scholarly journals Naturally Occurring Mutations of the Luteinizing-Hormone Receptor: Lessons Learned about Reproductive Physiology and G Protein–Coupled Receptors

1999 ◽  
Vol 65 (4) ◽  
pp. 949-958 ◽  
Author(s):  
Ana Claudia Latronico ◽  
Deborah L. Segaloff
Keyword(s):  
Luteinizing Hormone ◽  
G Protein ◽  
Hormone Receptor ◽  
Lessons Learned ◽  
G Protein Coupled Receptors ◽  
Reproductive Physiology ◽  
Luteinizing Hormone Receptor ◽  
Naturally Occurring ◽  
G Protein Coupled

Polyoxometalates function as indirect activators of a G protein-coupled receptor

Metallomics ◽  
2020 ◽  
Vol 12 (7) ◽  
pp. 1044-1061 ◽  
Author(s):  
Duaa Althumairy ◽  
Kahoana Postal ◽  
B. George Barisas ◽  
Giovana G. Nunes ◽  
Deborah A. Roess ◽  
...  
Keyword(s):  
Luteinizing Hormone ◽  
G Protein ◽  
Hormone Receptor ◽  
Luteinizing Hormone Receptor ◽  
G Protein Coupled Receptor ◽  
G Protein Coupled

A series of multivalent polyoxovanadates were found to activate signaling of a G protein coupled receptor, the luteinizing hormone receptor.

scholarly journals Rescue of defective G protein–coupled receptor function in vivo by intermolecular cooperation

2010 ◽  
Vol 107 (5) ◽  
pp. 2319-2324 ◽  
Author(s):  
Adolfo Rivero-Müller ◽  
Yen-Yin Chou ◽  
Inhae Ji ◽  
Svetlana Lajic ◽  
Aylin C. Hanyaloglu ◽  
...  
Keyword(s):  
G Protein ◽  
G Protein Coupled Receptors ◽  
Luteinizing Hormone Receptor ◽  
Wild Type ◽  
Gpcr Signaling ◽  
Physiological Relevance ◽  
Biosynthesis Activation ◽  
Mutant Receptors ◽  
G Protein Coupled

G protein–coupled receptors (GPCRs) are ubiquitous mediators of signaling of hormones, neurotransmitters, and sensing. The old dogma is that a one ligand/one receptor complex constitutes the functional unit of GPCR signaling. However, there is mounting evidence that some GPCRs form dimers or oligomers during their biosynthesis, activation, inactivation, and/or internalization. This evidence has been obtained exclusively from cell culture experiments, and proof for the physiological significance of GPCR di/oligomerization in vivo is still missing. Using the mouse luteinizing hormone receptor (LHR) as a model GPCR, we demonstrate that transgenic mice coexpressing binding-deficient and signaling-deficient forms of LHR can reestablish normal LH actions through intermolecular functional complementation of the mutant receptors in the absence of functional wild-type receptors. These results provide compelling in vivo evidence for the physiological relevance of intermolecular cooperation in GPCR signaling.

scholarly journals Identification and Functional Analysis of G Protein-Coupled Receptors in 20-Hydroxyecdysone Signaling From the Helicoverpa armigera Genome

2021 ◽  
Vol 9 ◽  
Author(s):  
Yan-Li Li ◽  
Yan-Xue Li ◽  
Xiao-Pei Wang ◽  
Xin-Le Kang ◽  
Ke-Qin Guo ◽  
...  
Keyword(s):  
G Protein ◽  
Helicoverpa Armigera ◽  
Hormone Receptor ◽  
G Protein Coupled Receptors ◽  
Membrane Receptors ◽  
Pest Species ◽  
Metamorphic Stage ◽  
Adipokinetic Hormone ◽  
Helicoverpa Armígera ◽  
G Protein Coupled

