help button home button Endocrine Society JCEM
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
This Article
Right arrow Full Text (PDF)
Right arrow Submit a related Letter to the Editor
Right arrow Alert me when this article is cited
Right arrow Alert me when eLetters are posted
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 Request Copyright Permission
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Hatzoglou, A.
Right arrow Articles by Castanas, E.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Hatzoglou, A.
Right arrow Articles by Castanas, E.

Journal of Clinical Endocrinology & Metabolism, Vol 80, 418-423, Copyright © 1995 by Endocrine Society

ARTICLES

Identification and characterization of opioid-binding sites present in the Ishikawa human endometrial adenocarcinoma cell line

A Hatzoglou, A Gravanis, AN Margioris, E Zoumakis and E Castanas
Department of Experimental Endocrinology, Medical School, University of Crete, Greece.

Normal epithelial cells of human endometrium, and Ishikawa human endometrial adenocarcinoma cells (an in vitro model for the study of steroid hormone effects on human endometrium) have been found to express and secrete opioid peptides deriving from proenkephalin, prodynorphin, and proopiomelanocortin. These opioids may act locally, affecting the uterine tissues. In the present study, we identified and characterized opioid-binding sites on the Ishikawa cell line, producing evidence for the mechanism of local opioid action. We used an acid shock before the receptor assay to dissociate any endogenously bound peptide. The acidification improved specific binding by 2- to 4.5-fold. Characterization of opioid binding using different radiolabeled opioids and effectors has shown the existence of a low concentration of delta- sites (Kd, 6.20 nmol/L; 4,890 sites/cell), no mu-sites, low affinity kappa 1-sites (Kd, 10.8 nmol/L; 276,000 sites/cell), kappa 2-sites with high affinity for ethylketocyclazocine (Kd, approximately 1 nmol/L) and low affinity for diprenorphine (Kd, approximately 8 nmol/L) at a concentration of 93,000 sites/cell, and high affinity kappa 3-sites (Kd, 3.6 nmol/L; 77,000 sites/cell). In conclusion, our report characterizes opioid sites in a particular and homogeneous cell type of human endometrium, i.e. in epithelial cells. The coexistence of opioid sites and their endogenous ligands in the Ishikawa cell line makes these cells a good model for the study of autocrine/paracrine interactions of opioids in nonneural tissues.


This article has been cited by other articles:


Home page
 Mol Hum ReprodHome page
E. Chatzaki, A. Makrigiannakis, A.N. Margioris, E. Kouimtzoglou, and A. Gravanis
The Fas/FasL apoptotic pathway is involved in {kappa}-opioid-induced apoptosis of human endometrial stromal cells
Mol. Hum. Reprod., September 1, 2001; 7(9): 867 - 874.
[Abstract] [Full Text] [PDF]

Home page
 Mol Hum ReprodHome page
E. Chatzaki, A.N. Margioris, A. Makrigiannakis, E. Castanas, V. Georgoulias, and A. Gravanis
Kappa opioids and TGF{beta}1 interact in human endometrial cells
Mol. Hum. Reprod., July 1, 2000; 6(7): 602 - 609.
[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
Copyright © 1995 by The Endocrine Society