scholarly journals Discrimination of intracellular calcium store subcompartments using TRPV1 (transient receptor potential channel, vanilloid subfamily member 1) release channel activity

2003 ◽  
Vol 371 (2) ◽  
pp. 341-350 ◽  
Author(s):  
Helen TURNER ◽  
Andrea FLEIG ◽  
Alexander STOKES ◽  
Jean-Pierre KINET ◽  
Reinhold PENNER
Keyword(s):  
Intracellular Calcium ◽  
Transient Receptor Potential ◽  
Receptor Potential ◽  
Transient Receptor Potential Channel ◽  
Calcium Stores ◽  
Calcium Store ◽  
Release Channel ◽  
Subfamily Member ◽  
Store Depletion ◽  
Transient Receptor

The store-operated calcium-release-activated calcium current, ICRAC, is a major mechanism for calcium entry into non-excitable cells. ICRAC refills calcium stores and permits sustained calcium signalling. The relationship between inositol 1,4,5-trisphosphate receptor (InsP3R)-containing stores and ICRAC is not understood. A model of global InsP3R store depletion coupling with ICRAC activation may be simplistic, since intracellular stores are heterogeneous in their release and refilling activities. Here we use a ligand-gated calcium channel, TRPV1 (transient receptor potential channel, vanilloid subfamily member 1), as a new tool to probe store heterogeneity and define intracellular calcium compartments in a mast cell line. TRPV1 has activity as an intracellular release channel but does not mediate global calcium store depletion and does not invade a store coupled with ICRAC. Intracellular TRPV1 localizes to a subset of the InsP3R-containing stores. TRPV1 sensitivity functionally subdivides the InsP3-sensitive store, as does heterogeneity in the sarcoplasmic/endoplasmic-reticulum Ca2+-ATPase isoforms responsible for store refilling. These results provide unequivocal evidence that a specific ‘CRAC store’ exists within the InsP3-releasable calcium stores and describe a novel methodology for manipulation of intracellular free calcium.

scholarly journals Elucidation of a TRPC6-TRPC5 Channel Cascade That Restricts Endothelial Cell Movement

2008 ◽  
Vol 19 (8) ◽  
pp. 3203-3211 ◽  
Author(s):  
Pinaki Chaudhuri ◽  
Scott M. Colles ◽  
Manjunatha Bhat ◽  
David R. Van Wagoner ◽  
Lutz Birnbaumer ◽  
...  
Keyword(s):  
Intracellular Calcium ◽  
Calcium Concentration ◽  
Transient Receptor Potential ◽  
Calcium Influx ◽  
Cell Movement ◽  
Receptor Potential ◽  
Receptor Activation ◽  
Calcium Stores ◽  
Trpc Channels ◽  
Transient Receptor

Canonical transient receptor potential (TRPC) channels are opened by classical signal transduction events initiated by receptor activation or depletion of intracellular calcium stores. Here, we report a novel mechanism for opening TRPC channels in which TRPC6 activation initiates a cascade resulting in TRPC5 translocation. When endothelial cells (ECs) are incubated in lysophosphatidylcholine (lysoPC), rapid translocation of TRPC6 initiates calcium influx that results in externalization of TRPC5. Activation of this TRPC6–5 cascade causes a prolonged increase in intracellular calcium concentration ([Ca2+]i) that inhibits EC movement. When TRPC5 is down-regulated with siRNA, the lysoPC-induced rise in [Ca2+]i is shortened and the inhibition of EC migration is lessened. When TRPC6 is down-regulated or EC from TRPC6−/− mice are studied, lysoPC has minimal effect on [Ca2+]i and EC migration. In addition, TRPC5 is not externalized in response to lysoPC, supporting the dependence of TRPC5 translocation on the opening of TRPC6 channels. Activation of this novel TRPC channel cascade by lysoPC, resulting in the inhibition of EC migration, could adversely impact on EC healing in atherosclerotic arteries where lysoPC is abundant.

185 TRANSIENT RECEPTOR POTENTIAL CHANNEL-2 (TRPP2) REGULATES MOTILITY AND INTRACELLULAR CALCIUM OF PORCINE SPERM

2016 ◽  
Vol 28 (2) ◽  
pp. 223
Author(s):  
B. W. Daigneault ◽  
D. J. Miller
Keyword(s):  
Membrane Protein ◽  
Intracellular Calcium ◽  
Transient Receptor Potential ◽  
Beat Frequency ◽  
Receptor Potential ◽  
Transient Receptor Potential Channel ◽  
Sperm Function ◽  
Cystic Kidneys ◽  
Mammalian Sperm ◽  
Transient Receptor

