scholarly journals Activation of Estrogen Receptor G Protein–Coupled Receptor 30 Enhances Cholesterol Cholelithogenesis in Female Mice

Hepatology ◽  
2020 ◽  
Vol 72 (6) ◽  
pp. 2077-2089 ◽  
Author(s):  
Helen H. Wang ◽  
Ornella Bari ◽  
Christopher K. Arnatt ◽  
Min Liu ◽  
Piero Portincasa ◽  
...  
Keyword(s):  
Estrogen Receptor ◽  
G Protein ◽  
G Protein Coupled Receptor ◽  
Female Mice ◽  
G Protein Coupled

scholarly journals Stroke Increases G Protein-Coupled Estrogen Receptor Expression in the Brain of Male but Not Female Mice

Neurosignals ◽  
2013 ◽  
Vol 21 (3-4) ◽  
pp. 229-239 ◽  
Author(s):  
Brad R.S. Broughton ◽  
Vanessa H. Brait ◽  
Elizabeth Guida ◽  
Seyoung Lee ◽  
Thiruma V. Arumugam ◽  
...  
Keyword(s):  
Estrogen Receptor ◽  
G Protein ◽  
Receptor Expression ◽  
Estrogen Receptor Expression ◽  
Female Mice ◽  
G Protein Coupled ◽  
The Brain

Impact of Aging and G Protein‐Coupled Estrogen Receptor Deletion in Arterial Stiffening and Cardiac Function in Male and Female Mice

2020 ◽  
Vol 34 (S1) ◽  
pp. 1-1
Author(s):  
Benard Ojwang Ogola ◽  
Margaret A. Zimmerman ◽  
Nicholas R. Harris ◽  
Isabella Kilanowski-Doroh ◽  
Leanne Groban ◽  
...  
Keyword(s):  
Estrogen Receptor ◽  
Cardiac Function ◽  
G Protein ◽  
Male And Female ◽  
Arterial Stiffening ◽  
Female Mice ◽  
G Protein Coupled

scholarly journals Human G protein-coupled receptor 30 is N-glycosylated and N-terminal domain asparagine 44 is required for receptor structure and activity

2019 ◽  
Vol 39 (2) ◽  
Author(s):  
Ernesto Gonzalez de Valdivia ◽  
Caroline Sandén ◽  
Robin Kahn ◽  
Björn Olde ◽  
L.M. Fredrik Leeb-Lundberg
Keyword(s):  
Estrogen Receptor ◽  
G Protein ◽  
Hek293 Cells ◽  
G Protein Coupled Receptor ◽  
Hek 293 ◽  
Receptor Structure ◽  
Terminal Domain ◽  
Endocytic Vesicles ◽  
G Protein Coupled ◽  
Structure And Activity

Abstract G protein-coupled receptor 30 (GPR30), or G protein-coupled estrogen receptor (GPER), is a G protein-coupled receptor (GPCR) that is currently attracting considerable attention in breast cancer and cardiometabolic regulation. The receptor was reported to be a novel membrane estrogen receptor mediating rapid non-genomic responses. However, questions remain about both the cognate ligand and the subcellular localization of receptor activity. Here, we used human embryonic kidney (HEK) 293 (HEK293) cells ectopically expressing N-terminally FLAG-tagged human GPR30 and three unique antibodies (Ab) specifically targetting the receptor N-terminal domain (N-domain) to investigate the role of N-glycosylation in receptor maturation and activity, the latter assayed by constitutive receptor-stimulated extracellular-regulated protein kinase (ERK) 1/2 (ERK1/2) activity. GPR30 expression was complex with receptor species spanning from approximately 40 kDa to higher molecular masses and localized in the endoplasmatic reticulum (ER), the plasma membrane (PM), and endocytic vesicles. The receptor contains three conserved asparagines, Asn25, Asn32, and Asn44, in consensus N-glycosylation motifs, all in the N-domain, and PNGase F treatment showed that at least one of them is N-glycosylated. Mutating Asn44 to isoleucine inactivated the receptor, yielding a unique receptor species at approximately 20 kDa that was recognized by Ab only in a denatured state. On the other hand, mutating Asn25 or Asn32 either individually or in combination, or truncating successively N-domain residues 1–42, had no significant effect either on receptor structure, maturation, or activity. Thus, Asn44 in the GPR30 N-domain is required for receptor structure and activity, whereas N-domain residues 1–42, including specifically Asn25 and Asn32, do not play any major structural or functional role(s).

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