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JBIC Journal of Biological Inorganic Chemistry

, Volume 24, Issue 8, pp 1171–1177 | Cite as

Is brain iron trafficking part of the physiology of the amyloid precursor protein?

  • Danielle K. Bailey
  • Daniel J. KosmanEmail author
Commentary
Part of the following topical collections:
  1. Metal Ions and Degenerative Diseases

Abstract

The amyloid precursor protein is so named, because a proteolytic fragment of it was found associated with a neuropathic disorder now known as Alzheimer’s disease. This fragment, Aβ, along with tau makes up the plaques and tangles that are the hallmark of AD. Iron (and other first-row transition metals) is found associated with these proteinaceous deposits. Much research has focused on the relationship of the plaques and iron to the etiology of the disease. This commentary asks another question, one only more recently addressed namely, what is the physiologic function of the amyloid precursor protein (APP) and of its secretase-generated soluble species? Overall, the data make clear that APP and its products have neurotrophic functions and some data indicate one of these may be to modulate the trafficking of iron in the brain.

Keywords

Amyloid precursor protein Ferroportin Iron efflux Hephaestin APP-like proteins Iron metabolism Cell surface protein Membrane transport Metal transport Metal binding Alzheimer’s disease 

Notes

Acknowledgements

The work in the Kosman lab is supported by a grant from the National Institute of Neurological Disorders and Stroke, NS102337. This support is gratefully acknowledged.

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Copyright information

© Society for Biological Inorganic Chemistry (SBIC) 2019

Authors and Affiliations

  1. 1.Department of Biochemistry, Jacobs School of Medicine and Biomedical SciencesThe University at BuffaloBuffaloUSA

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