Transient receptor potential channel-2 (TRPP2) is a membrane protein important for the regulation of calcium homeostasis in renal epithelial cells. Mutations in human TRPP2 cause enlarged cystic kidneys and contribute to polycystic kidney disease. In addition, TRPP2 functions have been described in some invertebrate sperm and are related to sperm-egg interactions and mating. Male Drosophila with mutated TRPP2 display a mild sperm motility phenotype but have a drastic reduction in fertility due to failed sperm migration and storage within the female tract. Although TRPP2 has critical roles for Drosophila sperm function, the protein has not been described in mammalian sperm. The TRPP2 mutations affecting sperm function could explain idiopathic subfertility that is not detected when evaluating sperm by routine analyses. Herein we report the location of TRPP2 in porcine sperm and have identified functions of TRPP2 in regulating sperm functions important for fertility. The TRPP2 was detected as a 110-kDa band in protein lysates from sperm after capacitation or mock incubation in conditions that do not capacitate sperm. With immunofluorescence, TRPP2 was most abundant on the head and principal piece of sperm with more consistent staining patterns when sperm were maintained in non-capacitating medium. Inhibition of TRPP2 by antiserum resulted in a reduction in sperm average path and curvilinear velocity and an increase in tail cross-beat frequency when sperm were incubated in capacitating conditions. Sperm incubated with TRPP2 antiserum also had a significant decrease in intracellular calcium concentration compared with control samples and failed to undergo an increase in calcium over 90 min that is characteristic of capacitating sperm. TRPP2 is a previously unreported mammalian sperm membrane protein that appears to function as an ion channel to regulate calcium and capacitation-like changes in porcine sperm. This project is supported by Agriculture and Food Research Initiative Competitive Grant no. 2011–67015–20099 and 2015–67015–23228 from the USDA National Institute of Food and Agriculture.

scholarly journals Dynamic interaction of hTRPC6 with the Orai1–STIM1 complex or hTRPC3 mediates its role in capacitative or non-capacitative Ca2+ entry pathways

2009 ◽  
Vol 420 (2) ◽  
pp. 267-277 ◽  
Author(s):  
Isaac Jardin ◽  
Luis J. Gómez ◽  
Gines M. Salido ◽  
Juan A. Rosado
Keyword(s):  
Acetic Acid ◽  
Transient Receptor Potential ◽  
Receptor Potential ◽  
Transient Receptor Potential Channel ◽  
Dynamic Interaction ◽  
Concentration Cell ◽  
Canonical Transient Receptor Potential ◽  
Store Depletion ◽  
Transient Receptor ◽  
Acid Loading

TRPC (canonical transient receptor potential) channel subunits have been shown to assemble into homo- or hetero-meric channel complexes, including different Ca2+-handling proteins, required for the activation of CCE (capacitative Ca2+ entry) or NCCE (non-CCE) pathways. In the present study we found evidence for the dynamic interaction between endogenously expressed hTRPC6 (human TRPC6) with either both Orai1 and STIM1 (stromal interaction molecule 1) or hTRPC3 to participate in CCE or NCCE. Electrotransjection of cells with an anti-hTRPC6 antibody, directed towards the C-terminal region, reduces CCE induced by TPEN [N,N,N′,N′-tetrakis-(2-pyridylmethyl)-ethylenediamine], which reduces the intraluminal free Ca2+ concentration. Cell stimulation with thrombin or extensive Ca2+-store depletion by TG (thapsigargin)+ionomycin enhanced the interaction between hTRPC6 and the CCE proteins Orai1 and STIM1. In contrast, stimulation with the diacylglycerol analogue OAG (1-oleoyl-2-acetyl-sn-glycerol) displaces hTRPC6 from Orai1 and STIM1 and enhances the association between hTRPC6 and hTRPC3. The interaction between hTRPC6 and hTRPC3 was abolished by dimethyl-BAPTA [1,2-bis-(o-aminophenoxy)ethane-N,N,N′,N′-tetra-acetic acid] loading, which indicates that this phenomenon is Ca2+-dependent. These findings support the hypothesis that hTRPC6 participates both in CCE and NCCE through its interaction with the Orai1–STIM1 complex or hTRPC3 respectively.

scholarly journals Function of the Porcine TRPC1 Gene in Myogenesis and Muscle Growth

Cells ◽  
2021 ◽  
Vol 10 (1) ◽  
pp. 147
Author(s):  
Yu Fu ◽  
Peng Shang ◽  
Bo Zhang ◽  
Xiaolong Tian ◽  
Ruixue Nie ◽  
...  
Keyword(s):  
Transient Receptor Potential ◽  
Growth Traits ◽  
Expression Profiles ◽  
Muscle Growth ◽  
Receptor Potential ◽  
Transient Receptor Potential Channel ◽  
Nucleotide Polymorphisms ◽  
Pig Breeds ◽  
Muscle Tissues ◽  
Transient Receptor

In animals, muscle growth is a quantitative trait controlled by multiple genes. Previously, we showed that the transient receptor potential channel 1 (TRPC1) gene was differentially expressed in muscle tissues between pig breeds with divergent growth traits base on RNA-seq. Here, we characterized TRPC1 expression profiles in different tissues and pig breeds and showed that TRPC1 was highly expressed in the muscle. We found two single nucleotide polymorphisms (SNPs) (C-1763T and C-1604T) in TRPC1 that could affect the promoter region activity and regulate pig growth rate. Functionally, we used RNAi and overexpression to illustrate that TRPC1 promotes myoblast proliferation, migration, differentiation, fusion, and muscle hypertrophy while inhibiting muscle degradation. These processes may be mediated by the activation of Wnt signaling pathways. Altogether, our results revealed that TRPC1 might promote muscle growth and development and plays a key role in Wnt-mediated myogenesis.

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