Purification of Functional Human TRP Channels Recombinantly Produced in Yeast

(1) Background: Human transient receptor potential (TRP) channels constitute a large family of ion-conducting membrane proteins that allow the sensation of environmental cues. As the dysfunction of TRP channels contributes to the pathogenesis of many widespread diseases, including cardiac disorders,...

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Bibliographic Details
Published in:Cells (Basel, Switzerland) Switzerland), 2019-02, Vol.8 (2), p.148
Main Authors: Zhang, Liying, Wang, Kaituo, Klaerke, Dan Arne, Calloe, Kirstine, Lowrey, Lillian, Pedersen, Per Amstrup, Gourdon, Pontus, Gotfryd, Kamil
Format: Article
Language:English
Subjects:
Animals
Cardiovascular disease
Chromatography
Coronary artery disease
Detergents - pharmacology
Glucose
Glycerol
Heart diseases
Humans
ion channels
Membrane proteins
Membranes
overproduction
Phylogeny
Plasmids
production platform
protein purification
Proteins
Recombinant Proteins - biosynthesis
Saccharomyces cerevisiae
Saccharomyces cerevisiae - metabolism
sensors
Solubility
Structure-function relationships
transient receptor potential (TRP) channels
Transient Receptor Potential Channels - biosynthesis
Transient Receptor Potential Channels - chemistry
Transient Receptor Potential Channels - isolation & purification
Transient receptor potential proteins
Yeast
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Summary:(1) Background: Human transient receptor potential (TRP) channels constitute a large family of ion-conducting membrane proteins that allow the sensation of environmental cues. As the dysfunction of TRP channels contributes to the pathogenesis of many widespread diseases, including cardiac disorders, these proteins also represent important pharmacological targets. TRP channels are typically produced using expensive and laborious mammalian or insect cell-based systems. (2) Methods: We demonstrate an alternative platform exploiting the yeast capable of delivering high yields of functional human TRP channels. We produce 11 full-length human TRP members originating from four different subfamilies, purify a selected subset of these to a high homogeneity and confirm retained functionality using TRPM8 as a model target. (3) Results: Our findings demonstrate the potential of the described production system for future functional, structural and pharmacological studies of human TRP channels.
ISSN:2073-4409
2073-4409
DOI:10.3390/cells8020148