Retinole acid inhibits human thyroid peroxidase and thyroglobulin gene expression in cultured human thyrocytes

1993 ◽  
Vol 16 (2) ◽  
pp. 87-93 ◽  
Author(s):  
H. Namba ◽  
S. Yamashita ◽  
S. Morita ◽  
M. C. Villadolid ◽  
H. Kimura ◽  
...  
Keyword(s):  
Gene Expression ◽  
Human Thyroid ◽  
Thyroid Peroxidase ◽  
Human Thyroid Peroxidase ◽  
Thyroglobulin Gene

Inhibition of human thyroid peroxidase gene expression by interleukin 1

1989 ◽  
Vol 121 (4) ◽  
pp. 465-469 ◽  
Author(s):  
Kiyoto Ashizawa ◽  
Shunichi Yamashita ◽  
Tamami Tobinaga ◽  
Yuji Nagayama ◽  
Hironori Kimura ◽  
...  
Keyword(s):  
Gene Expression ◽  
Interleukin 1 ◽  
Mrna Level ◽  
Inhibitory Effect ◽  
Human Thyroid ◽  
Thyroid Peroxidase ◽  
Hormone Synthesis ◽  
Peroxidase Gene ◽  
Camp Analogue ◽  
Human Thyroid Peroxidase

Abstract. We have already demonstrated the inhibitory effect of interleukin 1 on thyroglobulin gene expression. Recent availability of thyroid peroxidase cDNA has allowed us to investigate the regulation of thyroid peroxidase gene. Therefore, the regulation of thyroid peroxidase mRNA by interleukin 1 in cultured human thyrocytes was investigated. Thyrocytes dispersed from thyroid tissues from patients with Graves' disease were incubated with TSH with or withtout recombinant human interleukin 1. Unstimulated human thyrocytes did not contain any detectable thyroid peroxidase mRNA, however, TSH-stimulated thyrocytes expressed four thyroid peroxidase mRNA transcripts (4.0, 3.2, 2.1 and 1.7 kb, respectively). Both interleukin 1 α and β inhibited TSH-induced thyroid peroxidase mRNA in a dose responsive manner; 103 U/l interleukin l caused maximal suppression of TSH-induced thyroid peroxidase mRNA level to nearly basal levels. Interleukin l also inhibited cAMP analogue 8-bromo-cyclic AMP induced thyroid peroxidase mRNA level. In contrast the γ-actin mRNA hybridization signal was not altered in control or treated cells. These results demonstrate that interleukin 1 directly inhibits TSH-induced thyroid peroxidase gene expression and provide further evidence for a paracrine role of interleukin 1 as a local inhibitor of thyroid hormone synthesis.

Interleukin 6 inhibits human thyroid peroxidase gene expression

1991 ◽  
Vol 124 (3) ◽  
pp. 290-294 ◽  
Author(s):  
Tan Tominaga ◽  
Shunichi Yamashita ◽  
Yuji Nagayama ◽  
Shigeki Morita ◽  
Naokata Yokoyama ◽  
...  
Keyword(s):  
Gene Expression ◽  
Interleukin 6 ◽  
Interleukin 1 ◽  
Hormone Secretion ◽  
Interferon Γ ◽  
Human Thyroid ◽  
Thyroid Peroxidase ◽  
Dependent Manner ◽  
Human Thyroid Peroxidase ◽  
Dose Dependent

Abstract. It has been reported that cytokines, especially interleukin 1 and interferon-γ, inhibit the thyroid hormone secretion and the gene expression of human thyroid peroxidase and thyroglobulin. Interleukin 6 has recently been found to be an important cytokine for the regulation of immunoendocrine interaction and intrathyroidal production of interleukin 6 has been reported. Therefore, we investigated the regulation of thyroid hormone secretion and thyroid peroxidase messenger RNA by interleukin 6 in human thyrocytes to clarify further the functional role of interleukin 6 in thyroid glands. Thyrocytes dispersed from Graves' thyroid tissues were incubated with TSH with or without interleukin 6. TSH (5 U/l stimulated the expression of thyroid peroxidase mRNA transcripts (4.0, 3.2, 2.1, and 1.7 kb, respectively), although unstimulated thyrocytes contained the low level of 3.2 kb thyroid peroxidase mRNA transcript. Interleukin 6 (104-105 U/l) inhibited TSH-induced thyroid peroxidase mRNA in a dose-dependent manner, although the basal level of thyroid peroxidase mRNA expression was not suppressed by interleukin 6. Interleukin 6 also inhibited 8-bromo-cyclic adenosine monophosphate-induced thyroid peroxidase mRNA levels. In contrast, the γ-action mRNA hybridization signal was not altered in control or treated cells. Subsequently, interleukin 6 inhibited TSH-induced T3 secretion in a dose-dependent manner after 72 h treatment. However, interleukin 6 did not affect DNA synthesis. Pretreatment with specific antibody against interleukin 6 selectively restored the inhibitory effect of interleukin 6 on thyroid peroxidase gene expression. Our results suggest that interleukin 6 plays an inhibitory role in the thyroid gland, in addition to interleukin 1 and interferon γ.

