates the calorigenic response. In this study, the effects of triiodothyronine (T3) on total oxygen consumption (QOO2), the ouabain-sensitive oxygen consumption [QOO2(t)], and NaK-ATPase in liver, kidney, and cerebrum were measured. In liver, ∼90% of the increase in QOO2 produced by T3 in either thyroidectomized or euthyroid rats was attributable to the increase in QOO2(t). In kidney, the increase in QOO2(t) accounted for 29% of the increase in QOO2 in thyroidectomized and 46% of the increase in QOO2 in euthyroid rats. There was no demonstrable effect of T3 in euthyroid rats on QOO2 or QOO2(t) of cerebral slices. The effects of T3 on NaK-ATPase activity in homogenates were as follows: In liver +81% from euthyroid rats and +54% from hypothyroid rats. In kidney, +21% from euthyroid rats and +69% from hypothyroid rats. T3 in euthyroid rats produced no significant changes in NaK-ATPase or Mg-ATPase activity of cerebral homogenates. Liver plasma membrane fractions showed a 69% increase in NaK-ATPase and no significant changes in either Mg-ATPase or 5'-nucleotidase activities after T3 injection. These results indicate that thyroid hormones stimulate NaK-ATPase activity differentially. This effect may account, at least in part, for the calorigenic effects of these hormones.

Studies on the mechanism of thyroid hormone stimulation of human red cell Ca2+-ATPase activity

Life Sciences ◽  
1982 ◽  
Vol 30 (7-8) ◽  
pp. 675-682 ◽  
Author(s):  
Paul J. Davis ◽  
Faith B. Davis ◽  
Susan D. Blas
Keyword(s):  
Thyroid Hormone ◽  
Atpase Activity ◽  
Red Cell ◽  
Hormone Stimulation ◽  
Stimulation Of

scholarly journals Calcitonin gene-related peptide receptor antagonist human CGRP-(8-37)

1989 ◽  
Vol 256 (2) ◽  
pp. E331-E335 ◽  
Author(s):  
T. Chiba ◽  
A. Yamaguchi ◽  
T. Yamatani ◽  
A. Nakamura ◽  
T. Morishita ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Adenylate Cyclase ◽  
Calcitonin Gene Related Peptide ◽  
Human Calcitonin ◽  
Liver Plasma Membrane ◽  
Related Peptide ◽  
Calcitonin Gene ◽  
Liver Membranes ◽  
Calcitonin Receptors ◽  
Stimulation Of

From this study, we predicted that the human calcitonin gene-related peptide (hCGRP) fragment hCGRP-(8-37) would be a selective antagonist for CGRP receptors but an agonist for calcitonin (CT) receptors. In rat liver plasma membrane, where CGRP receptors predominate and CT appears to act through these receptors, hCGRP-(8-37) dose dependently displaced 125I-[Tyr0]rat CGRP binding. However, hCGRP-(8-37) had no effect on adenylate cyclase activity in liver plasma membrane. Furthermore, hCGRP-(8-37) inhibited adenylate cyclase activation induced not only by hCGRP but also by hCT. On the other hand, in LLC-PK1 cells, where calcitonin receptors are abundant and CGRP appears to act via these receptors, the bindings of 125I-[Tyr0]rat CGRP and 125I-hCT were both inhibited by hCGRP-(8-37). In contrast to liver membranes, interaction of hCGRP-(8-37) with these receptors led to stimulation of adenosine 3',5'-cyclic monophosphate (cAMP) production in LLC-PK1 cells, and moreover, this fragment did not inhibit the increased production of cAMP induced not only by hCT but also by hCGRP. Thus hCGRP-(8-37) appears to be a useful tool for determining whether the action of CGRP as well as that of CT is mediated via specific CGRP receptors or CT receptors.

scholarly journals Inhibition by Thyroid Hormones of Cell Migration Activated by IGF-1 and MCP-1 in THP-1 Monocytes: Focus on Signal Transduction Events Proximal to Integrin αvβ3

2021 ◽  
Vol 9 ◽  
Author(s):  
Elena Candelotti ◽  
Roberto De Luca ◽  
Roberto Megna ◽  
Mariangela Maiolo ◽  
Paolo De Vito ◽  
...  
Keyword(s):  
Cell Proliferation ◽  
Plasma Membrane ◽  
Cell Migration ◽  
Thyroid Hormone ◽  
Thyroid Hormones ◽  
Integrin Αvβ3 ◽  
Membrane Receptor ◽  
Αvβ3 Integrin ◽  
Plasma Membrane Receptor ◽  
Cell Migration And Proliferation

