{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,26]],"date-time":"2026-10-26T17:20:07Z","timestamp":1793035207722,"version":"4.5.0"},"reference-count":48,"publisher":"Bioscientifica","issue":"4","content-domain":{"domain":["jme.bioscientifica.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[2016,5]]},"abstract":"<jats:p>The remarkable conservation of the primary structures and anatomical location of dogfish \u03b1-melanocyte-stimulating hormone (MSH), corticotrophin-like intermediate lobe peptide (CLIP) and adrenocorticotrophic hormone (ACTH) compared with mammals reinforced the tissue-specific processing hypothesis of ACTH peptides in the pituitary gland. The cloning of dogfish pro-opiomelanocortin (POMC) led to the identification of \u03b4-MSH and simultaneously revealed the high conservation of the \u03b3-MSH sequence during evolution. These studies have also shown that \u03b2-MSH is much less conserved during evolution and in some species is not even processed from \u03b2-LPH. Human pro-\u03b3-MSH potentiates the corticosteroidogenic activity of ACTH and peptides generated from its N-terminal, in particular big-\u03b3-MSH, appear to have adrenal mitogenic activity. Human big-\u03b3-MSH (from the zona intermedia) may also cause the adrenache. The review finishes with a cautionary note with regard to the misdiagnosis of the ectopic ACTH syndrome in which partial processing of ACTH can result in large concentrations of \u03b1-MSH and CLIP, which can interfere in the performance of two-site immunoassays, and the problem of the correct disulphide bridge arrangement in synthetic N-POMC peptides is also discussed.<\/jats:p>","DOI":"10.1530\/jme-15-0260","type":"journal-article","created":{"date-parts":[[2015,12,8]],"date-time":"2015-12-08T10:55:58Z","timestamp":1449572158000},"page":"T1-T12","update-policy":"https:\/\/doi.org\/10.1530\/crossmarkpolicy-6","source":"Crossref","is-referenced-by-count":20,"title":["60 YEARS OF POMC: Purification and biological characterisation of melanotrophins and corticotrophins"],"prefix":"10.1530","volume":"56","author":[{"given":"Philip","family":"Lowry","sequence":"first","affiliation":[{"name":"Emeritus Professor School of Biological SciencesUniversity of Reading, Reading, UK"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"416","reference":[{"key":"2016060719184377000_56.4.T1.1","doi-asserted-by":"publisher","DOI":"10.1038\/291156a0"},{"key":"2016060719184377000_56.4.T1.2","doi-asserted-by":"publisher","DOI":"10.1042\/bj2040301"},{"key":"2016060719184377000_56.4.T1.3","doi-asserted-by":"publisher","DOI":"10.1006\/gcen.1999.7256"},{"key":"2016060719184377000_56.4.T1.4","doi-asserted-by":"publisher","DOI":"10.1042\/bj1410439"},{"key":"2016060719184377000_56.4.T1.5","doi-asserted-by":"crossref","first-page":"10096","DOI":"10.1016\/S0021-9258(18)33989-9","article-title":"Characterization of eight forms of corticotropin-like intermediary lobe peptide from the rat intermediary pituitary","volume":"257","author":"Bennett","year":"1982","journal-title":"Journal of Biological Chemistry"},{"key":"2016060719184377000_56.4.T1.6","doi-asserted-by":"crossref","first-page":"8108","DOI":"10.1016\/S0021-9258(20)82034-1","article-title":"Human phosphoserine 31 corticotropin1-39. 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