Regulation of Thyroid Peroxidase and Thyroglobulin Gene Expression by Thyrotropin in Cultured Human Thyroid Cells

1989 ◽  
Vol 68 (6) ◽  
pp. 1155-1159 ◽  
Author(s):  
YUJI NAGAYAMA ◽  
SHUNICHI YAMASHITA ◽  
HIDESHI HIRAYU ◽  
MOTOMORI IZUMI ◽  
TATSURO UGA ◽  
...  
Keyword(s):  
Gene Expression ◽  
Human Thyroid ◽  
Thyroid Peroxidase ◽  
Thyroid Cells ◽  
Thyroglobulin Gene

An Analysis of the Structure and Antigenicity of Different Forms of Human Thyroid Peroxidase

Thyroid ◽  
1994 ◽  
Vol 4 (2) ◽  
pp. 173-178 ◽  
Author(s):  
JAMES R. BAKER ◽  
PATRICIA ARSCOTT ◽  
JENNIFER JOHNSON
Keyword(s):  
Human Thyroid ◽  
Thyroid Peroxidase ◽  
Human Thyroid Peroxidase

scholarly journals Mutation screening of the thyroid peroxidase gene in a cohort of 55 Portuguese patients with congenital hypothyroidism

2005 ◽  
Vol 152 (2) ◽  
pp. 193-198 ◽  
Author(s):  
Carina Rodrigues ◽  
Paula Jorge ◽  
José Pires Soares ◽  
Isaura Santos ◽  
Regina Salomão ◽  
...  
Keyword(s):  
Congenital Hypothyroidism ◽  
Mutation Screening ◽  
Gene Mutations ◽  
Human Thyroid ◽  
Thyroid Peroxidase ◽  
Molecular Testing ◽  
Missense Mutations ◽  
Human Thyroid Peroxidase ◽  
Iodide Organification Defect ◽  
Organification Defect

Objective: Defects in the human thyroid peroxidase (TPO) gene are reported to be one of the causes of congenital hypothyroidism (CH) due to a total iodide organification defect. The aim of the present study was to determine the nature and frequency of TPO gene mutations in patients with CH, characterised by elevated TSH levels and orthotopic thyroid gland, identified in the Portuguese National Neonatal Screening Programme. Subjects and methods: The sample comprised 55 patients, from 53 unrelated families, with follow-up in the endocrinology clinics of the treatment centres of Porto and Lisbon. Mutation screening in the TPO gene (exons 1–17) was performed by single-strand conformational analysis followed by sequencing of fragments with abnormal migration patterns. Results: Eight different mutations were detected in 13 patients (seven homozygotes and six compound heterozygotes). Novel mutations included three missense mutations, namely 391T > C (S131P), 1274A > G (N425S) and 2512T > A (C838S), as well as the predictable splice mutation 2748G > A (Q916Q/spl?). The undocumented polymorphism 180-47A > C was also detected. Conclusion: The results are in accordance with previous observations confirming the genetic heterogeneity of TPO defects. The proportion of patients in which the aetiology was determined justifies the implementation of this molecular testing in our CH patients with dyshormonogenesis.

Purification of recombinant human thyroid peroxidase (hTPO) from AD293 mammalian cells

2018 ◽  
Vol 106 ◽  
pp. 87-94
Author(s):  
Parvinder Kaur ◽  
Harshada Patil ◽  
Paresh B. Bhanushali ◽  
Shamkant B. Badgujar ◽  
Anuj Kumar Gupta
Keyword(s):  
Mammalian Cells ◽  
Human Thyroid ◽  
Thyroid Peroxidase ◽  
Human Thyroid Peroxidase

scholarly journals The key residues in the immunodominant region 353–363 of human thyroid peroxidase were identified

2006 ◽  
Vol 18 (7) ◽  
pp. 1091-1099 ◽  
Author(s):  
Sandra A. Rebuffat ◽  
Damien Bresson ◽  
Brigitte Nguyen ◽  
Sylvie Péraldi-Roux
Keyword(s):  
Human Thyroid ◽  
Thyroid Peroxidase ◽  
Immunodominant Region ◽  
Human Thyroid Peroxidase ◽  
Key Residues
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