G protein-coupled receptors (GPCRs) are the largest family of membrane receptors in animals and humans, which transmit various signals from the extracellular environment into cells. Studies have reported that several GPCRs transmit the same signal; however, the mechanism is unclear. In the present study, we identified all 122 classical GPCRs from the genome of Helicoverpa armigera, a lepidopteran pest species. Twenty-four GPCRs were identified as upregulated at the metamorphic stage by comparing the transcriptomes of the midgut at the metamorphic and feeding stages. Nine of them were confirmed to be upregulated at the metamorphic stage. RNA interference in larvae revealed the prolactin-releasing peptide receptor (PRRPR), smoothened (SMO), adipokinetic hormone receptor (AKHR), and 5-hydroxytryptamine receptor (HTR) are involved in steroid hormone 20-hydroxyecdysone (20E)-promoted pupation. Frizzled 7 (FZD7) is involved in growth, while tachykinin-like peptides receptor 86C (TKR86C) had no effect on growth and pupation. Via these GPCRs, 20E regulated the expression of different genes, respectively, including Pten (encoding phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase), FoxO (encoding forkhead box O), BrZ7 (encoding broad isoform Z7), Kr-h1 (encoding Krüppel homolog 1), Wnt (encoding Wingless/Integrated) and cMyc, with hormone receptor 3 (HHR3) as their common regulating target. PRRPR was identified as a new 20E cell membrane receptor using a binding assay. These data suggested that 20E, via different GPCRs, regulates different gene expression to integrate growth and development.

scholarly journals Expression and Purification of the Extracellular Domain of Luteinizing Hormone Receptor From Ovis Aries Testicle

2021 ◽  
Author(s):  
Jose Luis Villalpando-Aguilar ◽  
Itzel López-Rosas ◽  
Arnulfo Montero-Pardo ◽  
Elisa Irene Azuara-Liceaga ◽  
Javier de Jesus Valencia-Méndez ◽  
...  
Keyword(s):  
Luteinizing Hormone ◽  
Hormone Receptor ◽  
Extracellular Domain ◽  
Insoluble Fraction ◽  
Ovis Aries ◽  
Luteinizing Hormone Receptor ◽  
New Drugs ◽  
E Coli ◽  
Fertility Disorders ◽  
G Protein Coupled

Abstract The luteinizing hormone receptor (LHR) is a glycoprotein member of the G protein-coupled receptor superfamily. Physiologically, this receptor participates in corpus luteum formation and ovulation in females. In males, it acts in testosterone synthesis and spermatogenesis and is involved in some fertility disorders. RNA was extracted from Ovis aries testicles, and the corresponding cDNA was synthesized to amplify the lhr gene, termed lhr-bed here, consisting of 762 bp that encodes 273 amino acids of the extracellular domain of LHR. Thus, the lhr-bed was cloned into pJET1.2/blunt, subcloned into the pCOLD II expression vector and finally transformed into E. coli BL21 cells. Since the induced rLHR-Bed protein was found in the insoluble fraction, the purification protocol was modified as follows: induction at 25°C, denaturing conditions (8 M UREA and 0.1% CHAPS) and refolding in the column to increase solubility. The rLHR-Bed expression was corroborated by western blotting and mass spectrometry (MS) analysis. This successful method to obtain the recombinant LHR extracellular domain yields 0.2 mg/L of the protein with approximately 90% purity from a single chromatographic purification step. The present approach demonstrates the feasibility of obtaining large quantities of rLHR-Bed. This might be useful to accomplish future studies regarding the structure and functional analysis of the binding interplay with its ligand luteinizing hormone and its isoforms. Additionally, this biotechnological strategy might be used to improve and to develop new drugs for the treatment of reproductive disorders and might also be applied to species reproduction in the livestock industry.

A Prospective Cross-Screening Study on G-Protein-Coupled Receptors: Lessons Learned in Virtual Compound Library Design

2012 ◽  
Vol 55 (11) ◽  
pp. 5311-5325 ◽  
Author(s):  
Marijn P. A. Sanders ◽  
Luc Roumen ◽  
Eelke van der Horst ◽  
J. Robert Lane ◽  
Henry F. Vischer ◽  
...  
Keyword(s):  
G Protein ◽  
Lessons Learned ◽  
G Protein Coupled Receptors ◽  
Library Design ◽  
Compound Library ◽  
Screening Study ◽  
G Protein Coupled
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