Biol Reprod Track the topics, authors and articles important to you
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 DARGA, N. C.
Right arrow Articles by REICHERT, L. E.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by DARGA, N. C.
Right arrow Articles by REICHERT, L. E., JR.
Agricola
Right arrow Articles by DARGA, N. C.
Right arrow Articles by REICHERT, L. E.

Biology of Reproduction, Vol 19, 235-241, Copyright © 1978 by Society for the Study of Reproduction

Some Properties of the Interaction of Follicle Stimulating Hormone with Bovine Granulosa Cells and Its Inhibition by Follicular Fluid

NINA C. DARGA 1, and LEO E. REICHERT JR. 1

1 Department of Biochemistry, Emory University School of Medicine, Atlanta, Georgia 30322


We have studied the binding of radiolabeled human follicle stimulating hormone (125I-hFSH) to bovine granulosa cells collected from follicles at varying stages of maturation as judged by size. Specific binding was time and temperature dependent, reaching its maximum after 2 h of incubation at 37°C and pH 7.5. Specific binding was saturable with respect to 125I-hFSH and receptor concentrations and could be inhibited by unlabeled purified human FSH (25 ng = 50% inhibition) and bovine FSH (35 ng = 50% inhibition), but not by large (5000 ng) amounts of bovine LH, TSH, GH, prolactin or human ACTH. Specific binding of 125I-hFSH to granulosa cells from large follicles (>6 mm) was at least as great as to granulosa cells from medium (3-6 mm) and small (<3 mm) follicles.

Fluid from bovine follicles of all sizes significantly inhibited binding of 125I-hFSH to granulosa cells in a dose related manner. The amount of FSH binding inhibition (FSH-BI)/ml of fluid from large follicles was approximately 2-fold greater than that from small follicles and contained approximately 100-fold higher levels of FSH-BI activity than did small follicles by virtue of increased fluid volume. FSH-BI activity was markedly reduced by dialysis, passing a membrane having a molecular weight retention of 8000 daltons and could be detected in the dialysate. The chemical nature of the dialyzable follicular fluid FSH-BI is not known, although it does not seem to be adsorbed by charcoal or soluble in diethyl ether.

 Submitted on December 8, 1977
Accepted on January 24, 1978




This article has been cited by other articles:


Home page
 J. Histochem. Cytochem.Home page
S. S. Chitnis, R. M. Navlakhe, G. C. Shinde, S. J. Barve, S. D'Souza, S. D. Mahale, and T. D. Nandedkar
Granulosa Cell Apoptosis Induced by a Novel FSH Binding Inhibitory Peptide From Human Ovarian Follicular Fluid
J. Histochem. Cytochem., November 1, 2008; 56(11): 961 - 968.
[Abstract] [Full Text] [PDF]

Home page
 Endocr. Rev.Home page
M. Simoni, J. Gromoll, and E. Nieschlag
The Follicle-Stimulating Hormone Receptor: Biochemistry, Molecular Biology, Physiology, and Pathophysiology
Endocr. Rev., December 1, 1997; 18(6): 739 - 773.
[Abstract] [Full Text]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 1978 by the Society for the Study of Reproduction.