scholarly journals Responses to transient receptor potential (TRP) channel agonists in Chlamydomonas reinhardtii

Biology Open ◽  
2020 ◽  
Vol 9 (7) ◽  
pp. bio053140
Author(s):  
Mamoru Wada ◽  
Itaru Kaizuka ◽  
Kenjiro Yoshimura
Keyword(s):  
Chlamydomonas Reinhardtii ◽  
Transient Receptor Potential ◽  
Receptor Potential ◽  
Trp Channel ◽  
Transient Receptor

scholarly journals Structure of the thermo-sensitive TRP channel TRP1 from the alga Chlamydomonas reinhardtii

2019 ◽  
Vol 10 (1) ◽  
Author(s):  
Luke L. McGoldrick ◽  
Appu K. Singh ◽  
Lusine Demirkhanyan ◽  
Ting-Yu Lin ◽  
Ryan G. Casner ◽  
...  
Keyword(s):  
Chlamydomonas Reinhardtii ◽  
Transient Receptor Potential ◽  
Trp Channels ◽  
Receptor Potential ◽  
Membrane Lipid ◽  
Membrane Receptors ◽  
Trp Channel ◽  
Structural Framework ◽  
Trp Ion Channels ◽  
Transient Receptor

Abstract Algae produce the largest amount of oxygen on earth and are invaluable for human nutrition and biomedicine, as well as for the chemical industry, energy production and agriculture. The mechanisms by which algae can detect and respond to changes in their environments can rely on membrane receptors, including TRP ion channels. Here we present a 3.5-Å resolution cryo-EM structure of the transient receptor potential (TRP) channel crTRP1 from the alga Chlamydomonas reinhardtii that opens in response to increased temperature and is positively regulated by the membrane lipid PIP2. The structure of crTRP1 significantly deviates from the structures of other TRP channels and has a unique 2-fold symmetrical rose-shape architecture with elbow domains and ankyrin repeat domains submerged and dipping into the membrane, respectively. Our study provides a structure of a TRP channel from a micro-organism and a structural framework for better understanding algae biology and TRP channel evolution.

scholarly journals Expression of transient receptor potential (TRP) channel mRNAs in the mouse olfactory bulb

2012 ◽  
Vol 524 (1) ◽  
pp. 49-54 ◽  
Author(s):  
Hong-Wei Dong ◽  
James C. Davis ◽  
ShengYuan Ding ◽  
Qiang Nai ◽  
Fu-Ming Zhou ◽  
...  
Keyword(s):  
Olfactory Bulb ◽  
Transient Receptor Potential ◽  
Receptor Potential ◽  
Trp Channel ◽  
Transient Receptor

scholarly journals Molecular Bases of Multimodal Regulation of a Fungal Transient Receptor Potential (TRP) Channel

2013 ◽  
Vol 288 (21) ◽  
pp. 15303-15317 ◽  
Author(s):  
Makoto Ihara ◽  
Shin Hamamoto ◽  
Yohei Miyanoiri ◽  
Mitsuhiro Takeda ◽  
Masatsune Kainosho ◽  
...  
Keyword(s):  
Transient Receptor Potential ◽  
Receptor Potential ◽  
Trp Channel ◽  
Transient Receptor ◽  
Molecular Bases

scholarly journals TRP Channels as Sensors of Aldehyde and Oxidative Stress

Biomolecules ◽  
2021 ◽  
Vol 11 (10) ◽  
pp. 1401
Author(s):  
Katharina E. M. Hellenthal ◽  
Laura Brabenec ◽  
Eric R. Gross ◽  
Nana-Maria Wagner
Keyword(s):  
Lipid Peroxidation ◽  
Transient Receptor Potential ◽  
Trp Channels ◽  
Treatment Options ◽  
Receptor Potential ◽  
The Body ◽  
Trp Channel ◽  
Alcoholic Beverages ◽  
Organ Injury ◽  
Transient Receptor

