Characterization of Glycoprotein Hormone Free α-Subunit from Human Pituitary and Placenta Extracts

1986 ◽  
Vol 23 (1) ◽  
pp. 38-49 ◽  
Author(s):  
Roulwhai Chen ◽  
Eytan Barnea ◽  
Robert Benveniste
Keyword(s):  
Alpha Subunit ◽  
Glycoprotein Hormone ◽  
Human Pituitary

scholarly journals The characterization of alpha-subunit of glycoprotein hormone produced by undifferentiated carcinoma.

1982 ◽  
Vol 29 (1) ◽  
pp. 11-19
Author(s):  
RYUICHIRO NISHIMURA ◽  
TAMOTSU HAMAMOTO ◽  
NORIHIKO MORIMOTO ◽  
MITSURU OZAWA ◽  
YOSHIHIKO ASHITAKA ◽  
...  
Keyword(s):  
Undifferentiated Carcinoma ◽  
Alpha Subunit ◽  
Glycoprotein Hormone

scholarly journals Characterization of the Equine Glycoprotein Hormone Alpha-Subunit Gene Reveals Divergence in the Mechanism of Pituitary and Placental Expression1

1997 ◽  
Vol 57 (5) ◽  
pp. 1104-1114 ◽  
Author(s):  
Todd A. Farmerie ◽  
Rula A. Abbud ◽  
Paul R. Budworth ◽  
Colin M. Clay ◽  
Ruth A. Keri ◽  
...  
Keyword(s):  
Alpha Subunit ◽  
Subunit Gene ◽  
Glycoprotein Hormone

Immunohistochemical detection of glycoprotein hormone alpha subunit in somatoprolactinic and pure somatotroph adenomas

1998 ◽  
Vol 21 (7) ◽  
pp. 434-440 ◽  
Author(s):  
M. C. Vantyghem ◽  
C. Cortet ◽  
C. Bauters ◽  
M. H. Gevaert ◽  
D. Dewailly ◽  
...  
Keyword(s):  
Alpha Subunit ◽  
Immunohistochemical Detection ◽  
Glycoprotein Hormone

Purification and characterization of a human pituitary growth factor

Biochemistry ◽  
1986 ◽  
Vol 25 (21) ◽  
pp. 6421-6425 ◽  
Author(s):  
John M. Rowe ◽  
Stephen F. Henry ◽  
Henry G. Friesen
Keyword(s):  
Growth Factor ◽  
Purification And Characterization ◽  
Human Pituitary

scholarly journals Characterization of Two Fly LGR (Leucine-Rich Repeat-Containing, G Protein-Coupled Receptor) Proteins Homologous to Vertebrate Glycoprotein Hormone Receptors: Constitutive Activation of Wild-Type Fly LGR1 But Not LGR2 in Transfected Mammalian Cells**This study was supported by NIH Grant HD-23273. The GenBank submission number for fly LGR2 is AF274591.

Endocrinology ◽  
2000 ◽  
Vol 141 (11) ◽  
pp. 4081-4090 ◽  
Author(s):  
Shinya Nishi ◽  
Sheau Yu Hsu ◽  
Karen Zell ◽  
Aaron J. W. Hsueh
Keyword(s):  
G Protein ◽  
Hormone Receptors ◽  
Coupling Mechanism ◽  
Leucine Rich Repeat ◽  
G Protein Coupled Receptor ◽  
Glycoprotein Hormone ◽  
Glycoprotein Hormone Receptors ◽  
Signaling Mechanisms ◽  
G Protein Coupled

Abstract The receptors for lutropin (LH), FSH, and TSH belong to the large G protein-coupled receptor (GPCR) superfamily and are unique in having a large N-terminal extracellular (ecto-) domain important for interactions with the large glycoprotein hormone ligands. Recent studies indicated the evolution of a large family of the leucine-rich repeat-containing, G protein-coupled receptors (LGRs) with at least seven members in mammals. Based on the sequences of mammalian glycoprotein hormone receptors, we have identified a new LGR in Drosophila melanogaster and named it as fly LGR2 to distinguish it from the previously reported fly LH/FSH/TSH receptor (renamed as fly LGR1). Genomic analysis indicated the presence of 10 exons in fly LGR2 as compared with 16 exons in fly LGR1. The deduced fly LGR2 complementary DNA (cDNA) showed 43 and 64% similarity to the fly LGR1 in the ectodomain and transmembrane region, respectively. Comparison of 12 LGRs from diverse species indicated that these proteins can be divided into three subfamilies and fly LGR1 and LGR2 belong to different subfamilies. Potential signaling mechanisms were tested in human 293T cells overexpressing the fly receptors. Of interest, fly LGR1, but not LGR2, showed constitutive activity as reflected by elevated basal cAMP production in transfected cells. The basal activity of fly LGR1 was further augmented following point mutations of key residues in the intracellular loop 3 or transmembrane VI, similar to those found in patients with familial male precocious puberty. The present study reports the cloning of fly LGR2 and indicates that the G protein-coupling mechanism is conserved in fly LGR1 as compared with the mammalian glycoprotein hormone receptors. The characterization of fly receptors with features similar to mammalian glycoprotein hormone receptors allows a better understanding of the evolution of this unique group of GPCRs and future elucidation of their ligand signaling mechanisms.

Identification and characterization of phosphorylated proteins in the human pituitary

PROTEOMICS ◽  
2004 ◽  
Vol 4 (3) ◽  
pp. 587-598 ◽  
Author(s):  
Francesco Giorgianni ◽  
Sarka Beranova-Giorgianni ◽  
Dominic M. Desiderio
Keyword(s):  
Human Pituitary ◽  
Phosphorylated Proteins ◽  
Identification And Characterization
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