Characterization, by Molecular Cloning, of Smaller Forms of Thyroid Peroxidase Messenger Ribonucleic Acid in Human Thyroid Cells as Alternatively Spliced Transcripts*

1990 ◽  
Vol 71 (2) ◽  
pp. 384-390 ◽  
Author(s):  
YUJI NAGAYAMA ◽  
PUI SETO ◽  
BASIL RAPOPORT
1997 ◽  
Vol 82 (10) ◽  
pp. 3331-3336 ◽  
Author(s):  
Tsukasa Saito ◽  
Toyoshi Endo ◽  
Akio Kawaguchi ◽  
Masato Ikeda ◽  
Minoru Nakazato ◽  
...  

Abstract The Na+/I− symporter (NIS) is important in hormone synthesis in the thyroid gland. NIS activity, as reflected by I− uptake, was increased by TSH (1 mU/mL) or forskolin (10μ mol/L) in primary cultured human thyroid cells. Northern blot analysis revealed that incubation of these cells with TSH or forskolin for 24 h increased the abundance of NIS messenger ribonucleic acid (mRNA) 2.3- and 2.5-fold, respectively. Immunoblot analysis revealed 2.7- and 2.4-fold increases, respectively, in the amount of NIS protein after 48 h, suggesting that elevated levels of intracellular cAMP induced the expression of NIS in human thyrocytes. We then studied the levels of NIS mRNA and protein in Graves’ thyroid tissue and found that the amount of NIS mRNA in thyroid tissue from individuals with Graves’ disease (n = 5) was 3.8 times that in normal thyroid tissue (n = 5). The abundance of NIS mRNA was significantly correlated with that of thyroid peroxidase or thyroglobulin mRNAs, but not with that of TSH receptor mRNA, in the Graves’ and normal thyroid tissue specimens. The amount of NIS protein was also increased 3.1-fold in Graves’ thyroid tissue compared with that in normal thyroid tissue. The increased expression of NIS may thus contribute to the development of Graves’ disease.


Endocrinology ◽  
1989 ◽  
Vol 124 (6) ◽  
pp. 2889-2894 ◽  
Author(s):  
GIUSEPPE DAMANTE ◽  
GREGORIO CHAZENBALK ◽  
DIEGO RUSSO ◽  
BASIL RAPOPORT ◽  
DANIELA FOTI ◽  
...  

1989 ◽  
Vol 3 (3) ◽  
pp. 532-538 ◽  
Author(s):  
Aimee D. Kohn ◽  
John Chan ◽  
Domenico Grieco ◽  
Vera M. Nikodem ◽  
Salvatore M. Aloj ◽  
...  

1987 ◽  
Vol 116 (1_Suppl) ◽  
pp. S57-S62 ◽  
Author(s):  
A. Pinchera ◽  
S. Mariotti ◽  
L. Chiovato ◽  
P. Vitti ◽  
G. Lopez ◽  
...  

Abstract. Evidence has been accumulated that human thyroid microsomal/microvillar autoantigen (M) is expressed both in the cytoplasm and on the surface of thyroid follicular cells. The availability of this autoantigen to the immune system, possibly associated with abnormally expressed HLA-DR antigens may be relevant both to the triggering and to maintenance of thyroid autoimmune reactions. Preliminary biochemical characterization of M suggested that it was a glycoprotein with a mol. wt. of about 100–110 kD. recent studies carried out in our laboratories taking advantage of monoclonal antibodies provided evidence that the structure presently referred as M-Ag is represented by thyroid peroxidase (TPO). The identity between TPO and M is further supported by four-layer immunofluorescence analysis showing a complete overlap of the two antigens both in the surface and in the cytoplasm of thyroid cells and by the observation that the expression of M and TPO is similarly modulated by TSH, possibly through a cAMP-dependent mechanism.


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