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• W53460884 abstract "Publisher Summary This chapter discusses glucocorticoid regulation of proopiomelanocortin gene expression in rodent pituitary. The pituitary peptide hormones, adrenocorticotropin (ACTH), endorphin, and melanocyte stimulating hormone (MSH) are derived from a larger precursor protein designated as proopiomelanocortin (POMC). The three MSH peptides contained within POMC, α, β, and γ are each located in a different region of the precursor. POMC is produced in many different tissues, particularly, the anterior and intermediate lobes of the pituitary which are the major sites of its synthesis. Radioimmunoassay and immunohistochemical evidence have identified POMC related peptides in the central nervous system tissue, intestinal tissue, and in certain ectopic tumors. POMC is processed to its end product hormones by several posttranslational events, some of which are tissue specific. Differential processing of the POMC precursor is best characterized in the anterior and intermediate lobes of the pituitary. Although the POMC protein appears to be the same in the two lobes, proteolytical processing results in distinctly different final peptide products. The anterior lobe of the pituitary is the source of the bioactive ACTH which is secreted into the blood stream. There are three basic mechanisms by which glucocorticoids could specifically decrease anterior pituitary content of POMC-related peptides in conjunction with a decrease in secretory rate: (1) increase the rate of intracellular degradation, (2) block the processing pathway, or (3) decrease the rate of synthesis." @default.
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• W53460884 date "1982-01-01" @default.
• W53460884 modified "2023-09-24" @default.
• W53460884 title "Glucocorticoid Regulation of Proopiomelanocortin Gene Expression in Rodent Pituitary" @default.
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• W53460884 doi "https://doi.org/10.1016/b978-0-12-571138-8.50011-1" @default.
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