Biol Reprod 2009 SSR Annual Meeting Abstracts
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 My Folders
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 Huang, J. L.
Right arrow Articles by Mead, R. A.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Huang, J. L.
Right arrow Articles by Mead, R. A.
Agricola
Right arrow Articles by Huang, J. L.
Right arrow Articles by Mead, R. A.

Biology of Reproduction, Vol 48, 647-654, Copyright © 1993 by Society for the Study of Reproduction

ARTICLES

Luteal protein secretion during preimplantation in the ferret

JL Huang, M Powell and RA Mead
Department of Biological Sciences, University of Idaho, Moscow 83843.

Ferret CL were collected on Days 5-11 of pregnancy or pseudopregnancy and incubated in McCoy's medium with radiolabeled amino acids to determine the ability of ferret CL to synthesize and secrete proteins during the preimplantation period. Products recovered from the medium were separated by one- and two-dimensional SDS-PAGE followed by fluorography and were quantified by densitometry. Selected secretory proteins were tentatively identified with specific antibodies on Western blots. Ferret CL synthesized and secreted a relatively large number of radiolabeled products. The predominant secretory proteins had molecular masses of 16, 22, 28, 32, 47, 68, and 185 kDa and were secreted at all stages of the preimplantation period. There were no qualitative changes in ferret luteal protein synthesis and secretion between Days 5-11 of pregnancy, and neither ovine prolactin (oPRL) nor dibutyryl cAMP (dcAMP) affected the pattern of protein secretion. However, oPRL (100 and 1000 ng/ml) increased incorporation of radiolabeled amino acids into luteal proteins during a 36-h incubation. The relative mobility of a 185-kDa radiolabeled product was identical to that of alpha 2-macroglobulin (alpha 2M) subunits. Antibody to human alpha 2M cross-reacted with a product (185 kDa) in ferret luteal extracts and culture medium, and the partially purified protein (185 kDa) inhibited trypsin activity. The major radiolabeled secretory protein (32 kDa) exhibited weak cross-reaction with antibody to a human tissue inhibitor of metalloproteinase (TIMP). This study demonstrates the wide range of proteinaceous secretory products of the ferret CL, two of which have been tentatively identified as protease inhibitors.


This article has been cited by other articles:


Home page
 Biol. Reprod.Home page
M. Sato, T. Tsubota, T. Komatsu, G. Watanabe, K. Taya, T. Murase, I. Kita, and T. Kudo
Changes in Sex Steroids, Gonadotropins, Prolactin, and Inhibin in Pregnant and Nonpregnant Japanese Black Bears (Ursus thibetanus japonicus)
Biol Reprod, October 1, 2001; 65(4): 1006 - 1013.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 1993 by the Society for the Study of Reproduction.