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urge on; cause to act; "The other children egged the boy on, but he did not want to throw the stone through the window" (同)incite, egg on
a pointed instrument that is used to prod into a state of motion (同)goad
in favor of a proposition, opinion, etc.
an argument in favor of a proposal
in favor of (an action or proposal etc.); "a pro vote"

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出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2014/04/15 06:13:23」(JST)

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Pro-opiomelanocortin (POMC) is a precursor polypeptide with 241 amino acid residues. POMC is synthesized from the 285-amino-acid-long polypeptide precursor pre-pro-opiomelanocortin (pre-POMC), by the removal of a 44-amino-acid-long signal peptide sequence during translation.

Function

POMC is 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:

α-MSH produced by neurons in the arcuate nucleus has important roles in the regulation of appetite and sexual behavior, while α-MSH secreted from the intermediate lobe of the pituitary regulates the production of melanin.
ACTH is a peptide hormone that regulates the secretion of glucocorticoids from the adrenal cortex.
β-Endorphin and [Met]enkephalin are endogenous opioid peptides with widespread actions in the brain.

Synthesis

The POMC gene is located on chromosome 2p23.3. The POMC gene is expressed in both the anterior and intermediate lobes of the pituitary gland. 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 encoded protein is synthesized mainly in corticotroph cells of the anterior pituitary, where four cleavage sites are used; adrenocorticotrophin (ACTH), essential for normal steroidogenesis and the maintenance of normal adrenal weight, and β-lipotropin are the major end-products. However, there are at least eight potential cleavage sites within the polypeptide precursor and, depending on tissue type and the available convertases, processing may yield as many as ten biologically active peptides involved in diverse cellular functions. Cleavage sites consist of the sequences Arg-Lys, Lys-Arg, or Lys-Lys. Enzymes responsible for processing of POMC peptides include prohormone convertase 1 (PC1), prohormone convertase 2 (PC2), carboxypeptidase E (CPE), peptidyl α-amidating monooxygenase (PAM), N-acetyltransferase (N-AT), and prolylcarboxypeptidase (PRCP).

The processing of POMC involves glycosylations, acetylations, and extensive proteolytic cleavage at sites shown to contain regions of basic protein sequences. However, the proteases that recognize these cleavage sites are tissue-specific. In some tissues, including the hypothalamus, placenta, and epithelium, all cleavage sites may be used, giving rise to peptides with roles in pain and energy homeostasis, melanocyte stimulation, and immune modulation. These include several distinct melanotropins, lipotropins, and endorphins that are contained within the adrenocorticotrophin and β-lipotropin peptides.

It is synthesized by:

Corticotrope cells of the anterior pituitary gland
Melanotrope cells of the intermediate lobe of the pituitary gland
3,148±62 Neurons in the arcuate nucleus of the hypothalamus^[1]
Smaller populations of neurons in the dorsomedial hypothalamus and brainstem
Melanocytes in the skin

Derivatives

proopiomelanocortin derivatives
POMC

γ-MSH	ACTH		β-lipotropin

	α-MSH	CLIP	γ-lipotropin		β-endorphin

				β-MSH

The large molecule of POMC is the source of several important biologically active substances. POMC can be cleaved enzymatically into the following peptides:

N-Terminal Peptide of Proopiomelanocortin (NPP, or pro-γ-MSH)
γ-Melanotropin (γ-MSH)
Corticotropin (Adrenocorticotropic Hormone, or ACTH)
α-Melanotropin (α-Melanocyte-Stimulating Hormone, or α-MSH)
Corticotropin-like Intermediate Peptide (CLIP)
β-Lipotropin (β-LPH)
Lipotropin Gamma (γ-LPH)
β-Melanotropin (β-MSH)
β-Endorphin
[Met]Enkephalin

Although the N-terminal 5 amino acids of β-endorphin are identical to the sequence of [Met]enkephalin, it is not generally thought that β-endorphin is converted into [Met]enkephalin.^{[citation needed]} Instead, [Met]enkephalin is produced from its own precursor, proenkephalin A.

The production of β-MSH occurs in humans but not in mice or rats due to the absence of the enzymatic processing site in the rodent POMC.

Clinical significance

Mutations in this gene have been associated with early onset obesity, adrenal insufficiency, and red hair pigmentation. Alternatively spliced transcript variants encoding the same protein have been described.^[2]^[3]

Interactions

Proopiomelanocortin has been shown to interact with melanocortin 4 receptor.^[4]^[5]

References

^ Cowley MA, Smart JL, Rubinstein M, Cerdán MG, Diano S, Horvath TL, Cone RD, Low MJ (May 2001). "Leptin activates anorexigenic POMC neurons through a neural network in the arcuate nucleus". Nature 411 (6836): 480–4. doi:10.1038/35078085. PMID 11373681.
^ "Entrez Gene: POMC proopiomelanocortin (adrenocorticotropin/ beta-lipotropin/ alpha-melanocyte stimulating hormone/ beta-melanocyte stimulating hormone/ beta-endorphin)".
^ Kuehnen P, Mischke M, Wiegand S, Sers C, Horsthemke B, Lau S, Keil T, Lee YA, Grueters A, Krude H (2012). "An Alu element-associated hypermethylation variant of the POMC gene is associated with childhood obesity". In Yeo, Giles S. H. PLoS Genet. 8 (3): e1002543. doi:10.1371/journal.pgen.1002543. PMC 3305357. PMID 22438814.
^ Yang YK, Fong TM, Dickinson CJ, Mao C, Li JY, Tota MR, Mosley R, Van Der Ploeg LH, Gantz I (December 2000). "Molecular determinants of ligand binding to the human melanocortin-4 receptor". Biochemistry 39 (48): 14900–11. doi:10.1021/bi001684q. PMID 11101306.
^ Yang YK, Ollmann MM, Wilson BD, Dickinson C, Yamada T, Barsh GS, Gantz I (March 1997). "Effects of recombinant agouti-signaling protein on melanocortin action". Mol. Endocrinol. 11 (3): 274–80. doi:10.1210/me.11.3.274. PMID 9058374.