Interaction between thyroid hormones and the immune system is reported in the literature. Thyroid hormones, thyroxine, T4, but also T3, act non-genomically through mechanisms that involve a plasma membrane receptor αvβ3 integrin, a co-receptor for insulin-like growth factor-1 (IGF-1). Previous data from our laboratory show a crosstalk between thyroid hormones and IGF-1 because thyroid hormones inhibit the IGF-1-stimulated glucose uptake and cell proliferation in L-6 myoblasts, and the effects are mediated by integrin αvβ3. IGF-1 also behaves as a chemokine, being an important factor for tissue regeneration after damage. In the present study, using THP-1 human leukemic monocytes, expressing αvβ3 integrin in their cell membrane, we focused on the crosstalk between thyroid hormones and either IGF-1 or monocyte chemoattractant protein-1 (MCP-1), studying cell migration and proliferation stimulated by the two chemokines, and the role of αvβ3 integrin, using inhibitors of αvβ3 integrin and downstream pathways. Our results show that IGF-1 is a potent chemoattractant in THP-1 monocytes, stimulating cell migration, and thyroid hormone inhibits the effect through αvβ3 integrin. Thyroid hormone also inhibits IGF-1-stimulated cell proliferation through αvβ3 integrin, an example of a crosstalk between genomic and non-genomic effects. We also studied the effects of thyroid hormone on cell migration and proliferation induced by MCP-1, together with the pathways involved, by a pharmacological approach and docking simulation. Our findings show a different downstream signaling for IGF-1 and MCP-1 in THP-1 monocytes mediated by the plasma membrane receptor of thyroid hormones, integrin αvβ3.

scholarly journals The effect of thyroid hormone on the high affinity Ca2+-ATPase in rat liver plasma membrane.

1984 ◽  
Vol 31 (2) ◽  
pp. 141-149 ◽  
Author(s):  
KAZUTAKA HARAGUCHI ◽  
KIYOSHI HASHIZUME ◽  
KAZUO ICHIKAWA ◽  
MUTSUHIRO KOBAYASHI
Keyword(s):  
Plasma Membrane ◽  
Thyroid Hormone ◽  
Rat Liver ◽  
Liver Plasma Membrane ◽  
High Affinity

Phosphorylation of liver plasma membrane-bound calmodulin

1988 ◽  
Vol 66 (8) ◽  
pp. 922-927 ◽  
Author(s):  
Shobha Ghosh ◽  
Jon G. Church ◽  
Basil D. Roufogalis ◽  
Antonio Villalobo
Keyword(s):  
Plasma Membrane ◽  
Calcium Ion ◽  
Polyacrylamide Gel Electrophoresis ◽  
Protein Band ◽  
Bovine Brain ◽  
Antibody Treatment ◽  
Liver Plasma Membrane ◽  
Phosphate Donor ◽  
Membrane Bound ◽  
Stimulation Of

In highly purified rat liver plasma membrane preparations, membrane-bound calmodulin was phosphorylated by a membrane-bound protein kinase using [γ-32P] ATP as phosphate donor. Maximum phosphorylation of calmodulin occurred in the absence of calcium ion, but was significantly decreased in its presence. Plasma membrane-bound calmodulin was identified by the following criteria: (i) extraction from the membrane by EGTA, (ii) stimulation of the activity of the Ca2+-calmodulin-dependent enzyme, (3′:5′ AMP)-phosphodiesterase, by the EGTA extract, and (iii) electrophoretic comigration of EGTA-extracted protein with standard bovine brain calmodulin, both in the presence and the absence of Ca2+. Phosphorylation of the plasma membrane-bound calmodulin was shown by electrophoretic comigration of the 32P-labelled molecule with bovine brain calmodulin, the absence of phosphorylation of this protein band in calmodulin-depleted membranes, and a Western blot of the phosphorylated band using a calmodulin antibody. Treatment of plasma membrane preparations with sheep anticalmodulin serum prevented the phosphorylation of the calmodulin band. Phosphocalmodulin, which could be partially extracted from the membrane by EGTA, comigrated with bovine brain calmodulin in polyacrylamide gel electrophoresis.

Prolactin and Growth Hormone Stimulation of Lactation in Mice Requires Thyroid Hormones

1999 ◽  
Vol 221 (4) ◽  
pp. 345-351 ◽  
Author(s):  
A. V. Capuco ◽  
S. Kahl ◽  
L. J. W. Jack ◽  
J. O. Bishop ◽  
H. Wallace
Keyword(s):  
Growth Hormone ◽  
Thyroid Hormones ◽  
Hormone Stimulation ◽  
Stimulation Of

Adrenal hormones and oxidative metabolism of the garden lizard (Calotes versicolor)

1983 ◽  
Vol 99 (2) ◽  
pp. 211-216 ◽  
Author(s):  
B. B. Pd. Gupta ◽  
J. P. Thapliyal
Keyword(s):  
Oxygen Consumption ◽  
Thyroid Hormones ◽  
Oxidative Metabolism ◽  
Whole Body ◽  
Endocrine Glands ◽  
Adrenal Hormones ◽  
Calotes Versicolor ◽  
Specific Tissue ◽  
Almost All ◽  
Stimulation Of

Daily administration of adrenaline over a 10-day period invariably induced significant increases in the metabolic rate of the whole body and of specific tissue (liver, muscle, kidney and brain) of both intact and thyroidectomized lizards except during June (breeding season) when the presence of thyroid hormones was a prerequisite for the stimulation of oxygen consumption by the whole body, muscle, kidney and brain but not by the liver. Corticosterone had no effect on whole body oxygen consumption but stimulated, inhibited or was without influence on the oxygen consumption of individual tissues, depending on the season and the presence or absence of thyroid hormones. It is suggested that adrenaline, due to its temperature-independent calorigenic effect, acts as the emergency hormone for energy release and helps the animal to survive during hibernation (winter months) when almost all the endocrine glands are inactive.

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