The transient receptor potential (TRP) cation channel superfamily comprises more than 50 channels that play crucial roles in physiological processes. TRP channels are responsive to several exogenous and endogenous biomolecules, with aldehydes emerging as a TRP channel trigger contributing to a cellular cascade that can lead to disease pathophysiology. The body is not only exposed to exogenous aldehydes via tobacco products or alcoholic beverages, but also to endogenous aldehydes triggered by lipid peroxidation. In response to lipid peroxidation from inflammation or organ injury, polyunsaturated fatty acids undergo lipid peroxidation to aldehydes, such as 4-hydroxynonenal. Reactive aldehydes activate TRP channels via aldehyde-induced protein adducts, leading to the release of pro-inflammatory mediators driving the pathophysiology caused by cellular injury, including inflammatory pain and organ reperfusion injury. Recent studies have outlined how aldehyde dehydrogenase 2 protects against aldehyde toxicity through the clearance of toxic aldehydes, indicating that targeting the endogenous aldehyde metabolism may represent a novel treatment strategy. An addition approach can involve targeting specific TRP channel regions to limit the triggering of a cellular cascade induced by aldehydes. In this review, we provide a comprehensive summary of aldehydes, TRP channels, and their interactions, as well as their role in pathological conditions and the different therapeutical treatment options.

scholarly journals Functional characterization of transient receptor potential channels in mouse urothelial cells

2010 ◽  
Vol 298 (3) ◽  
pp. F692-F701 ◽  
Author(s):  
Wouter Everaerts ◽  
Joris Vriens ◽  
Grzegorz Owsianik ◽  
Giovanni Appendino ◽  
Thomas Voets ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Patch Clamp ◽  
Calcium Imaging ◽  
Transient Receptor Potential ◽  
Receptor Potential ◽  
Functional Expression ◽  
Sensory Function ◽  
Trp Channel ◽  
Urothelial Cells ◽  
Transient Receptor

The bladder urothelium is currently believed to be a sensory structure, contributing to mechano- and chemosensation in the bladder. Transient receptor potential (TRP) cation channels act as polymodal sensors and may underlie some of the receptive properties of urothelial cells. However, the exact TRP channel expression profile of urothelial cells is unclear. In this study, we have performed a systematic analysis of the molecular and functional expression of various TRP channels in mouse urothelium. Urothelial cells from control and trpv4−/− mice were isolated, cultured (12–48 h), and used for quantitative real-time PCR, immunocytochemistry, calcium imaging, and whole cell patch-clamp experiments. At the mRNA level, TRPV4, TRPV2, and TRPM7 were the most abundantly expressed TRP genes. Immunohistochemistry showed a clear expression of TRPV4 in the plasma membrane, whereas TRPV2 was more prominent in the cytoplasm. TRPM7 was detected in the plasma membrane as well as cytoplasmic vesicles. Calcium imaging and patch-clamp experiments using TRP channel agonists and antagonists provided evidence for the functional expression of TRPV4, TRPV2, and TRPM7 but not of TRPA1, TRPV1, and TRPM8. In conclusion, we have demonstrated functional expression of TRPV4, TRPV2, and TRPM7 in mouse urothelial cells. These channels may contribute to the (mechano)sensory function of the urothelial layer and represent potential targets for the treatment of bladder dysfunction.

scholarly journals Human transient receptor potential (TRP) channel expression profiling in carcinogenesis

2015 ◽  
Vol 59 (7-8-9) ◽  
pp. 399-406 ◽  
Author(s):  
Michela Bernardini ◽  
Alessandra Fiorio Pla ◽  
Natalia Prevarskaya ◽  
Dimitra Gkika
Keyword(s):  
Expression Profiling ◽  
Transient Receptor Potential ◽  
Receptor Potential ◽  
Trp Channel ◽  
Channel Expression ◽  
Transient Receptor

Transient receptor potential (TRP) channel function in the reproductive axis

Cell Calcium ◽  
2017 ◽  
Vol 67 ◽  
pp. 138-147 ◽  
Author(s):  
Viktoria Götz ◽  
Sen Qiao ◽  
Andreas Beck ◽  
Ulrich Boehm
Keyword(s):  
Transient Receptor Potential ◽  
Receptor Potential ◽  
Trp Channel ◽  
Channel Function ◽  
Reproductive Axis ◽  
Transient Receptor

