scholarly journals Activation of canonical transient receptor potential channels preserves Ca 2+ entry and endothelium-derived hyperpolarizing factor–mediated function in vitro in porcine coronary endothelial cells and coronary arteries under conditions of hyperkalemia

2014 ◽  
Vol 148 (4) ◽  
pp. 1665-1673.e1 ◽  
Author(s):  
Qin Yang ◽  
Jun-Hao Huang ◽  
Xiao-Qiang Yao ◽  
Malcolm John Underwood ◽  
Cheuk-Man Yu
Keyword(s):  
Endothelial Cells ◽  
Coronary Arteries ◽  
Transient Receptor Potential ◽  
Receptor Potential ◽  
Transient Receptor Potential Channels ◽  
Canonical Transient Receptor Potential ◽  
Coronary Endothelial Cells ◽  
Potential Channels ◽  
Transient Receptor

scholarly journals Genetic variants affecting human TRPA1 or TRPM8 structure can be classified in vitro as ‘well expressed’, ‘poorly expressed’ or ‘salvageable’

2015 ◽  
Vol 35 (5) ◽  
Author(s):  
Kevin Morgan ◽  
Laura Rachel Sadofsky ◽  
Alyn Hugh Morice
Keyword(s):  
Genetic Variants ◽  
Transient Receptor Potential ◽  
Kinase Inhibitor ◽  
Receptor Potential ◽  
Transient Receptor Potential Channels ◽  
Human Embryonic Kidney ◽  
Potential Channels ◽  
Pre Treatment ◽  
Transient Receptor

Genetic variants of human transient receptor potential channels A1 and M8 expressed in human embryonic kidney HEK293 and SH-SY5Y cells were assayed using Ca2+ signalling. TRPA1 Y69C responded well. Poorly expressed variant signalling was enhanced by pre-treatment with tyrosine kinase inhibitor PP2 or Zn2+.

scholarly journals The Membrane Proximal Domain of TRPV1 and TRPV2 Channels Mediates Protein–Protein Interactions and Lipid Binding In Vitro

2019 ◽  
Vol 20 (3) ◽  
pp. 682 ◽  
Author(s):  
Pau Doñate-Macián ◽  
Elena Álvarez-Marimon ◽  
Francesc Sepulcre ◽  
José Vázquez-Ibar ◽  
Alex Perálvarez-Marín
Keyword(s):  
Protein Interactions ◽  
Transient Receptor Potential ◽  
Receptor Potential ◽  
Lipid Binding ◽  
Transient Receptor Potential Channels ◽  
Trpv Channels ◽  
Potential Channels ◽  
Transient Receptor ◽  
Lipid Protein Interactions

Constitutive or regulated membrane protein trafficking is a key cell biology process. Transient receptor potential channels are somatosensory proteins in charge of detecting several physical and chemical stimuli, thus requiring fine vesicular trafficking. The membrane proximal or pre-S1 domain (MPD) is a highly conserved domain in transient receptor potential channels from the vanilloid (TRPV) subfamily. MPD shows traits corresponding to protein-protein and lipid-protein interactions, and protein regulatory regions. We have expressed MPD of TRPV1 and TRPV2 as green fluorescente protein (GFP)-fusion proteins to perform an in vitro biochemical and biophysical characterization. Pull-down experiments indicate that MPD recognizes and binds Soluble N-ethylmaleimide-sensitive factor Attachment Protein Receptors (SNARE). Synchrotron radiation scattering experiments show that this domain does not self-oligomerize. MPD interacts with phosphatidic acid (PA), a metabolite of the phospholipase D (PLD) pathway, in a specific manner as shown by lipid strips and Trp fluorescence quenching experiments. We show for the first time, to the best of our knowledge, the binding to PA of an N-terminus domain in TRPV channels. The presence of a PA binding domain in TRPV channels argues for putative PLD regulation. Findings in this study open new perspectives to understand the regulated and constitutive trafficking of TRPV channels exerted by protein-protein and lipid-protein interactions.

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