Results 191 to 200 of about 2,484 (221)

Emerging roles for the relaxin/RXFP1 system in cancer therapy

Molecular and Cellular Endocrinology, 2019
A role for the hormone relaxin in cancer was described well before the receptor was identified. Relaxin predominantly increases the growth and invasive potential in cancers of different origins. However, relaxin was also shown to promote cell differentiation and to act in a dose-and time-dependent manner in different cancer cell models used.
Thomas Klonisch, Sabine Hombach-Klonisch
exaly   +3 more sources

Modeling the Primary Hormone‐Binding Site of RXFP1 and RXFP2

Annals of the New York Academy of Sciences, 2009
The primary binding sites of the relaxin and insulin‐like peptide 3 (INSL3) receptors, RXFP1 and RXFP2, are found within the leucine‐rich repeats (LRRs) of the ectodomains. Specific B‐chain residues in the peptides interact with residues in the inner β‐sheets of the LRRs of the receptors.
Daniel J Scott, Roger J Summers
exaly   +3 more sources

RXFP1, the relaxin receptor: Lost and found in translation

Drug Discovery Today
Relaxin, historically recognized as a pregnancy hormone, is today characterized as a circulating protein possessing several cardiovascular modulating and anti-fibrotic properties of high clinical interest. Although it has long been recognized that there exists remarkable species diversity regarding the tissue sources and physiological effects of ...
Mark Lal, Jeffrey Hodgin, Pernille B Hansen   +2 more
exaly   +3 more sources

Relaxin Receptor LGR7 (RXFP1) Is Regulated by Estrogen

Annals of the New York Academy of Sciences, 2009
Estrogen regulates LGR7 (RXFP1) mRNA expression in an in vitro model of human term pregnancy cervix that utilizes lower uterine segment fibroblasts. LGR7 mRNA levels were increased by estradiol to mean levels of 152%± 5.9% above those in untreated control cells. Therefore, estradiol may amplify relaxin's actions in the cervix.
Priya, Maseelall, Jeff, Gardner, Andrea, Wojtczuk, Gerson, Weiss, Laura T, Goldsmith   +4 more
openaire   +2 more sources

Recombinant RXFP1-LDL-A module does not form dimers

Italian Journal of Anatomy and Embryology, 2014
The Relaxin receptor, RXFP1, is a complex G-protein coupled receptor (GPCR). It has a rhodopsin- like 7 transmembrane helix region and a large ecto-domain containing Leucine-rich repeats and a Low Desnsity Lipoprotein Class-A module at the N-terminus. RXFP1 and the closely related receptor for INSL3, RXFP2 are the only mammalian GPCRs to contain an LDL-
Petrie, Emma J., Periguini, Matthew A., Bathgate, Ross A.D., Gooley, Paul R.   +3 more
openaire   +2 more sources

Mechanisms of Relaxin Receptor (LGR7/RXFP1) Expression and Function

Annals of the New York Academy of Sciences, 2009
The LGR7/RXFP1 and LGR8/RXFP2 receptors are unique receptors among the G‐protein‐coupled receptors (GPCRs) in having a low‐density lipoprotein class A (LDL‐A) module. Their complex gene organization, among the intron‐richest of the GPCRs, suggests that alternative splicing is a common occurrence.
András, Kern, Gillian D, Bryant-Greenwood   +1 more
openaire   +2 more sources

Resolving the Unconventional Mechanisms Underlying RXFP1 and RXFP2 Receptor Function

Annals of the New York Academy of Sciences, 2009
The receptors for relaxin and insulin‐like peptide 3 (INSL3) are now well‐characterized as the relaxin family peptide (RXFP) receptors RXFP1 and RXFP2, respectively. They are G‐protein‐coupled receptors (GPCRs) with closest similarity to the glycoprotein hormone receptors, with both containing large ectodomains with 10 leucine‐rich repeats (LRRs ...
Daniel J Scott, Emma J Petrie, Roger J Summers   +2 more
exaly   +3 more sources

Expression of RXFP1 in skin of scleroderma patients and control subjects

Scandinavian Journal of Rheumatology, 2012
Relaxin (RLX) is involved in extracellular matrix and collagen remodelling. The therapeutic role of the circulating isoform RLX-2 as an anti-fibrotic factor in systemic sclerosis (SSc) has been investigated. Several RLX family peptide receptors (RXFPs) are recognized in humans: RLX-2 is a ligand for RXFP1/LGR7 and RXFP2/LGR8.
Giordano, N., Volpi, Nila, Franci, D., Corallo, Claudio, Fioravanti, A., Papakostas, Panagiotis, Montella, Antonio, Biagioli, Maurizio, Fimiani, Michele, Grasso, Giovanni, Muscettola, M. M., Guerranti, R., Vannoni, D., Galeazzi, Mauro, Nuti, Ranuccio   +14 more
openaire   +4 more sources

H3 Relaxin Demonstrates Antifibrotic Properties via the RXFP1 Receptor

Biochemistry, 2011
Human gene 3 (H3) relaxin is the most recently discovered member of the relaxin peptide family and can potentially bind all of the defined relaxin family peptide receptors (RXFP1-4). While its effects as a neuromodulator are being increasingly studied through its primary receptor, RXFP3, its actions via other RXFPs are poorly understood.
Mohammed Akhter, Hossain, Bryna Chow Suet, Man, Chongxin, Zhao, Qi, Xu, Xiao-Jun, Du, John D, Wade, Chrishan S, Samuel   +6 more
openaire   +2 more sources

Relaxin‐Induced Changes in Renal Function and RXFP1 Receptor Expression in the Female Rat

Annals of the New York Academy of Sciences, 2009
Relaxin causes renal hyperfiltration, natriuresis, and diuresis in male rats. This study determined the effect of recombinant human relaxin (rhRLX) on renal function in the female rat. After 7 days of rhRLX treatment (0.4 μg/h) urinary excretion of sodium and chloride were significantly lower in the rhRLX‐treated group, but urine flow rate was not ...
Bogzil, Alsadek H., Ashton, Nick
openaire   +2 more sources