caa a22 4500 463208455 CHVBK 20180405153133.0 cr unu---uuuuu 170326e20071201xx s 000 0 eng 10.1007/s10863-007-9101-2 doi (NATIONALLICENCE)springer-10.1007/s10863-007-9101-2 Copper-transporting ATPases ATP7A and ATP7B: cousins, not twins [Elektronische Daten] [Rachel Linz, Svetlana Lutsenko] Copper plays an essential role in human physiology and is indispensable for normal growth and development. Enzymes that are involved in connective tissue formation, neurotransmitter biosynthesis, iron transport, and others essential physiological processes require copper as a cofactor to mediate their reactions. The biosynthetic incorporation of copper into these enzymes takes places within the secretory pathway and is critically dependent on the activity of copper-transporting ATPases ATP7A or ATP7B. In addition, ATP7A and ATP7B regulate intracellular copper concentration by removing excess copper from the cell. These two transporters belong to the family of P1-type ATPases, share significant sequence similarity, utilize the same general mechanism for their function, and show partial colocalization in some cells. However, the distinct biochemical characteristics and dissimilar trafficking properties of ATP7A and ATP7B in cells, in which they are co-expressed, indicate that specific functions of these two copper-transporting ATPases are not identical. Immuno-detection studies in cells and tissues have begun to suggest specific roles for ATP7A and ATP7B. These experiments also revealed technical challenges associated with quantitative detection of copper-transporting ATPases in tissues, as illustrated here by comparing the results of ATP7A and ATP7B immunodetection in mouse cerebellum. Springer Science+Business Media, LLC, 2007 ATP7A nationallicence ATP7B nationallicence Copper nationallicence Wilson disease nationallicence Menkes disease nationallicence Trafficking nationallicence Transport nationallicence Linz Rachel Department of Biochemistry and Molecular Biology, Oregon Health & Science University, 97239, Portland, OR, USA aut Lutsenko Svetlana Department of Biochemistry and Molecular Biology, Oregon Health & Science University, 97239, Portland, OR, USA aut Journal of Bioenergetics and Biomembranes Springer US; http://www.springer-ny.com 39/5-6(2007-12-01), 403-407 0145-479X 39:5-6<403 2007 39 10863 https://doi.org/10.1007/s10863-007-9101-2 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/s10863-007-9101-2 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Linz Rachel Department of Biochemistry and Molecular Biology, Oregon Health & Science University, 97239, Portland, OR, USA aut NATIONALLICENCE 700 1- Lutsenko Svetlana Department of Biochemistry and Molecular Biology, Oregon Health & Science University, 97239, Portland, OR, USA aut NATIONALLICENCE 773 0- Journal of Bioenergetics and Biomembranes Springer US; http://www.springer-ny.com 39/5-6(2007-12-01), 403-407 0145-479X 39:5-6<403 2007 39 10863 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer