Peptidylgycine α-amidating monooxygenase and copper: a gene-nutrient interaction critical to nervous system function
Danielle Bousquet-Moore1, Richard E Mains, Betty A Eipper
1University of Connecticut Health Center, Farmington, Connecticut 06030-3401, USA.
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.
Related Concept Videos
Human Genetics
The complex relationship between genetics and psychology is observable through common biological components such...
RNA Editing
Protein Modifications in the RER
Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal sequences.
Amino Acid Biosynthetic Pathways
Phase II Reactions: Sulfation and Conjugation with α-Amino Acids
Amino Acid Catabolism


