Peptidylgycine α-amidating monooxygenase and copper: a gene-nutrient interaction critical to nervous system function.

Journal of Neuroscience Research
Danielle Bousquet-MooreBetty A Eipper

Abstract

Peptidylgycine alpha-amidating monooxygenase (PAM), a highly conserved copper-dependent enzyme, is essential for the synthesis of all amidated neuropeptides. Biophysical studies revealed that the binding of copper to PAM affects its structure, and cell biological studies demonstrated that the endocytic trafficking of PAM was sensitive to copper. We review data indicating that genetic reduction of PAM expression and mild copper deficiency in mice cause similar alterations in several physiological functions known to be regulated by neuropeptides: thermal regulation, seizure sensitivity, and anxiety-like behavior.

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Citations

Jan 21, 2014·Progress in Neurobiology·Ivo F ScheiberRalf Dringen
Jan 7, 2016·Frontiers in Molecular Neuroscience·Małgorzata LenartowiczLisbeth Birk Møller
Jul 19, 2015·Neurochemistry International·Nadia D'Ambrosi, Luisa Rossi
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Mar 22, 2014·Journal of Neurochemistry·Robert VassarStefan F Lichtenthaler
Nov 7, 2019·Journal of Biological Inorganic Chemistry : JBIC : a Publication of the Society of Biological Inorganic Chemistry·Svetlana LutsenkoKatharina Schmidt
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May 1, 2021·Biomedicines·Nina Horn, Pernilla Wittung-Stafshede
Aug 27, 2021·Metabolites·Mark GermanosMelkam A Kebede

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