REVIEW Using video intensification fluorescence microscopy and tetramethylrhodamine (Rho)-labeled 3, 3', 5-triiodo-L-thyronine (T3), the uptake of T3 by cultured mouse fibroblasts was studied. The binding of 3, 3', 5-triiodo-L-thyronine (T3) to GH3 rat pituitary tumor cells was studied at 15 degrees C and was shown to be saturable, reversible, and stereospecific. A fluorescent derivative of the thyroid hormone 3,3'-triiodo-L-thyronine binds to cultured mouse fibroblasts; such binding is saturable. 3,3?,5-Triiodo-L-thyronine Up-regulation of Na,K-ATPase Activity and Cell Surface Expression in Alveolar Epithelial Cells Is Src Kinase- and Phosphoinositide 3-Kinase-dependent.
REFERENCES
[1]
R Horiuchi,; M L Johnson,; M C Willingham,; I Pastan,; S Cheng. Affinity labeling of the plasma membrane 3,3',5-triiodo-L-thyronine receptor in GH3 cells. PNAS. 1982 , 79(18),5527-5531.
[2]
Jianxun Lei,; Cary N. Mariash.; David H. Ingbar. 3,3?,5-Triiodo-L-thyronine Up-regulation of Na,K-ATPase Activity and Cell Surface Expression in Alveolar Epithelial Cells Is Src Kinase- and Phosphoinositide 3-Kinase-dependent . Journal of Biological Chemistry. 2004 , 279 , 47589-47600.
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