Biol Reprod Lalor Postdoctoral Fellowships -- Application Deadline January 15, 2009
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

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
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Kliem, A.
Right arrow Articles by Fischer, B.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Kliem, A.
Right arrow Articles by Fischer, B.
Agricola
Right arrow Articles by Kliem, A.
Right arrow Articles by Fischer, B.

Biology of Reproduction, Vol 58, 1367-1371, Copyright © 1998 by Society for the Study of Reproduction

ARTICLES

Only a truncated epidermal growth factor receptor protein is present in porcine endometrium [In Process Citation]

A Kliem, F Tetens, H Niemann and B Fischer
Department of Anatomy and Cell Biology, Martin Luther University Faculty of Medicine, Halle, Germany.

The epidermal growth factor receptor (EGF-R) is a 170-kDa transmembrane protein, of which a truncated 100-kDa form (trEGF-R) lacking the cytoplasmic and the transmembrane domains, and an oncogenic 68-kDa form (v-erb) lacking the extracellular domain have been described. The trEGF- R is secreted and not able to transmit signals into the cell. Growth factors of the EGF family have been shown in porcine uterine fluids and blastocyst. Employing differential immunohistochemistry, we found the extracellular domain, but not the cytoplasmic domain, of the EGF-R in porcine endometrium on Days 9-11 of pregnancy. Blastocysts from Days 9 to 11 post coitum (p.c.) were positive for both antibodies, indicating the presence of the full-size receptor. Western Blotting of endometrial protein resulted in a 100-kDa band, but no 170-kDa band. No evidence for a coexpression of the 170- or 68-kDa forms of the receptor was found. ELISA analysis demonstrated trEGF-R in porcine uterine flushings. We conclude that 1) the trEGF-R is the only EGF-R form present in porcine endometrium, and 2) growth factors of the EGF family in porcine uterine fluids can exert their function via the EGF-R only on blastocysts, not on the endometrium.




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 1998 by the Society for the Study of Reproduction.