Proenkephalin

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PENK
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesPENK, PE, PENK-A, proenkephalin
External IDsOMIM: 131330 MGI: 104629 HomoloGene: 4528 GeneCards: PENK
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_006211
NM_001135690

NM_001002927
NM_001348209

RefSeq (protein)

NP_001129162

NP_001002927
NP_001335138

Location (UCSC)Chr 8: 56.44 – 56.45 MbChr 4: 4.13 – 4.14 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

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.[5] 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.[5] 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,[6] amidorphin,[7] BAM-18,[8] BAM-20P,[9] BAM-22P,[9] peptide B,[10] peptide E,[11] and peptide F.[12]

See also[edit]

References[edit]

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000181195 - Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000045573 - Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ a b Donald W. Pfaff (2002). Hormones, brain, and behavior. Elsevier. p. 173. ISBN 978-0-12-532109-9. Retrieved 25 November 2011.
  6. ^ Matsuo H, Miyata A, Mizuno K (1983). "Novel C-terminally amidated opioid peptide in human phaeochromocytoma tumour". Nature. 305 (5936): 721–3. doi:10.1038/305721a0. PMID 6633641.
  7. ^ Seizinger BR, Liebisch DC, Gramsch C, et al. (1985). "Isolation and structure of a novel C-terminally amidated opioid peptide, amidorphin, from bovine adrenal medulla". Nature. 313 (5997): 57–9. doi:10.1038/313057a0. PMID 3965972.
  8. ^ Hurlbut DE, Evans CJ, Barchas JD, Leslie FM (June 1987). "Pharmacological properties of a proenkephalin A-derived opioid peptide: BAM 18". European Journal of Pharmacology. 138 (3): 359–66. doi:10.1016/0014-2999(87)90474-2. PMID 3040439.
  9. ^ a b Mizuno K, Minamino N, Kangawa K, Matsuo H (December 1980). "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". Biochemical and Biophysical Research Communications. 97 (4): 1283–90. doi:10.1016/S0006-291X(80)80005-2. PMID 7213356.
  10. ^ Micanovic R, Kruggel W, Ray P, Lewis RV (1984). "Purification and sequence of a non-opioid peptide derived from ovine proenkephalin: implications for possible species specific processing". Peptides. 5 (5): 853–6. doi:10.1016/0196-9781(84)90105-0. PMID 6504720.
  11. ^ Boarder MR, Evans C, Adams M, Erdelyi E, Barchas JD (December 1987). "Peptide E and its products, BAM 18 and Leu-enkephalin, in bovine adrenal medulla and cultured chromaffin cells: release in response to stimulation". Journal of Neurochemistry. 49 (6): 1824–32. doi:10.1111/j.1471-4159.1987.tb02443.x. PMID 3681299.
  12. ^ Jones BN, Stern AS, Lewis RV, et al. (October 1980). "Structure of two adrenal polypeptides containing multiple enkephalin sequences". Archives of Biochemistry and Biophysics. 204 (1): 392–5. doi:10.1016/0003-9861(80)90048-X. PMID 7425644.

External links[edit]