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- W135320823 abstract "This chapter discusses clinical implications of glycosylation and posttranslational processing of thyroid-stimulating hormone (TSH). TSH is a glycoprotein hormone of molecular weight 28,000 which is composed of two noncovalently linked subunits, α and β. It is chemically related to the pituitary gonadotropins, luteinizing hormone (LH), follicle-stimulating hormone (FSH), and to chorionic gonadotropin (CG). Elevated serum α/TSH ratios have been described in patients with TSH-secreting pituitary tumors. The excess production from such tumors has been of value in differentiating patients with neoplastic from non-neoplastic causes of TSH-induced hyperthyroidism. In addition, isolated production of α subunit, without concomitant production of TSH or gonadotropins, by certain pituitary adenomas and other malignant tumors is demonstrated. Elevated serum TSH-β/TSH ratios are described in two patients, one with an enlarged thyroid and one with an enlarged pituitary. The TSH-β in both cases have large molecular weight, display immunologic properties different from standard TSH-β, and is unresponsive to thyrotropin releasing hormone. Although this unusual form of TSH-β has been partially characterized, its significance remains unknown. The chapter also describes unusual forms of human TSH with decreased bioactivity. One apparently normal subject was found to have a high-molecular-weight form of TSH with normal receptor-binding properties but decreased bioactivity. Such forms can result from aggregated or protein-bound TSH caused by abnormalities of glycosylation, similar to those noted after tunicamycin treatment." @default.
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- W135320823 date "1985-01-01" @default.
- W135320823 modified "2023-09-27" @default.
- W135320823 title "Glycosylation and Posttranslational Processing of Thyroid-Stimulating Hormone: Clinical Implications" @default.
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- W135320823 doi "https://doi.org/10.1016/b978-0-12-571141-8.50018-4" @default.
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