| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
Journal of Clinical Endocrinology & Metabolism, Vol 64, 433-440, Copyright © 1987 by Endocrine Society
ARTICLES |
RI Cruz, DM Anderson, EG Armstrong and WR Moyle
When hCG adsorbs to surfaces, including membranes from tissues that lack specific hCG receptors, it adsorbs with a particular orientation. Some sites on the alpha- and beta-subunits project away from the surface and can be detected with radiolabeled monoclonal antibodies. Other epitopes, which are located on a region on the hormone that presumably contacts the surface, lose their ability to bind antibody. Using antibodies specific for epitopes on hCG which remain exposed and can be detected when the hormone is adsorbed to rat brain homogenates, we found hCG or closely related substances bound to progestational decidual tissues. Immunologically reactive material adsorbed to the decidual tissue increased and decreased in parallel with the serum levels of hCG throughout pregnancy. Binding of labeled monoclonal antibody to substances similar or identical to hCG in other tissues, including placenta and fetal lung, but not red cells, also was identified. Unlike material adsorbed to decidual tissues, receptor- bound hCG was not recognized by any of our alpha-subunit-specific antibodies. This finding suggests either that the adsorbed hormone has a different orientation than receptor-bound hormone or that the adsorbed hormone has dissociated into subunits. These studies represent the first detection of nonreceptor binding of hCG or related molecules to tissues lacking receptors or presumed not to synthesize the hormone. The role of nonreceptor-bound hCG, if any, is unknown. Other than its effects on stimulation of luteal steroidogenesis during early pregnancy, the role of hCG during most of pregnancy has not been determined. Conceivably, the nonreceptor binding we identified is related to a role for hCG in pregnancy that is not associated with an action on the ovarian LH receptor.
This article has been cited by other articles:
![]() |
Y. Xing, C. Williams, R. K. Campbell, S. Cook, M. Knoppers, T. Addona, V. Altarocca, and W. R. Moyle Threading of a glycosylated protein loop through a protein hole: Implications for combination of human chorionic gonadotropin subunits Protein Sci., February 1, 2001; 10(2): 226 - 235. [Abstract] [Full Text] |
||||
![]() |
L. Cosowsky, W. Lin, Y. Han, M. P. Bernard, RobertK. Campbell, and WilliamR. Moyle Influence of Subunit Interactions on Lutropin Specificity. IMPLICATIONS FOR STUDIES OF GLYCOPROTEIN HORMONE FUNCTION J. Biol. Chem., February 7, 1997; 272(6): 3309 - 3314. [Abstract] [Full Text] [PDF] |
||||
![]() |
L. Cosowsky, S. N. V. Rao, G. J. Macdonald, H. Papkoff, R. K. Campbell, and W. R. Moyle The Groove between the alpha- and beta-Subunits of Hormones with Lutropin (LH) Activity Appears to Contact the LH Receptor, and Its Conformation Is Changed during Hormone Binding J. Biol. Chem., August 25, 1995; 270(34): 20011 - 20019. [Abstract] [Full Text] [PDF] |
||||
![]() |
W. R. Moyle, R. K. Campbell, S. N. V. Rao, N. G. Ayad, M. P. Bernard, Y. Han, and Y. Wang Model of Human Chorionic Gonadotropin and Lutropin Receptor Interaction That Explains Signal Transduction of the Glycoprotein Hormones J. Biol. Chem., August 25, 1995; 270(34): 20020 - 20031. [Abstract] [Full Text] [PDF] |
||||
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
| Endocrinology | Endocrine Reviews | J. Clin. End. & Metab. |
| Molecular Endocrinology | Recent Prog. Horm. Res. | All Endocrine Journals |