Follicular thyroglobulin (TG) suppression of thyroid-restricted genes involves the apical membrane asialoglycoprotein receptor and TG phosphorylation
Open accessAbstract
Follicular thyroglobulin (TG) decreases expression of the thyroid-restricted transcription factors, thyroid transcription factor (TTF)-1, TTF-2, and Pax-8, thereby suppressing expression of the sodium iodide symporter, thyroid peroxidase, TG, and thyrotropin receptor genes (Suzuki, K., Lavaroni, S., Mori, A., Ohta, M., Saito, J., Pietrarelli, M., Singer, D. S., Kimura, S., Katoh, R., Kawaoi, A. , and Kohn, L. D. (1997) Proc. Natl. Acad. Sci. U. S. A. 95, 8251-8256). The ability of highly purified 27, 19, or 12 S follicular TG to suppress thyroid-restricted gene expression correlates with their ability to bind to FRTL-5 thyrocytes and is inhibited by a specific antibody to the thyroid apical membrane asialoglycoprotein receptor (ASGPR), which is related to the ASGPR of liver cells. Phosphorylating serine/threonine residues of TG, by autophosphorylation or protein kinase A, eliminates TG suppression and enhances transcript levels of the thyroid-restricted genes 2-fold in the absence of a change in TG binding to the ASGPR. Follicular TG suppression of thyroid-restricted genes is thus mediated by the ASPGR on the thyrocyte apical membrane and regulated by a signal system wherein phosphorylation of serine/threonine residues on the bound ligand is an important component. These data provide a hitherto unsuspected role for the ASGPR in transcriptional signaling, aside from its role in endocytosis. They establish a functional role for phosphorylated serine/threonine residues on the TG molecule.
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ASGPR can bind more recently synthesized, poorly iodinated and sialylated TG and route them away from the lysosomal pathway such that they serve as negative feedback signals to repress thyroid-specific TFs (TTFs).
“ASGPR can also bind more recently synthesized, poorly iodinated and sialylated TG and route them away from the lysosomal pathway such that they serve as negative feedback signals to repress thyroid-specific TFs (TTFs) (68, 92).”
From Intrathyroidal feedforward and feedback network regulating thyroid hormone synthesis and secretion (2022) · cites this paper as [68]
The passage labeled Abstract (page unavailable) hypothesizes that apical ASGPR binds recently synthesized, poorly iodinated and poorly sialylated TG, sequestering it from fluid pinocytosis. The same section supports ASGPR-mediated suppression of thyroid-restricted transcription factors, but does not establish that ASGPR routes TG away from lysosomes; it also describes the selective binding as a hypothesis, not a demonstrated pathway. (LLM, conf=0.86)
Experimental — accuracy not yet measuredMore recently synthesized TG molecules, which are low or yet to be iodinated, tend to bind to membrane receptors including megalin and ASGPR and are internalized along with receptor recycling, while highly iodinated and sialylated TG molecules preferentially undergo nonspecific fluid pinocytosis.
“more recently synthesized TG molecules, which are low or yet to be iodinated, tend to bind to membrane receptors including megalin and ASGPR and are internalized along with receptor recycling, while highly iodinated and sialylated TG molecules preferentially undergo nonspecific fluid pinocytosis (68).”
From Intrathyroidal feedforward and feedback network regulating thyroid hormone synthesis and secretion (2022) · cites this paper as [68]
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Intrathyroidal feedforward and feedback network regulating thyroid hormone synthesis and secretion
Jing, L., & Zhang, Q. (2022) · Frontiers in Endocrinology · doi:10.3389/fendo.2022.992883 · Cited by 61 · see citing works
- Authors
- Ulianich, L., Suzuki, K., Mori, A., Nakazato, M., Pietrarelli, M., Goldsmith, P., Pacifico, F., Consiglio, E., Formisano, S., & Kohn, L. D.
- Affiliations
- National Institutes of Health (US)
- University of Naples Federico II (IT)
- Corresponding author
- Kohn, Leonard D.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1999-08
- Volume
- 274
- Issue
- 35
- Pages
- 25099-25107
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2149955916
- Cited by
- 62
- References
- 0
- Citations by year
- 2023: 3 · 2022: 3 · 2019: 2 · 2018: 1 · 2017: 4 · 2016: 2 · 2015: 2 · 2014: 4 · 2013: 2 · 2012: 2
- FWCI
- 3.92
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Institutional Repositories DataBase (IRDB) (submittedVersion)
- INFM-OAR (INFN Catania) (submittedVersion, cc-by)
- Topics
- Health Sciences › Medicine › Endocrinology, Diabetes and Metabolism › Thyroid Disorders and Treatments
- Health Sciences › Medicine › Endocrinology, Diabetes and Metabolism › Thyroid Cancer Diagnosis and Treatment
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Developmental Biology and Gene Regulation
- Keywords
- asialoglycoprotein receptor, TTF-1, PAX8, sodium iodide symporter, thyroid peroxidase, TSH receptor, FRTL-5 cells, protein kinase A, transcriptional regulation, endocytosis
- MeSH terms
- Thyroid Nuclear Factor 1, Animals, Cell Line, Gene Expression Regulation, Genes, MHC Class I, Iodide Peroxidase, Nuclear Proteins, Phosphorylation, Phosphoserine, Promoter Regions, Genetic, Protein Binding, Receptors, Cell Surface, Recombinant Proteins, RNA, Messenger, Suppression, Genetic, Thyroglobulin, Thyroid Gland, Transcription Factors, Transfection, Okadaic Acid, Asialoglycoprotein Receptor, Rats
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