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Proopiomelanocortin
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Proopiomelanocortin
Pro-opiomelanocortin (POMC) is a precursor polypeptide with 241 amino acid residues. POMC is synthesized in corticotrophs of the anterior pituitary from the 267-amino-acid-long polypeptide precursor pre-pro-opiomelanocortin (pre-POMC), by the removal of a 26-amino-acid-long signal peptide sequence during translation. POMC is part of the central melanocortin system.
The POMC gene is located on chromosome 2p23.3. This gene encodes a 285-amino acid polypeptide hormone precursor that undergoes extensive, tissue-specific, post-translational processing via cleavage by subtilisin-like enzymes known as prohormone convertases.
The POMC gene is expressed in both the anterior and intermediate lobes of the pituitary gland. Its protein product is primarily synthesized by corticotropic cells in the anterior pituitary, but it is also produced in several other tissues:
POMC is cut (cleaved) to give rise to multiple peptide hormones. Each of these peptides is packaged in large dense-core vesicles that are released from the cells by exocytosis in response to appropriate stimulation:[citation needed]
The POMC gene encodes a 285-amino acid polypeptide precursor that undergoes extensive, tissue-specific post-translational processing. This processing is primarily mediated by subtilisin-like prohormone convertases, which cleave the precursor at specific basic amino acid sequences—typically Arg-Lys, Lys-Arg, or Lys-Lys.
In many tissues, four primary cleavage sites are utilized, resulting in the production of two major bioactive peptides: adrenocorticotrophin (ACTH), which is essential for normal steroidogenesis and adrenal gland maintenance, and β-lipotropin. However, the POMC precursor contains at least eight potential cleavage sites, and depending on the tissue type and the specific convertases expressed, it can be processed into up to ten biologically active peptides with diverse functions.
Key processing enzymes include prohormone convertase 1 (PC1), prohormone convertase 2 (PC2), carboxypeptidase E (CPE), peptidyl α-amidating monooxygenase (PAM), N-acetyltransferase (N-AT), and prolylcarboxypeptidase (PRCP).[citation needed]
In addition to proteolytic cleavage, POMC processing involves other post-translational modifications such as glycosylation and acetylation. The specific pattern of cleavage and modification is tissue-dependent. For example, in the hypothalamus, placenta, and epithelium, all cleavage sites may be active, generating peptides involved in pain modulation, energy homeostasis, immune responses, and melanocyte stimulation. These peptides include multiple melanotropins, lipotropins, and endorphins, many of which are derived from the larger ACTH and β-lipotropin peptides.[citation needed]
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Proopiomelanocortin
Pro-opiomelanocortin (POMC) is a precursor polypeptide with 241 amino acid residues. POMC is synthesized in corticotrophs of the anterior pituitary from the 267-amino-acid-long polypeptide precursor pre-pro-opiomelanocortin (pre-POMC), by the removal of a 26-amino-acid-long signal peptide sequence during translation. POMC is part of the central melanocortin system.
The POMC gene is located on chromosome 2p23.3. This gene encodes a 285-amino acid polypeptide hormone precursor that undergoes extensive, tissue-specific, post-translational processing via cleavage by subtilisin-like enzymes known as prohormone convertases.
The POMC gene is expressed in both the anterior and intermediate lobes of the pituitary gland. Its protein product is primarily synthesized by corticotropic cells in the anterior pituitary, but it is also produced in several other tissues:
POMC is cut (cleaved) to give rise to multiple peptide hormones. Each of these peptides is packaged in large dense-core vesicles that are released from the cells by exocytosis in response to appropriate stimulation:[citation needed]
The POMC gene encodes a 285-amino acid polypeptide precursor that undergoes extensive, tissue-specific post-translational processing. This processing is primarily mediated by subtilisin-like prohormone convertases, which cleave the precursor at specific basic amino acid sequences—typically Arg-Lys, Lys-Arg, or Lys-Lys.
In many tissues, four primary cleavage sites are utilized, resulting in the production of two major bioactive peptides: adrenocorticotrophin (ACTH), which is essential for normal steroidogenesis and adrenal gland maintenance, and β-lipotropin. However, the POMC precursor contains at least eight potential cleavage sites, and depending on the tissue type and the specific convertases expressed, it can be processed into up to ten biologically active peptides with diverse functions.
Key processing enzymes include prohormone convertase 1 (PC1), prohormone convertase 2 (PC2), carboxypeptidase E (CPE), peptidyl α-amidating monooxygenase (PAM), N-acetyltransferase (N-AT), and prolylcarboxypeptidase (PRCP).[citation needed]
In addition to proteolytic cleavage, POMC processing involves other post-translational modifications such as glycosylation and acetylation. The specific pattern of cleavage and modification is tissue-dependent. For example, in the hypothalamus, placenta, and epithelium, all cleavage sites may be active, generating peptides involved in pain modulation, energy homeostasis, immune responses, and melanocyte stimulation. These peptides include multiple melanotropins, lipotropins, and endorphins, many of which are derived from the larger ACTH and β-lipotropin peptides.[citation needed]
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