AJP - Endo Watch the video to learn how APS reaches out to developing nations.
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

Am J Physiol Endocrinol Metab 267: E68-E76, 1994;
0193-1849/94 $5.00
This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
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
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Avissar, N.
Right arrow Articles by Cohen, H. J.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Avissar, N.
Right arrow Articles by Cohen, H. J.

AJP - Endocrinology and Metabolism, Vol 267, Issue 1 E68-E76, Copyright © 1994 by American Physiological Society

ARTICLES

Human placenta makes extracellular glutathione peroxidase and secretes it into maternal circulation

N. Avissar, C. Eisenmann, J. G. Breen, S. Horowitz, R. K. Miller and H. J. Cohen
Department of Pediatrics, University of Rochester Medical Center 14642.

Extracellular glutathione peroxidase (eGPX) is a selenoglycoprotein distinct from cellular glutathione peroxidase (cGPX). The cDNA for eGPX has recently been cloned from human placenta. To determine whether human placenta makes both cGPX and eGPX and secretes eGPX, we used specific immunoprecipitations of 75Se metabolically labeled proteins from full-term placental explants in culture and perfused placental lobules. Placental explants and metabolically active, dually perfused placental lobules synthesized and contained both cGPX and eGPX and secreted eGPX. Perfused tissue secreted eGPX into the maternal but not into the fetal perfusate. In situ hybridizations using antisense and sense eGPX riboprobes were performed on sections of first-, second-, and third-trimester placentas. In the first-trimester placenta, transcripts were localized predominantly to cytotrophoblast cells, whereas in the full-term placenta syncytiotrophoblast cells and stromal cells but not fetal endothelial cells expressed eGPX mRNA. It is concluded that human placenta synthesizes both cGPX and eGPX and secretes eGPX into the maternal circulation, consistent with the location of the eGPX mRNA.


This article has been cited by other articles:


Home page
 Am. J. Physiol. Gastrointest. Liver Physiol.Home page
D. M. Tham, J. C. Whitin, K. K. Kim, S. X. Zhu, and H. J. Cohen
Expression of extracellular glutathione peroxidase in human and mouse gastrointestinal tract
Am J Physiol Gastrointest Liver Physiol, December 1, 1998; 275(6): G1463 - G1471.
[Abstract] [Full Text] [PDF]

Home page
 Am. J. Respir. Cell Mol. Bio.Home page
M. Salathe, M. Holderby, R. Forteza, W. M. Abraham, A. Wanner, and G. E. Conner
Isolation and Characterization of a Peroxidase from the Airway
Am. J. Respir. Cell Mol. Biol., July 1, 1997; 17(1): 97 - 105.
[Abstract] [Full Text]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Visit Other APS Journals Online