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2016 ; 56
(4
): T77-97
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60 YEARS OF POMC: Biosynthesis, trafficking, and secretion of
pro-opiomelanocortin-derived peptides
#MMPMID26880796
Cawley NX
; Li Z
; Loh YP
J Mol Endocrinol
2016[May]; 56
(4
): T77-97
PMID26880796
show ga
Pro-opiomelanocortin (POMC) is a prohormone that encodes multiple smaller peptide
hormones within its structure. These peptide hormones can be generated by
cleavage of POMC at basic residue cleavage sites by prohormone-converting enzymes
in the regulated secretory pathway (RSP) of POMC-synthesizing endocrine cells and
neurons. The peptides are stored inside the cells in dense-core secretory
granules until released in a stimulus-dependent manner. The complexity of the
regulation of the biosynthesis, trafficking, and secretion of POMC and its
peptides reflects an impressive level of control over many factors involved in
the ultimate role of POMC-expressing cells, that is, to produce a range of
different biologically active peptide hormones ready for action when signaled by
the body. From the discovery of POMC as the precursor to adrenocorticotropic
hormone (ACTH) and ?-lipotropin in the late 1970s to our current knowledge, the
understanding of POMC physiology remains a monumental body of work that has
provided insight into many aspects of molecular endocrinology. In this article,
we describe the intracellular trafficking of POMC in endocrine cells, its sorting
into dense-core secretory granules and transport of these granules to the RSP.
Additionally, we review the enzymes involved in the maturation of POMC to its
various peptides and the mechanisms involved in the differential processing of
POMC in different cell types. Finally, we highlight studies pertaining to the
regulation of ACTH secretion in the anterior and intermediate pituitary and POMC
neurons of the hypothalamus.
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