cardiovascular-agents has been researched along with apelin-13-peptide* in 3 studies
3 other study(ies) available for cardiovascular-agents and apelin-13-peptide
| Article | Year |
|---|---|
Biphenyl Acid Derivatives as APJ Receptor Agonists.
The APJ receptor and its endogenous peptidic ligand apelin have been implicated as important modulators of cardiovascular function, and APJ receptor agonists may be beneficial in the treatment of heart failure. In this article, we describe the discovery of a series of biphenyl acid derivatives as potent APJ receptor agonists. Following the identification of initial high-throughput screen lead Topics: Animals; Apelin Receptors; Biphenyl Compounds; Blood Pressure; Cardiovascular Agents; Dose-Response Relationship, Drug; Heart Rate; HEK293 Cells; High-Throughput Screening Assays; Humans; Intercellular Signaling Peptides and Proteins; Male; Rats, Sprague-Dawley; Small Molecule Libraries; Structure-Activity Relationship | 2019 |
Synthetic Modification within the "RPRL" Region of Apelin Peptides: Impact on Cardiovascular Activity and Stability to Neprilysin and Plasma Degradation.
Apelin is an important mammalian peptide hormone with a range of physiological roles, especially in the cardiovascular system. The apelinergic system is a promising target for treatment of disease, but this remains to be realized due to rapid proteolysis of apelin-derived peptides by proteases, including neprilysin (NEP). The synthetic analogues modified within the NEP degradation site ("RPRL" motif) showed improved in vitro proteolytic stability while maintaining receptor-binding affinities, with three candidate peptides retaining full cardiovascular activities for potential therapeutic application. Many such analogues proved physiologically inactive even with relatively conservative modifications, highlighting the importance of this region for full agonist activity of this peptide hormone. Topics: Animals; Apelin Receptors; Blood Pressure; Cardiovascular Agents; CHO Cells; Cricetulus; Heart Rate; Humans; Intercellular Signaling Peptides and Proteins; Mice; Neprilysin; Protein Isoforms; Rats; Receptors, G-Protein-Coupled; Stereoisomerism; Structure-Activity Relationship | 2017 |
Discovery and Structure-Activity Relationship of a Bioactive Fragment of ELABELA that Modulates Vascular and Cardiac Functions.
ELABELA (ELA) was recently discovered as a novel endogenous ligand of the apelin receptor (APJ), a G protein-coupled receptor. ELA signaling was demonstrated to be crucial for normal heart and vasculature development during embryogenesis. We delineate here ELA's structure-activity relationships and report the identification of analogue 3 (ELA(19-32)), a fragment of ELA that binds to APJ, activates the Gαi1 and β-arrestin-2 signaling pathways, and induces receptor internalization similarly to its parent endogenous peptide. An alanine scan performed on 3 revealed that the C-terminal residues are critical for binding to APJ and signaling. Finally, using isolated-perfused hearts and in vivo hemodynamic and echocardiographic measurements, we demonstrate that ELA and 3 both reduce arterial pressure and exert positive inotropic effects on the heart. Altogether, these results present ELA and 3 as potential therapeutic options in managing cardiovascular diseases. Topics: Amino Acid Sequence; Amino Acid Substitution; Animals; Apelin Receptors; Blood Pressure; Cardiovascular Agents; Electrocardiography; Heart; Heart Ventricles; Humans; Intercellular Signaling Peptides and Proteins; Male; Molecular Sequence Data; Organ Culture Techniques; Peptide Fragments; Peptide Hormones; Rats, Sprague-Dawley; Receptors, G-Protein-Coupled; Structure-Activity Relationship | 2016 |