Abstract
Carboxy-terminal amidation of biologically active peptides, an important characteristic of more than half of these substances, occurs during the maturation process of peptide precursors. It is catalyzed by peptidylglycine α-amidating monooxygenase (PAM), an enzyme that is copper-dependent. We show here that alterations of copper stores in cultured cells from different origins (pancreas and hypothalamus) affect the immunoreactivity of thyrotropin-releasing hormone (TRH) and corticotropin-releasing factor (CRF) (two α-amidated peptides). This suggests that copper can affect neuropeptide biosynthesis and may play a role in the endocrine or central nervous system function.
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Giraud, P., Maltèse, JY., Boudouresque, F. et al. Peptidylglycine α-amidating monooxygenase activity and TRH and CRF biosynthesis. Biol Trace Elem Res 32, 293–301 (1992). https://doi.org/10.1007/BF02784614
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DOI: https://doi.org/10.1007/BF02784614