External links

Pro-Opiomelanocortin at the US National Library of Medicine Medical Subject Headings (MeSH)

This article incorporates public domain material from websites or documents of the National Center for Biotechnology Information (Reference Sequence collection).

UpToDate Contents

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English Journal

Effects of sleeve gastrectomy and gastric banding on the hypothalamic feeding center in an obese rat model.

Kawasaki T1, Ohta M2, Kawano Y2, Masuda T2, Gotoh K3, Inomata M2, Kitano S4.
Surgery today.Surg Today.2015 Dec;45(12):1560-6. doi: 10.1007/s00595-015-1135-1. Epub 2015 Feb 28.
PURPOSE: Laparoscopic sleeve gastrectomy (SG) and gastric banding (GB) are popular bariatric procedures for treating morbid obesity. This study aimed to investigate changes in the hypothalamic feeding center after these surgeries in a diet-induced obese rat model.METHODS: Obesity was induced in 60 S
PMID 25724939

Tankyrases regulate glucoregulatory mechanisms and somatic growth via the central melanocortin system in zebrafish larvae.

Wang H1, Semenova S1, Kuusela S1, Panula P1, Lehtonen S2.
FASEB journal : official publication of the Federation of American Societies for Experimental Biology.FASEB J.2015 Nov;29(11):4435-48. doi: 10.1096/fj.15-271817. Epub 2015 Jul 13.
The central melanocortin system is a key regulator of energy homeostasis. Recent studies indicate that tankyrases (TNKSs), which poly(ADP-ribosyl)ate target proteins and direct them toward proteasomal degradation, affect overall metabolism, but the exact molecular mechanisms remain unclear. We used
PMID 26169937

The Complementary Role of Transcription Factors in the Accurate Diagnosis of Clinically Nonfunctioning Pituitary Adenomas.

Nishioka H1,2, Inoshita N3,4, Mete O5, Asa SL5, Hayashi K6, Takeshita A6,4, Fukuhara N7, Yamaguchi-Okada M7, Takeuchi Y6,4, Yamada S7,4.
Endocrine pathology.Endocr Pathol.2015 Oct 19. [Epub ahead of print]
Clinically nonfunctioning pituitary adenomas (NFAs) may be hormonally inactive tumors of differentiated cells, mainly not only gonadotroph adenomas (GAs) but also silent corticotroph adenomas (SCAs) and other differentiated silent adenomas. Recently, the use of transcription factors has been recomme
PMID 26481628

Japanese Journal

Possible Involvement of Hypothalamic Nucleobindin-2 in Hyperphagic Feeding in Tsumura Suzuki Obese Diabetes Mice

Miyata Shigeo,Yamada Nao,Kawada Tomie
Biological and Pharmaceutical Bulletin 35(10), 1784-1793, 2012
… The mRNA levels of galanin, melanin-concentrating hormone, neuropeptide Y, and pro-opiomelanocortin were significantly changed in the hypothalamus in TSOD mice at several time points. …
NAID 130001872381

Hypothalamic Melanocortin System on Feeding Regulation in Birds : A Review

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The journal of poultry science 48(1), 1-13, 2011-01-25
NAID 10027817305

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リンク元	「プロオピオメラノコルチン」
拡張検索	「pro-opiomelanocortin peptide family」
関連記事	「prod」「pros」「pro」「p」

「プロオピオメラノコルチン」

Available protein structures:
Pfam	structures
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary

Opioids neuropeptide
Identifiers
Symbol	Op_neuropeptide
Pfam	PF08035
InterPro	IPR013532
PROSITE	PDOC00964
Available protein structures:
Pfam	structures
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary

Proopiomelanocortin
Identifiers
Symbols	POMC ; ACTH; CLIP; LPH; MSH; NPP; POC
External IDs	OMIM: 176830 MGI: 97742 HomoloGene: 723 GeneCards: POMC Gene
Gene Ontology
Molecular function	• G-protein coupled receptor binding; • receptor binding; • hormone activity; • type 3 melanocortin receptor binding; • type 4 melanocortin receptor binding; • type 1 melanocortin receptor binding;
Cellular component	• extracellular region; • extracellular space; • cytoplasm; • peroxisome; • peroxisomal matrix; • secretory granule; • secretory granule lumen;
Biological process	• generation of precursor metabolites and energy; • signal transduction; • neuropeptide signaling pathway; • cell-cell signaling; • regulation of blood pressure; • peptide hormone processing; • regulation of appetite; • negative regulation of tumor necrosis factor production; • cellular pigmentation; • cellular protein metabolic process; • positive regulation of transcription from RNA polymerase II promoter;
	Sources: Amigo / QuickGO
RNA expression pattern
	More reference expression data
Orthologs
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