scholarly journals Glycoprotein Hormone Receptor Knockdown Leads to Reduced Reproductive Success in Male Aedes aegypti

2019 ◽  
Vol 10 ◽  
Author(s):  
David A. Rocco ◽  
Ana S. G. Garcia ◽  
Elton L. Scudeler ◽  
Daniela C. dos Santos ◽  
Rafael H. Nóbrega ◽  
...  
Keyword(s):  
Reproductive Success ◽  
Aedes Aegypti ◽  
Hormone Receptor ◽  
Glycoprotein Hormone ◽  
Glycoprotein Hormone Receptor

Structures of full-length glycoprotein hormone receptor signalling complexes

Nature ◽  
2021 ◽  
Author(s):  
Jia Duan ◽  
Peiyu Xu ◽  
Xi Cheng ◽  
Chunyou Mao ◽  
Tristan Croll ◽  
...  
Keyword(s):  
Hormone Receptor ◽  
Full Length ◽  
Glycoprotein Hormone ◽  
Receptor Signalling ◽  
Glycoprotein Hormone Receptor

scholarly journals A sea lamprey glycoprotein hormone receptor similar with gnathostome thyrotropin hormone receptor

2008 ◽  
Vol 41 (4) ◽  
pp. 219-228 ◽  
Author(s):  
Mihael Freamat ◽  
Stacia A Sower
Keyword(s):  
Hormone Receptor ◽  
Hormone Receptors ◽  
Functional Divergence ◽  
Sea Lamprey ◽  
Glycoprotein Hormone ◽  
Receptor System ◽  
Glycoprotein Hormone Receptors ◽  
Molecular Phylogenetic ◽  
Synthetic Ligand ◽  
Glycoprotein Hormone Receptor

The specificity of the vertebrate hypothalamic–pituitary–gonadal and hypothalamic–pituitary–thyroid axes is explained by the evolutionary refinement of the specificity of expression and selectivity of interaction between the glycoprotein hormones GpH (FSH, LH, and TSH) and their cognate receptors GpH-R (FSH-R, LH-R, and TSH-R). These two finely tuned signaling pathways evolved by gene duplication and functional divergence from an ancestral GpH/GpH-R pair. Comparative analysis of the protochordate and gnathostome endocrine systems suggests that this process took place prior or concomitantly with the emergence of the gnathostome lineage. Here, we report identification and characterization of a novel glycoprotein hormone receptor (lGpH-R II) in the Agnathan sea lamprey. This 781 residue protein was found ∼43% identical with mammalian TSH-R and FSH-R representative sequences, and similarly with these two classes of mammalian receptors it is assembled from ten exons. A synthetic ligand containing the lamprey glycoprotein hormone β-chain tethered upstream of a mammalian α-chain activated the lGpH-R II expressed in COS-7 cells but in a lesser extent than lGpH-R I. Molecular phylogenetic analysis of vertebrate GpH-R protein sequences suggests a closer relationship between lGpH-R II and gnathostome thyrotropin receptors. Overall, the presence and characteristics of the lamprey glycoprotein hormone receptors suggest existence of a primitive functionally overlapping glycoprotein hormone/glycoprotein hormone receptor system in this animal.

scholarly journals GRIS: Glycoprotein-Hormone Receptor Information System

2006 ◽  
Vol 20 (9) ◽  
pp. 2247-2255 ◽  
Author(s):  
Joost Van Durme ◽  
Florence Horn ◽  
Sabine Costagliola ◽  
Gert Vriend ◽  
Gilbert Vassart
Keyword(s):  
Information System ◽  
Hormone Receptor ◽  
Glycoprotein Hormone ◽  
Glycoprotein Hormone Receptor

1-Methyladenine: a starfish oocyte maturation-inducing substance

Zygote ◽  
1999 ◽  
Vol 8 (S1) ◽  
pp. S9-S11 ◽  
Author(s):  
Masatoshi Mita
Keyword(s):  
Oocyte Maturation ◽  
Hormone Receptor ◽  
Ovarian Follicle ◽  
Germinal Vesicle ◽  
Follicle Cells ◽  
Glycoprotein Hormone ◽  
Late Prophase ◽  
Immature Oocytes ◽  
Extracellular Region ◽  
Glycoprotein Hormone Receptor

1-Methyladenine (1-MeAde) in starfish was the first compound to be identified as an oocyte maturation-inducing substance (MIS) among invertebrates in 1969 by Kanatani and co-workers. In starfish, the ripe ovary contains a huge number of fully grown oocytes of almost equal size. Each oocyte possesses a large nucleus (germinal vesicle, GV), which is arrested in late prophase of the first maturation division. The oocyte is surrounded by a single follicle layer. Such immature oocytes are not fertilisable. Resumption of meiosis in immature oocytes can be induced by 1-MeAde, and the mature oocytes thus become fertilisable (Kanatani et al., 1969; Kanatani, 1985). 1-MeAde is produced by ovarian follicle cells upon stimulation with a gonad-stimulating substance (GSS) released from the radial nerves (Fig. 1).It has been demonstrated that GSS is a peptide hormone (Kanatani et al., 1971). The action of GSS on 1-MeAde production in follicle cells appears to be mediated by its receptor, G-proteins and adenylyl cyclase (Mita & Nagahama, 1991). These findings suggest that a G-protein coupled (seven transmembrane type) receptor is involved in GSS signal transduction, similarly to the pituitary-gonadal axis in vertebrates.Thus, using degenerate probes derived from consensus sequences of the mammalian glycoprotein hormone (GTH and TSH) receptors, cDNA was cloned from mRNA of ovaries of Asterina pectinifera. The cDNA showed striking structural homology with members of the glycoprotein hormone receptor family in the transmembrane region, and contained a very large extracellular region. Expression was observed in isolated ovarian follicle cells. Thus, it seems likely that the glycoprotein hormone receptor (GTHR) family gene is related to GSS receptor in ovarian follicle cells. The phylogenic relatedness of the starfish GTHR was also assessed in relation to other vertebrate GTHRs. The analysis showed that the starfish gene diverged before differentiation of the gonadotropin (LH and FSH) and TSH receptors in vertebrates.

