ATP7B expression in human breast epithelial cells is mediated by lactational hormones Michalczyk, Agnes, Bastow, Edward, Greenough, Mark, Camakaris, James, Freestone, David, Taylor, Philip, Linder, Maria, Mercer, Julian and Ackland, M. Leigh 2008, ATP7B expression in human breast epithelial cells is mediated by lactational hormones, Journal of histochemistry and cytochemistry, vol. 56, no. 4, pp. 389-399, doi: 10.1369/jhc.7A7300.2008. Attached Files Name Description MIMEType Size Downloads Title ATP7B expression in human breast epithelial cells is mediated by lactational hormones Author(s) Michalczyk, Agnes orcid.org/0000-0001-5716-0783 Bastow, Edward Greenough, Mark Camakaris, James Freestone, David Taylor, Philip orcid.org/0000-0002-4204-1893 Linder, Maria Mercer, Julian Ackland, M. Leigh orcid.org/0000-0002-7474-6556 Journal name Journal of histochemistry and cytochemistry Volume number 56 Issue number 4 Start page 389 End page 399 Total pages 11 Publisher Histochemical Society Place of publication Seattle, Wash. Publication date 2008-04 ISSN 0022-1554 1551-5044 Keyword(s) ATP7B copper mammary gland secretion lactational hormones Summary A role for the copper transporter, ATP7B, in secretion of copper from the human breast into milk has previously not been reported, although it is known that the murine ortholog of ATP7B facilitates copper secretion in the mouse mammary gland. We show here that ATP7B is expressed in luminal epithelial cells in both the resting and lactating human breast, where it has a perinuclear localization in resting epithelial cells and a diffuse location in lactating tissue. ATP7B protein was present in a different subset of vesicles from those containing milk proteins and did not overlap with Menkes ATPase, ATP-7A, except in the perinuclear region of cells. In the cultured human mammary line, PMC42-LA, treatment with lactational hormones induced a redistribution of ATP7B from a perinuclear region to a region adjacent, but not coincident with, the apical plasma membrane. Trafficking of ATP7B was copper dependent, suggesting that the hormone-induced redistribution of ATP7A was mediated through an increase in intracellular copper. Radioactive copper (64Cu) studies using polarized PMC42-LA cells that overexpressed mAtp7B protein showed that this transporter facilitates copper efflux from the apical surface of the cells. In summary, our results are consistent with an important function of ATP7B in the secretion of copper from the human mammary gland. Notes First publishedin the Journal of Histochemistry and Cytochemistry by the Histochemical Society Language eng DOI 10.1369/jhc.7A7300.2008 Field of Research 060199 Biochemistry and Cell Biology not elsewhere classified HERDC Research category C1 Refereed article in a scholarly journal HERDC collection year 2008 Copyright notice ©2008, The Histochemical Society Free to Read? Yes Persistent URL http://hdl.handle.net/10536/DRO/DU:30017277 Document type: Journal Article Collections: Faculty of Science, Engineering and Built Environment School of Life and Environmental Sciences Open Access Collection Related Links Link Description Link to full-text (open access)   Connect to published version (restricted access) Go to link with your DU access privileges     Unless expressly stated otherwise, the copyright for items in DRO is owned by the author, with all rights reserved. Every reasonable effort has been made to ensure that permission has been obtained for items included in DRO. If you believe that your rights have been infringed by this repository, please contact drosupport@deakin.edu.au. Versions Version Filter Type Fri, 14 Aug 2009, 13:51:37 EST Mon, 07 Sep 2009, 12:29:11 EST Mon, 07 Sep 2009, 12:32:36 EST Wed, 16 Sep 2009, 12:15:02 EST Wed, 16 Sep 2009, 12:16:10 EST Mon, 19 Jan 2015, 10:49:47 EST Fri, 06 Feb 2015, 10:26:06 EST Tue, 06 Sep 2016, 12:34:32 EST Tue, 05 Dec 2017, 06:30:25 EST Fri, 07 Sep 2018, 14:16:12 EST Tue, 23 Oct 2018, 13:17:00 EST Thu, 07 Nov 2019, 02:39:23 EST Thu, 27 Jan 2022, 15:36:41 EST Tue, 15 Feb 2022, 11:35:56 EST Filtered Full Citation counts:   Cited 31 times in TR Web of Science Cited 35 times in Scopus Search Google Scholar Access Statistics: 1249 Abstract Views, 207 File Downloads  -  Detailed Statistics Created: Fri, 14 Aug 2009, 13:51:37 EST