Structure of the human PKD1-PKD2 complex

Science ◽  
2018 ◽  
Vol 361 (6406) ◽  
pp. eaat9819 ◽  
Author(s):  
Qiang Su ◽  
Feizhuo Hu ◽  
Xiaofei Ge ◽  
Jianlin Lei ◽  
Shengqiang Yu ◽  
...  
Keyword(s):  
Transient Receptor Potential ◽  
Complex Structure ◽  
Transmembrane Helix ◽  
Receptor Potential ◽  
Trp Channel ◽  
Cryo Electron Microscopy ◽  
Disease Mechanisms ◽  
Autosomal Dominant Polycystic Kidney ◽  
Transient Receptor ◽  
Positively Charged

Mutations in two genes, PKD1 and PKD2, account for most cases of autosomal dominant polycystic kidney disease, one of the most common monogenetic disorders. Here we report the 3.6-angstrom cryo–electron microscopy structure of truncated human PKD1-PKD2 complex assembled in a 1:3 ratio. PKD1 contains a voltage-gated ion channel (VGIC) fold that interacts with PKD2 to form the domain-swapped, yet noncanonical, transient receptor potential (TRP) channel architecture. The S6 helix in PKD1 is broken in the middle, with the extracellular half, S6a, resembling pore helix 1 in a typical TRP channel. Three positively charged, cavity-facing residues on S6b may block cation permeation. In addition to the VGIC, a five–transmembrane helix domain and a cytosolic PLAT domain were resolved in PKD1. The PKD1-PKD2 complex structure establishes a framework for dissecting the function and disease mechanisms of the PKD proteins.

scholarly journals The nonselective cation channel TRPV4 inhibits angiotensin II receptors

2020 ◽  
Vol 295 (29) ◽  
pp. 9986-9997
Author(s):  
Nicholas W. Zaccor ◽  
Charlotte J. Sumner ◽  
Solomon H. Snyder
Keyword(s):  
Angiotensin Ii ◽  
G Protein ◽  
Transient Receptor Potential ◽  
Trp Channels ◽  
Receptor Potential ◽  
Trp Channel ◽  
Luciferase Assay ◽  
Transient Receptor Potential Vanilloid ◽  
Dependent Manner ◽  
Transient Receptor

G-protein–coupled receptors (GPCRs) are a ubiquitously expressed family of receptor proteins that regulate many physiological functions and other proteins. They act through two dissociable signaling pathways: the exchange of GDP to GTP by linked G-proteins and the recruitment of β-arrestins. GPCRs modulate several members of the transient receptor potential (TRP) channel family of nonselective cation channels. How TRP channels reciprocally regulate GPCR signaling is less well-explored. Here, using an array of biochemical approaches, including immunoprecipitation and fluorescence, calcium imaging, phosphate radiolabeling, and a β-arrestin–dependent luciferase assay, we characterize a GPCR–TRP channel pair, angiotensin II receptor type 1 (AT1R), and transient receptor potential vanilloid 4 (TRPV4), in primary murine choroid plexus epithelial cells and immortalized cell lines. We found that AT1R and TRPV4 are binding partners and that activation of AT1R by angiotensin II (ANGII) elicits β-arrestin–dependent inhibition and internalization of TRPV4. Activating TRPV4 with endogenous and synthetic agonists inhibited angiotensin II–mediated G-protein–associated second messenger accumulation, AT1R receptor phosphorylation, and β-arrestin recruitment. We also noted that TRPV4 inhibits AT1R phosphorylation by activating the calcium-activated phosphatase calcineurin in a Ca2+/calmodulin–dependent manner, preventing β-arrestin recruitment and receptor internalization. These findings suggest that when TRP channels and GPCRs are co-expressed in the same tissues, many of these channels can inhibit GPCR desensitization.

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