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Thyroid hormones and fat cell phosphorylation.

B Omri, J M Gavaret, C Corrèze

Molecular and Cellular Endocrinology

|December 1, 1984

Summary

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Thyroid hormones regulate protein phosphorylation in rat fat cells, impacting lipolytic and lipogenic pathways. Hypothyroidism affects hormonal responses in these cells.

Area of Science:

Biochemistry
Cell Biology
Endocrinology

Background:

Protein phosphorylation is a key regulatory mechanism in cellular signaling.
Thyroid hormones play a crucial role in regulating metabolism.

Purpose of the Study:

To investigate the effect of thyroid status on protein phosphorylation in rat adipocytes.
To determine how thyroid hormones influence basal and stimulated phosphorylation of cytosolic and plasma membrane proteins.

Main Methods:

Isolated rat fat cells from euthyroid and thyroidectomized rats were used.
Phosphorylation was analyzed using sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE) and two-dimensional gel electrophoresis.
Cells were stimulated with isoproterenol or dibutyryl adenosine cyclic monophosphate (dbcAMP).

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Main Results:

Basal phosphorylation of cytosolic and plasma membrane proteins was unaffected by hypothyroidism.
In euthyroid cells, isoproterenol and dbcAMP increased phosphorylation of specific cytosolic proteins and a 26-22 kDa plasma membrane protein.
In hypothyroid cells, dbcAMP stimulated phosphorylation of the 26-22 kDa plasma membrane protein, but isoproterenol did not.

Conclusions:

Thyroid hormones modulate the 32P-labeling of proteins in rat fat cell cytosol and plasma membrane.
Thyroid hormones are essential for the full response of fat cell protein phosphorylation to hormonal stimulation, influencing lipolytic and lipogenic pathways.