Biol Reprod Track the topics, authors and articles important to you
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

BOR - Papers in Press, published online ahead of print July 11, 2007.
Biol Reprod 2007, 10.1095/biolreprod.107.061747
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow [Supplemental Tables]
Right arrow All Versions of this Article:
77/4/648    most recent
biolreprod.107.061747v1
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
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
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Robinson, N. J
Right arrow Articles by Aplin, J. D
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Robinson, N. J
Right arrow Articles by Aplin, J. D
Agricola
Right arrow Articles by Robinson, N. J
Right arrow Articles by Aplin, J. D
BIOLOGY OF REPRODUCTION 77, 648–657 (2007)
DOI: 10.1095/biolreprod.107.061747
© 2007 by the Society for the Study of Reproduction, Inc.

A Role for Tissue Transglutaminase in Stabilization of Membrane-Cytoskeletal Particles Shed from the Human Placenta

Nicola J Robinson , Philip N Baker , Carolyn J.P Jones , and John D Aplin  1

Maternal and Fetal Health Research Centre, Division of Human Development, University of Manchester, St. Mary's Hospital, Manchester M13 0JH, United Kingdom

ABSTRACT

Tissue transglutaminase (TGM2; also known as TG2 or tTG) localizes to the syncytial microvillous membrane (MVM) of the human placenta, the primary interface between maternal and fetal tissue. To identify TGM2 substrates in the MVM, membrane vesicles were prepared and labeled with biotinylated acyl donor or acceptor probes. Biotinylated species were selected on an avidin affinity matrix and identified by mass spectrometry of tryptic peptides. The most abundant were cytoskeletal (actin, tubulin, and cytokeratin) and membrane-associated (annexins, integrins, and placental alkaline phosphatase) proteins. During pregnancy, apoptotic particulate material, the end product of the trophoblast life cycle, is shed from the MVM into maternal circulation. Shed material was isolated from primary trophoblast cultures in which syncytial-like masses develop by fusion. A substantial fraction of actin in the particles was in the form of covalent polymeric aggregates, in contrast to cellular actin, which dissociated completely into monomer in SDS-PAGE. When cells were cultured in the presence of transglutaminase inhibitors, actin in the shed particles remained exclusively in monomeric form, and a reduction in trophoblast intercellular fusion and differentiation was observed. These findings suggest that transglutaminase-mediated cross-linking stabilizes the particulate material shed from the placenta.

actin, cytoskeleton, immunology, placenta, plasma membrane, pregnancy, shedding, syncytiotrophoblast, tissue transglutaminase, trophoblast

Correspondence: 1John Aplin, Division of Human Development, University of Manchester, St. Mary's Hospital, Research Floor Room 74, Hathersage Rd., Manchester M13 0JH, U.K. FAX: 44 0 161 276 6134; e-mail: john.aplin{at}manchester.ac.uk






HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 2007 by the Society for the Study of Reproduction.