scholarly journals Relationship between Thyrotropin Receptor Hinge Region Proteolytic Posttranslational Modification and Receptor Physiological Function

2011 ◽  
Vol 25 (1) ◽  
pp. 184-194 ◽  
Author(s):  
Sepehr Hamidi ◽  
Chun-Rong Chen ◽  
Yumiko Mizutori-Sasai ◽  
Sandra M. McLachlan ◽  
Basil Rapoport
Keyword(s):  
Signal Transduction ◽  
Amino Acids ◽  
Hormone Receptor ◽  
Hinge Region ◽  
Receptor Function ◽  
Glycoprotein Hormone ◽  
Glycoprotein Hormone Receptor ◽  
Functional Alteration

The glycoprotein hormone receptor hinge region is the least conserved component and the most variable in size; the TSH receptor (TSHR) being the longest (152 amino acids; residues 261–412). The TSHR is also unique among the glycoprotein hormone receptor in undergoing in vivo intramolecular cleavage into disulfide-linked A- and B-subunits with removal of an intervening ‘C-peptide’ region. Experimentally, hinge region amino acids 317–366 (50 residues) can be deleted without alteration in receptor function. However, in vivo, more than 50 amino acids are deleted during TSHR intramolecular cleavage; furthermore, the boundaries of this deleted region are ragged and poorly defined. Studies to determine the extent to which hinge region deletions can be tolerated without affecting receptor function (‘minimal hinge’) are lacking. Using as a template the functionally normal TSHR with residues 317–366 deleted, progressive downstream extension of deletions revealed residue 371 to be the limit compatible with normal TSH binding and coupling with cAMP signal transduction. Based on the foregoing downstream limit, upstream deletion from residue 307 (307–371 deletion) was also tolerated without functional alteration, as was deletion of residues 303–366. Addressing a related issue regarding the functional role of the TSHR hinge region, we observed that downstream hinge residues 377–384 contribute to coupling ligand binding with cAMP signal transduction. In summary, we report the first evaluation of TSHR function in relation to proteolytic posttranslational hinge region modifications. Deletion of TSHR hinge amino acids 303–366 (64 residues) or 307–371 (65 residues) are the maximum hinge region deletions compatible with normal TSHR function.

scholarly journals Model of Glycoprotein Hormone Receptor Ligand Binding and Signaling

2004 ◽  
Vol 279 (43) ◽  
pp. 44442-44459 ◽  
Author(s):  
William R. Moyle ◽  
Yongna Xing ◽  
Win Lin ◽  
Donghui Cao ◽  
Rebecca V. Myers ◽  
...  
Keyword(s):  
Ligand Binding ◽  
Hormone Receptor ◽  
Glycoprotein Hormone ◽  
Receptor Ligand ◽  
Glycoprotein Hormone Receptor

scholarly journals Genomic Checkpoints for Exon 10 Usage in the Luteinizing Hormone Receptor Type 1 and Type 2

2007 ◽  
Vol 21 (8) ◽  
pp. 1984-1996 ◽  
Author(s):  
Jörg Gromoll ◽  
Lisa Lahrmann ◽  
Maren Godmann ◽  
Thomas Müller ◽  
Caroline Michel ◽  
...  
Keyword(s):  
Alternative Splicing ◽  
Hormone Receptor ◽  
Regulatory Elements ◽  
Luteinizing Hormone Receptor ◽  
In Vitro Mutagenesis ◽  
Glycoprotein Hormone ◽  
Glycoprotein Hormone Receptor ◽  
Exon 10

Abstract Alternative splicing is a hallmark of glycoprotein hormone receptor gene regulation, but its molecular mechanism is unknown. The LH receptor (LHR) gene possesses 11 exons, but exon 10 is constitutively skipped in the New World monkey lineage (LHR type 2), whereas it is constitutively spliced in the human (LHR type 1). This study identifies the regulatory elements of exon 10 usage. Sequencing of genomic marmoset DNA revealed that the cryptic LHR exon 10 is highly homologous to exon 10 from other species and displays intact splice sites. Functional studies using a minigene approach excluded the contribution of intronic, marmoset-specific long interspersed nucleotide-1 elements to exon 10 skipping. Sequencing of the genomic regions surrounding exon 10 from several primate lineages, sequence comparisons including the human and mouse LHR gene, revealed the presence of unique nucleotides at 3′-intronic position −19 and −10 and at position +26 within exon 10 of the marmoset LHR. Exon trap experiments and in vitro mutagenesis of these nucleotides resulted in the identification of a composite regulatory element of splicing consisting of cis-acting elements represented by two polypyrimidine tracts and a trans-acting element within exon 10, which affect the secondary RNA structure. Changes within this complex resulted either in constitutive exon inclusion, constitutive skipping, or alternative splicing of exon 10. This work delineates the molecular pathway leading to intronization of exon 10 in the LHR type 2 and reveals, for the first time, the essential function of regulatory and structural elements involved in glycoprotein hormone receptor splicing.

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