Journal
CELL REPORTS
Volume 9, Issue 3, Pages 801-809Publisher
CELL PRESS
DOI: 10.1016/j.celrep.2014.10.006
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Funding
- Funding Program for Next Generation World Leading Researchers (NEXT Program) initiated by the Council for Science and Technology Policy (CSTP) [LS055]
- Japan Society for the Promotion of Science (JSPS) Fellows [22005794]
- JSPS KAKENHI [26000013]
- WPI program
- NIH [R37DK15070]
- Grants-in-Aid for Scientific Research [26650033, 26000013, 26860163] Funding Source: KAKEN
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Thyroid-stimulating hormone (TSH; thyrotropin) is a glycoprotein secreted from the pituitary gland. Pars distalis-derived TSH (PD-TSH) stimulates the thyroid gland to produce thyroid hormones (THs), whereas pars tuberalis-derived TSH (PT-TSH) actsonthe hypothalamus to regulate seasonal physiology and behavior. However, it had not been clear how these two TSHs avoid functional crosstalk. Here, we show that this regulation ismediated by tissue-specific glycosylation. Although PT-TSH is released into the circulation, it does not stimulate the thyroid gland. PD-TSH is known to have sulfated biantennary N-glycans, and sulfated TSH is rapidly metabolized in the liver. In contrast, PT-TSH has sialylated multibranched N-glycans; in the circulation, it forms the macro-TSH complex with immunoglobulin or albumin, resulting in the loss of its bioactivity. Glycosylation is fundamental to a wide range of biological processes. This report demonstrates its involvement in preventing functional crosstalk of signaling molecules in the body.
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