The effects of pro-opiomelanocortin peptides on cyclic AMP and tyrosinase in melanoma cells |
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| Authors: | J M Farah J F Bishop H Q Nguyen T L O'Donohue |
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| Affiliation: | 1. Department of Public Health and Clinical and Molecular Medicine University of Cagliari, Italy, Cagliari, Italy;2. Department of Radiology, Azienda Ospedaliero Universitaria (A.O.U.), di Cagliari-Polo di Monserrato s.s. 554 Monserrato, Cagliari, 09045, Italy;3. UOC of Gastroenterology, Azienda Ospedaliero - Universitaria, Cagliari, Italy;4. International Mood Center, University of CA, San Diego, USA |
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| Abstract: | Des-, mono-, and diacetylated melanotropin (des-, mono-, and di-Ac MSH, respectively) were compared for their dose-related effects on content of adenosine 3':5'-monophosphate (cAMP) and tyrosinase activity in the Cloudman S91 mouse melanoma tumor. Des-Ac MSH was more potent than the acetylated forms of MSH at increasing cellular levels of cAMP; mono- and di-Ac MSHs, however, were more potent than des-Ac MSH at elevating the activity of the enzyme, tyrosinase. Lysine-gamma1 MSH, a melanotropin from the amino terminus of pro-opiomelanocortin, exhibited slight stimulatory effects on tyrosinase and these actions were less than additive to those of mono-Ac MSH. Unlike their actions on amphibian skin-darkening or in mammalian behavior, neither beta-endorphin1-31 nor its derivatives, N-Ac-beta-endorphin1-27 or beta-endorphin30-31 (glycylglutamine), exhibited any influence on tyrosinase activity evoked by mono-Ac MSH in the tumor cells. |
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