help button home button Am J Pathol ASIP MEMBERSHIP
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS

This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Purchase Article
Right arrow View Shopping Cart
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Meyer zu Schwabedissen, H. E.U.
Right arrow Articles by Jedlitschky, G.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Meyer zu Schwabedissen, H. E.U.
Right arrow Articles by Jedlitschky, G.
(American Journal of Pathology. 2005;166:39-48.)
© 2005 American Society for Investigative Pathology

Expression, Localization, and Function of MRP5 (ABCC5), a Transporter for Cyclic Nucleotides, in Human Placenta and Cultured Human Trophoblasts

Effects of Gestational Age and Cellular Differentiation

Henriette E.U. Meyer zu Schwabedissen*, Markus Grube*, Björn Heydrich*, Knud Linnemann{dagger}, Christoph Fusch{dagger}, Heyo K. Kroemer* and Gabriele Jedlitschky*

From the Department of Pharmacology,* Peter Holtz Research Center of Pharmacology and Experimental Therapeutics, and the Department of Neonatology,{dagger} Ernst-Moritz-Arndt-University, Greifswald, Germany

The placenta functions both as site for nutrition and protection of the fetus. Transport proteins, including members of the multidrug resistance protein (MRP)/ABCC subfamily, have been recognized to contribute to the latter function. MRP5 (ABCC5) was identified as transmembrane transport protein for cyclic nucleotides, especially 3',5'-cyclic GMP (cGMP), indicating an additional role in signal transduction and a potential role in placenta development. We therefore studied expression, localization, and function of MRP5 in placenta of different gestational ages. Quantitative real-time polymerase chain reaction revealed expression of MRP5 in all 60 samples from pre-term and term placenta, with a decreasing mean expression with gestational age (MRP5/18S-ratio x 1000; < 32 weeks: 2.91 ± 0.73, n = 15; 32 to 37 weeks: 2.10 ± 0.87, n = 15; > 37 weeks: 0.46 ± 0.08, n = 30; P < 0.01). Immunofluorescence microscopy with an anti-MRP5 antibody indicated localization of MRP5 preferentially in the basal membrane of syncytiotrophoblasts and in and around fetal vessels. ATP-dependent [3H]cGMP transport as evidence for MRP5 function could be demonstrated in isolated basal membrane vesicles. Moreover, the influence of cellular differentiation on MRP5 expression was studied in isolated trophoblasts, revealing an increase of the MRP5 expression in parallel with the hCG production (MRP5/18S-ratio x 1000 was 2.4 ± 0.5 at day 5 of culture and 1.45 ± 0.5 at day 0 of culture, n = 3 preparations, significant difference with P < 0.05). In conclusion, MRP5 expression depends on gestational age and varies throughout the differentiation process. In view of the important role of cGMP for cellular differentiation, MRP5 may play a role in placental development in context with a specific need for cellular cGMP export.





This article has been cited by other articles:


Home page
Drug Metab. Dispos.Home page
L. M. Aleksunes, Y. Cui, and C. D. Klaassen
Prominent Expression of Xenobiotic Efflux Transporters in Mouse Extraembryonic Fetal Membranes Compared with Placenta
Drug Metab. Dispos., September 1, 2008; 36(9): 1960 - 1970.
[Abstract] [Full Text] [PDF]


Home page
Drug Metab. Dispos.Home page
M. Grube, S. Reuther, H. Meyer zu Schwabedissen, K. Kock, K. Draber, C. A. Ritter, C. Fusch, G. Jedlitschky, and H. K. Kroemer
Organic Anion Transporting Polypeptide 2B1 and Breast Cancer Resistance Protein Interact in the Transepithelial Transport of Steroid Sulfates in Human Placenta
Drug Metab. Dispos., January 1, 2007; 35(1): 30 - 35.
[Abstract] [Full Text] [PDF]


Home page
Drug Metab. Dispos.Home page
H. E. M. zu Schwabedissen, M. Grube, A. Dreisbach, G. Jedlitschky, K. Meissner, K. Linnemann, C. Fusch, C. A. Ritter, U. Volker, and H. K. Kroemer
EPIDERMAL GROWTH FACTOR-MEDIATED ACTIVATION OF THE MAP KINASE CASCADE RESULTS IN ALTERED EXPRESSION AND FUNCTION OF ABCG2 (BCRP)
Drug Metab. Dispos., April 1, 2006; 34(4): 524 - 533.
[Abstract] [Full Text] [PDF]


Home page
Reproductive SciencesHome page
X. Bai, H. A. Lacey, S. L. Greenwood, P. N. Baker, M. A. Turner, C. P. Sibley, and G. K. Fyfe
TASK Channel Expression in Human Placenta and Cytotrophoblast Cells
Reproductive Sciences, January 1, 2006; 13(1): 30 - 39.
[Abstract] [PDF]


Home page
Drug Metab. Dispos.Home page
H. E. Meyer zu Schwabedissen, G. Jedlitschky, M. Gratz, S. Haenisch, K. Linnemann, C. Fusch, I. Cascorbi, and H. K. Kroemer
VARIABLE EXPRESSION OF MRP2 (ABCC2) IN HUMAN PLACENTA: INFLUENCE OF GESTATIONAL AGE AND CELLULAR DIFFERENTIATION
Drug Metab. Dispos., July 1, 2005; 33(7): 896 - 904.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 2005 by the American Society for Investigative Pathology.