You are not logged in.

Ceruloplasmin is regulated by copper and lactational hormones in PMC42-LA mammary epithelial cell culture models

Freestone, David, Denoyer, Delphine, Jakab, Matthew, Ackland, M. Leigh, Cater, Michael and Michalczyk, Agnes 2016, Ceruloplasmin is regulated by copper and lactational hormones in PMC42-LA mammary epithelial cell culture models, Metallomics, vol. 8, no. 9, pp. 941-950, doi: 10.1039/c6mt00086j.

Attached Files
Name Description MIMEType Size Downloads

Title Ceruloplasmin is regulated by copper and lactational hormones in PMC42-LA mammary epithelial cell culture models
Author(s) Freestone, David
Denoyer, DelphineORCID iD for Denoyer, Delphine orcid.org/0000-0001-8932-5116
Jakab, Matthew
Ackland, M. LeighORCID iD for Ackland, M. Leigh orcid.org/0000-0002-7474-6556
Cater, Michael
Michalczyk, AgnesORCID iD for Michalczyk, Agnes orcid.org/0000-0001-5716-0783
Journal name Metallomics
Volume number 8
Issue number 9
Start page 941
End page 950
Total pages 10
Publisher Royal Society of Chemistry
Place of publication Cambridge, Eng.
Publication date 2016-09-01
ISSN 1756-591X
Summary Ceruloplasmin (Cp) is a multicopper ferroxidase that is considered to be an important source of copper in milk for normal neonatal development. We investigated the expression, subcellular localization and secretion of Cp in PMC42-LA cell culture models representative of resting, lactating and suckled human mammary epithelia. Both secreted Cp (sCp) and plasma membrane associated glycosylphosphatidylinositol-linked Cp (GPI-Cp) were expressed in PMC42-LA cells. In all three epithelial models (resting, lactating and suckled), the expression and secretion of copper-bound, ferroxidase active, Cp (holo-Cp) was dependent on media copper concentration. In low copper (bathocuproinedisulphonic acid/d-penicillamine treated models) there was greater than a 2-fold decrease in holo-Cp expression and secretion, which was mirrored by a 2-fold increase in the expression and secretion of copper-free Cp protein (apo-Cp). Cell surface biotinylation studies revealed that the state of PMC42-LA cell differentiation (functionality), and the level of extracellular copper, had no significant effect on the level of plasma membrane bound GPI-Cp. Quantitative real time PCR analyses determined that there was no significant (P > 0.05) difference in Cp mRNA levels across all copper conditions investigated (0, 5, 50 μM). However, there was a significant (P < 0.05) increase (∼2-fold) in Cp mRNA in both the lactating and suckled models in comparison to the resting model. Furthermore, the Cp mRNA increase in response to PMC42-LA differentiation corresponded with more secreted Cp protein, both apo and holo forms, indicating a link between function and Cp requirement. Our results provide significant insight on the regulation of Cp expression and secretion in lactation and copper incorporation into milk.
Language eng
DOI 10.1039/c6mt00086j
Field of Research 119999 Medical and Health Sciences not elsewhere classified
Socio Economic Objective 970106 Expanding Knowledge in the Biological Sciences
HERDC Research category C1 Refereed article in a scholarly journal
ERA Research output type C Journal article
Copyright notice ©2016, The Royal Society of Chemistry
Persistent URL http://hdl.handle.net/10536/DRO/DU:30085296

Connect to link resolver
 
Unless expressly stated otherwise, the copyright for items in DRO is owned by the author, with all rights reserved.

Versions
Version Filter Type
Citation counts: TR Web of Science Citation Count  Cited 1 times in TR Web of Science
Scopus Citation Count Cited 1 times in Scopus
Google Scholar Search Google Scholar
Access Statistics: 66 Abstract Views, 0 File Downloads  -  Detailed Statistics
Created: Thu, 18 Aug 2016, 12:28:45 EST

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.