proenkephalin

{{Short description|Protein-coding gene in the species Homo sapiens}}

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Proenkephalin (PENK), formerly known as proenkephalin A (since proenkephalin B was renamed prodynorphin), is an endogenous opioid polypeptide hormone which, via proteolyic cleavage, produces the enkephalin peptides met-enkephalin, and to a lesser extent, leu-enkephalin.{{cite book | author = Donald W. Pfaff | title = Hormones, brain, and behavior | url = https://books.google.com/books?id=cGbE2nC__Q0C&pg=PA173 | access-date = 25 November 2011 | year = 2002 | publisher = Elsevier | isbn = 978-0-12-532109-9 | pages = 173}} Upon cleavage, each proenkephalin peptide results in the generation of four copies of Met-enkephalin, two extended copies of met-enkephalin, and one copy of leu-enkephalin. Contrarily, Leu-enkephalin is predominantly synthesized from prodynorphin, which produces three copies of it per cleavage, and no copies of Met-enkephalin. Other endogenous opioid peptides produced by proenkephalin include adrenorphin,{{cite journal | vauthors = Matsuo H, Miyata A, Mizuno K | title = Novel C-terminally amidated opioid peptide in human phaeochromocytoma tumour | journal = Nature | volume = 305 | issue = 5936 | pages = 721–723 | year = 1983 | pmid = 6633641 | doi = 10.1038/305721a0 | s2cid = 4320171 | bibcode = 1983Natur.305..721M }} amidorphin,{{cite journal | vauthors = Seizinger BR, Liebisch DC, Gramsch C, Herz A, Weber E, Evans CJ, Esch FS, Böhlen P | title = Isolation and structure of a novel C-terminally amidated opioid peptide, amidorphin, from bovine adrenal medulla | journal = Nature | volume = 313 | issue = 5997 | pages = 57–59 | year = 1985 | pmid = 3965972 | doi = 10.1038/313057a0 | s2cid = 4363051 | bibcode = 1985Natur.313...57S }} BAM-18,{{cite journal | vauthors = Hurlbut DE, Evans CJ, Barchas JD, Leslie FM | title = Pharmacological properties of a proenkephalin A-derived opioid peptide: BAM 18 | journal = European Journal of Pharmacology | volume = 138 | issue = 3 | pages = 359–366 | date = June 1987 | pmid = 3040439 | doi = 10.1016/0014-2999(87)90474-2 }} BAM-20P,{{cite journal | vauthors = Mizuno K, Minamino N, Kangawa K, Matsuo H | title = A new family of endogenous "big" Met-enkephalins from bovine adrenal medulla: purification and structure of docosa- (BAM-22P) and eicosapeptide (BAM-20P) with very potent opiate activity | journal = Biochemical and Biophysical Research Communications | volume = 97 | issue = 4 | pages = 1283–1290 | date = December 1980 | pmid = 7213356 | doi = 10.1016/S0006-291X(80)80005-2 }} BAM-22P, peptide B,{{cite journal | vauthors = Micanovic R, Kruggel W, Ray P, Lewis RV | title = Purification and sequence of a non-opioid peptide derived from ovine proenkephalin: implications for possible species specific processing | journal = Peptides | volume = 5 | issue = 5 | pages = 853–856 | year = 1984 | pmid = 6504720 | doi = 10.1016/0196-9781(84)90105-0 | s2cid = 3869685 }} peptide E,{{cite journal | vauthors = Boarder MR, Evans C, Adams M, Erdelyi E, Barchas JD | title = Peptide E and its products, BAM 18 and Leu-enkephalin, in bovine adrenal medulla and cultured chromaffin cells: release in response to stimulation | journal = Journal of Neurochemistry | volume = 49 | issue = 6 | pages = 1824–1832 | date = December 1987 | pmid = 3681299 | doi = 10.1111/j.1471-4159.1987.tb02443.x | s2cid = 19919675 }} and peptide F.{{cite journal | vauthors = Jones BN, Stern AS, Lewis RV, Kimura S, Stein S, Udenfriend S, Shively JE | title = Structure of two adrenal polypeptides containing multiple enkephalin sequences | journal = Archives of Biochemistry and Biophysics | volume = 204 | issue = 1 | pages = 392–395 | date = October 1980 | pmid = 7425644 | doi = 10.1016/0003-9861(80)90048-X }}