scholarly journals Substantial expression of luteinizing hormone-releasing hormone (LHRH) receptor type I in human uveal melanoma

Oncotarget ◽  
2013 ◽  
Vol 4 (10) ◽  
pp. 1721-1728 ◽  
Author(s):  
Andrea Treszl ◽  
Zita Steiber ◽  
Andrew V. Schally ◽  
Norman L Block ◽  
Balazs Dezso ◽  
...  
Keyword(s):  
Luteinizing Hormone ◽  
Uveal Melanoma ◽  
Receptor Type ◽  
Type I ◽  
Luteinizing Hormone Releasing Hormone ◽  
Releasing Hormone ◽  
Lhrh Receptor

scholarly journals Expression of Luteinizing Hormone-Releasing Hormone (LHRH) and Type-I LHRH Receptor in Transitional Cell Carcinoma Type of Human Bladder Cancer

Molecules ◽  
2021 ◽  
Vol 26 (5) ◽  
pp. 1253
Author(s):  
Zsuzsanna Szabó ◽  
Balázs Dezső ◽  
Klára Fodor ◽  
Krisztián Szegedi ◽  
Tibor Flaskó ◽  
...  
Keyword(s):  
Bladder Cancer ◽  
Luteinizing Hormone ◽  
Transitional Cell Carcinoma ◽  
Cell Carcinoma ◽  
Transitional Cell ◽  
Type I ◽  
Human Bladder ◽  
Luteinizing Hormone Releasing Hormone ◽  
Releasing Hormone ◽  
Lhrh Receptor

Bladder cancer (BC) is the tenth most frequently detected cancer in both sexes. Type-I luteinizing hormone-releasing hormone (LHRH) receptor (LHRH-R-I) is expressed not only in the pituitary, but also in several types of cancer disease. There are few data about LHRH-R-I expression in human BC. This study aimed to investigate the expression of LHRH and LHRH-R-I in the transitional cell carcinoma (TCC) type of human BC. RNA was extracted from 24 human bladder tumor specimens and three BC cell lines. RT-PCR was performed to detect mRNA for LHRH and LHRH-R-I. The protein of LHRH-R-I was further studied by immunohistochemistry (IHC), ligand competition assay, and Western Blot. PCR products of LHRH were found in 19 of 24 (79%) specimens and mRNA of LHRH-R-I was detected in 20 of 24 specimens (83%). Positive immunostaining for LHRH-R-I with different expression intensity was found in all samples examined, showing negative correlation with TCC grade. Radioligand binding studies also showed the presence of specific LHRH-R-I and high affinity binding of LHRH analogs. The high incidence of LHRH-R in BC suggests that it could serve as a molecular target for therapy of human BC with cytotoxic LHRH analogs or modern powerful antagonistic analogs of LHRH.

Discovery of a Novel, Potent, and Orally Active Nonpeptide Antagonist of the Human Luteinizing Hormone-Releasing Hormone (LHRH) Receptor

1998 ◽  
Vol 41 (22) ◽  
pp. 4190-4195 ◽  
Author(s):  
Nobuo Cho ◽  
Masataka Harada ◽  
Toshihiro Imaeda ◽  
Takashi Imada ◽  
Hirokazu Matsumoto ◽  
...  
Keyword(s):  
Luteinizing Hormone ◽  
Luteinizing Hormone Releasing Hormone ◽  
Releasing Hormone ◽  
Orally Active ◽  
Lhrh Receptor

scholarly journals Novel ligands for the affinity labelling of luteinizing hormone releasing hormone receptors

1989 ◽  
Vol 258 (3) ◽  
pp. 881-888
Author(s):  
S A Ogier ◽  
R Mitchell ◽  
C M Bladon
Keyword(s):  
Luteinizing Hormone ◽  
Hormone Receptors ◽  
Specific Binding ◽  
Receptor Site ◽  
Covalent Attachment ◽  
Scatchard Analysis ◽  
Luteinizing Hormone Releasing Hormone ◽  
Releasing Hormone ◽  
Specific Binding Ratio ◽  
Lhrh Receptor

A number of novel luteinizing hormone releasing hormone (LHRH) analogues incorporating biotin together with potential covalent attachment sites have been synthesized. Those based on the des-Gly10-[D-Lys6]-LHRH ethylamide peptide backbone resulted in the most useful characteristics of binding to the LHRH receptor in rat anterior pituitary gland membranes. Of these, des-Gly10-[biotinyl-aminoethylglycyl-D-Lys6]-LHRH ethylamide (XBAL) gave the best specific: non-specific binding ratio, with 44 +/- 6% (+/- S.E.M.) of total binding being specific with a Kd of 131 +/- 16 pM (+/- S.E.M., n = 4) as determined by Scatchard analysis. Two methods have been used to covalently crosslink these analogues with the LHRH receptor; photoaffinity labelling and the use of homobifunctional N-hydroxysuccinimide ester crosslinkers. The photoaffinity analogues gave poor specific: non-specific binding ratios. Of the chemical crosslinkers tested, ethylene glycolbis(succinimidylsuccinate) (EGS) was found to be the most efficient at covalently linking the 125I-XBAL bound to the LHRH receptor site. At an EGS concentration of 5 mM, 23 +/- 3% (+/- S.E.M.) of the specific binding of 125I-XBAL was covalently crosslinked.

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