Cloning and Expression, Pharmacological Characterization, and Internalization Kinetics of the Pituitary GnRH Receptor in a Metatherian Species of Mammal

King, Judy A.; Fidler, Andrew E.; Lawrence, S.B.; Adam, Tasneem; Millar, Robert P.; Katz, Arieh A.

doi:10.1006/gcen.1999.7418

Cited by 20 publications

(7 citation statements)

References 21 publications

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“…Homologs of many mammalian GnRH receptors were cloned from a marsupial (possum) (King et al, 2000;Cheung and Hearn, 2002), two forms from the goldfish , bullfrog, brown frog and clawed toad (Troskie et al, 2000;Wang et al, 2001;Seong et al, 2003), chicken (Sun et al, 2000), medaka (Okubo et al, 2001), striped bass (Alok et al, 2000), trout and salmon (Madigou et al, 2000;Jodo et al, 2003), cichlid (Robinson et al, 2001), Japanesse eel (Okubo et al, 2000), amberjack, rubber eel, and sea squirt (Millar et al, 2004). The non-mammalian receptors with the greatest homology to the mammalian pituitary receptors have 42-47% amino acid identity with them, but 58-67% identity among each other.…”

Section: Structure Of the Gnrh Receptor And Its Genementioning

confidence: 99%

Evolution of gonadotropin-releasing hormone (GnRH) structure and its receptor

Kochman¹

2012

J. Anim. Feed Sci.

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It is evident now that the gonadotropin-releasing hormone (GnRH) structure was already in existence very early in the evolution of animals and was co-opted in diverse ways to regulate reproduction. During 600 million years of animal evolution, the N and C termini of GnRH have been conserved as functional domains for binding and activating cognate receptors to accomplish its functions. About 400 millions years ago, a single substitution of the chiral amino acid in position 6 of GnRH in jawless fish by the achiral glycine facilitated a type II' β-turn conformation of GnRH to allow spatially close interaction of functional domains of GnRH with receptors, in contrast to the interaction of more extended GnRH structures with their cognate receptors in earlier-evolved species. GnRH II was preconfigured to this conformation through intramolecular interactions, which accounts for its high binding affinity and total conservation of primary structure over 400 million years of evolution. It is very surprising and fascinating that the coordinated evolutionary selection of amino acids participating in binding GnRH has resulted in such perfection, that no substitution with a natural amino acid in any position improves binding potency.

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Section: Structure Of the Gnrh Receptor And Its Genementioning

confidence: 99%

Evolution of gonadotropin-releasing hormone (GnRH) structure and its receptor

Kochman¹

2012

J. Anim. Feed Sci.

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“…Internalization of 125 I-labeled lamprey GnRH-I was performed based on the acid-wash method, as previously described (Hazum et al 1983, Pawson et al 1998, King et al 2000. Briefly, COS7 cells transfected with the wild type lamprey GnRH receptor or C-terminal tail truncated mutants were seeded (1 10 5 cells) in 24-well plates in 500 µl medium, and were grown for 48 h. Cells were incubated with 10 nM 125 I-labeled lamprey GnRH-I on ice at 4 C for 3·5 h. Cells were then immediately brought to 37 C for increasing periods of time.…”

Section: Lamprey Gnrh Receptor Internalization Assaymentioning

confidence: 99%

Functional characterization and kinetic studies of an ancestral lamprey GnRH-III selective type II GnRH receptor from the sea lamprey, Petromyzon marinus

Silver

Sower

2006

Journal of Molecular Endocrinology

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The recently cloned lamprey GnRH receptor was shown to have several unique features, including the longest intracellular C-terminal tail (120 amino acids (aa)) of any previously described GnRH receptor. In the current study, a series of experiments were performed examining cAMP responses, binding kinetics, whole cell competitive binding assays and internalization studies of the lamprey GnRH receptor using a series of three C-terminal tail truncations (80 aa, 40 aa and 0 aa) to better describe the functional significance of this unique vertebrate GnRH receptor.

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“…Full species names and GenBank accession numbers for the receptor cDNAs are as follows: African catfish, Clarias gariepinus, O42329; goldfish, Carassius auratus, IA: AAD20001 and IB: AAD20002; eel, Anguilla japonica, BAB11961; pig, Sus scrofa, P49922; cow, Bos taurus, AAC48857; mouse, Mus musculus, AAB59636; sheep, Ovis aries, AAC37336; rat, Rattus norvegicus, AAC27349; and human, Homo sapiens, NP 000397. Also, the sequences for possum (Trichosurus vulpecula) GnRH-R (14) and frog (Xenopus laevis) type I GnRH-R (4) were used. The following sequences were unpublished at the time of this writing: perciform fishes Seriola dumerilii (CAB65407) and striped bass (Morone saxatilis, AAF28464), a caecilian amphibian (Typhlonectes natans, AAD49750), horse (Equus caballus, O18821), and type II from Xenopus (Troskie, B., N. Illing, and R. Millar, unpublished data).…”

Section: Phylogenetic Analysis Of Gnrh-rmentioning

confidence: 99%

Gonadotropin-Releasing Hormone Receptor in the Teleost Haplochromis burtoni: Structure, Location, and Function

Robison¹

2001

Endocrinology

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GnRH acts via GnRH receptors (GnRH-R) in the pituitary to cause the release of gonadotropins that regulate vertebrate reproduction. In the teleost fish, Haplochromis burtoni, reproduction is socially regulated through the hypothalamus-pituitary-gonadal axis, making the pituitary GnRH-R a likely site of action for this control. As a first step toward understanding the role of GnRH-R in the social control of reproduction, we cloned and sequenced candidate GnRH-R complementary DNAs from H. burtoni tissue. We isolated a complementary DNA that predicts a peptide encoding a G protein-coupled receptor that shows highest overall identity to other fish type I GnRH-R (goldfish IA and IB and African catfish). Functional testing of the expressed protein in vitro confirmed high affinity binding of multiple forms of GNRH: Localization of GnRH-R messenger RNA using RT-PCR revealed that it is widely distributed in the brain and retina as well as elsewhere in the body. Taken together, these data suggest that this H. burtoni GnRH receptor probably interacts in vivo with all three forms of GNRH:

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Cloning and Expression, Pharmacological Characterization, and Internalization Kinetics of the Pituitary GnRH Receptor in a Metatherian Species of Mammal

Cited by 20 publications

References 21 publications

Evolution of gonadotropin-releasing hormone (GnRH) structure and its receptor

Evolution of gonadotropin-releasing hormone (GnRH) structure and its receptor

Functional characterization and kinetic studies of an ancestral lamprey GnRH-III selective type II GnRH receptor from the sea lamprey, Petromyzon marinus

Gonadotropin-Releasing Hormone Receptor in the Teleost Haplochromis burtoni: Structure, Location, and Function

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