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.
Publication types
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Research Support, N.I.H., Extramural
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Review
MeSH terms
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Animals
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Copper / deficiency
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Copper / physiology*
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Cytosol / enzymology
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Cytosol / metabolism
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Cytosol / pathology
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Disease Models, Animal
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Endocytosis / genetics
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Gene Expression Regulation, Enzymologic / physiology*
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Heart Atria / enzymology
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Heart Atria / metabolism
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Heart Atria / pathology
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Humans
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Mice
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Mixed Function Oxygenases / chemistry
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Mixed Function Oxygenases / genetics
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Mixed Function Oxygenases / physiology*
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Multienzyme Complexes / chemistry
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Multienzyme Complexes / genetics
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Multienzyme Complexes / physiology*
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Nervous System Diseases / enzymology*
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Nervous System Diseases / metabolism
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Nervous System Diseases / physiopathology
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Neuropeptides / genetics
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Neuropeptides / physiology*
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Pituitary Diseases / enzymology
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Pituitary Diseases / metabolism
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Pituitary Diseases / physiopathology
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Protein Transport / genetics
Substances
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Multienzyme Complexes
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Neuropeptides
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Copper
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Mixed Function Oxygenases
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peptidylglycine monooxygenase