Localization of plasma membrane and secretory calcium pumps in the mammary gland

被引：72

作者：

Faddy, Helen M. ^{[1
]}

Smart, Chanel E. ^{[2
]}

Xu, Ren ^{[3
]}

Lee, Genee Y. ^{[3
]}

Kenny, Paraic A. ^{[3
]}

Feng, Mingye ^{[4
]}

Rao, Rajini ^{[4
]}

Brown, Melissa A. ^{[2
]}

Bissell, Mina J. ^{[3
]}

Roberts-Thomson, Sarah J. ^{[1
]}

Monteith, Gregory R. ^{[1
]}

机构：

[1] Univ Queensland, Sch Pharm, Brisbane, Qld 4072, Australia

[2] Univ Queensland, Sch Mol & Microbial Sci, Brisbane, Qld 4072, Australia

[3] Univ Calif Berkeley, Lawrence Berkeley Natl Lab, Div Life Sci, Berkeley, CA USA

[4] Johns Hopkins Univ, Sch Med, Dept Physiol, Baltimore, MD USA

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 2008年 / 369卷 / 03期

关键词：

calcium; PMCA1; SPCA1; PMCA2; SPCA2; mouse; mammary gland; 3D mammary culture; milk;

D O I：

10.1016/j.bbrc.2008.03.003

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Until recently the mechanism for the enrichment of milk with calcium was thought to be almost entirely via the secretory pathway. However, recent studies suggest that a plasma membrane calcium ATPase, PMCA2, is the primary mechanism for calcium transport into milk, highlighting a major role for apical calcium transport. We compared the expression of the recently identified secretory calcium ATPase, SPCA2, and SPCA1, in the mouse mammary gland during development. SPCA2 levels increased over 35-fold during lactation with expression localized to luminal secretory cells, while SPCA1 increased only a modest 2-fold and was expressed throughout the cells of the mammary gland. We also observed major differences in the localization of PMCA2 and PMCA1. Our studies highlight the likely specific roles of PMCA2 and SPCA2 in lactation and indicate that calcium transport into milk is a complex interplay between apical and secretory pathways. (c) 2008 Elsevier Inc. All rights reserved.

引用

页码：977 / 981

页数：5

共 26 条

[1] Regulation of Ca2+ mobilization by prolactin in mammary gland cells:: Possible role of secretory pathway Ca2+-ATPase type 2 [J].

Anantamongkol, Utchariya ;

Takemura, Haruo ;

Suthiphongchai, Tuangporn ;

Krishnamra, Nateetip ;

Horio, Yoshiyuki .

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 2007, 352 (02) :537-542

[2]

BARCELLOSHOFF MH, 1989, DEVELOPMENT, V105, P223

[3] Calcium signalling: Dynamics, homeostasis and remodelling [J].

Berridge, MJ ;

Bootman, MD ;

Roderick, HL .

NATURE REVIEWS MOLECULAR CELL BIOLOGY, 2003, 4 (07) :517-529

[4] Calcium signaling: A tale for all seasons [J].

Carafoli, E .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2002, 99 (03) :1115-1122

[5]

Desprez Pierre-Yves, 1993, Molecular and Cellular Differentiation, V1, P99

[6]

DESPREZ PY, 1995, MOL CELL BIOL, V15, P3398

[7] Dissection of the functional differences between human secretory pathway Ca2+/Mn2+-ATPase (SPCA) 1 and 2 isoenzymes by steady-state and transient kinetic analyses [J].

Dode, L ;

Andersen, JP ;

Vanoevelen, J ;

Raeymaekers, L ;

Missiaen, L ;

Vilsen, B ;

Wuytack, F .

JOURNAL OF BIOLOGICAL CHEMISTRY, 2006, 281 (06) :3182-3189

[8] The galactosyltransferase family [J].

Hennet, T .

CELLULAR AND MOLECULAR LIFE SCIENCES, 2002, 59 (07) :1081-1095

[9] Balance and hearing deficits in mice with a null mutation in the gene encoding plasma membrane Ca2+-ATPase isoform 2 [J].

Kozel, PJ ;

Friedman, RA ;

Erway, LC ;

Yamoah, EN ;

Liu, LH ;

Riddle, T ;

Duffy, JJ ;

Doetschman, T ;

Miller, ML ;

Cardell, EL ;

Shull, GE .

JOURNAL OF BIOLOGICAL CHEMISTRY, 1998, 273 (30) :18693-18696

[10] Three-dimensional culture models of normal and malignant breast epithelial cells [J].

Lee, Genee Y. ;

Kenny, Paraic A. ;

Lee, Eva H. ;

Bissell, Mina J. .

NATURE METHODS, 2007, 4 (04) :359-365

← 1 2 3 →