Titrating Luteinizing Hormone Replacement to Sustain the Structure and Function of the Corpus Luteum after Gonadotropin-Releasing Hormone Antagonist Treatment in Rhesus Monkeys

1999 ◽  
Vol 84 (1) ◽  
pp. 342-349 ◽  
Author(s):  
D. M. Duffy
1997 ◽  
Vol 77 (4) ◽  
pp. 727-730 ◽  
Author(s):  
E. Rubianes ◽  
T. de Castro ◽  
R. Ungerfeld ◽  
A. Meikle ◽  
A. Rivero

To study the ovarian response of seasonally anestrous Corriedale ewes to a gonadotropin releasing hormone challenge, daily transrectal ultrasonography or laparotomy were performed and luteinizing hormone and progesterone profiles were determined. Of the responding ewes (8/17), three ovulated and formed a healthy corpus luteum and five formed large luteinized follicular cysts that secreted low progesterone levels for 2 to 3 d. Therefore, the study of progesterone profiles alone could lead to erroneous interpretations of the ovarian response to GnRH challenge in sheep. Key words: GnRH, progesterone, ovary, anestrous, ultrasonography, ewes


2020 ◽  
Vol 21 (21) ◽  
pp. 7900
Author(s):  
Lorraine Peacey ◽  
Charlotte Peacey ◽  
Adele Gutzinger ◽  
Christopher E. Jones

In vertebrate reproductive biology copper can influence peptide and protein function both in the pituitary and in the gonads. In the pituitary, copper binds to the key reproductive peptides gonadotropin-releasing hormone I (GnRH-I) and neurokinin B, to modify their structure and function, and in the male gonads, copper plays a role in testosterone production, sperm morphology and, thus, fertility. In addition to GnRH-I, most vertebrates express a second isoform, GnRH-II. GnRH-II can promote testosterone release in some species and has other non-reproductive roles. The primary sequence of GnRH-II has remained largely invariant over millennia, and it is considered the ancestral GnRH peptide in vertebrates. In this work, we use a range of spectroscopic techniques to show that, like GnRH-I, GnRH-II can bind copper. Phylogenetic analysis shows that the proposed copper-binding ligands are retained in GnRH-II peptides from all vertebrates, suggesting that copper-binding is an ancient feature of GnRH peptides.


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