TRPC1 functions as a store-operated Ca2+ channel in intestinal epithelial cells and regulates early mucosal restitution after wounding.

  title={TRPC1 functions as a store-operated Ca2+ channel in intestinal epithelial cells and regulates early mucosal restitution after wounding.},
  author={Jaladanki N Rao and Oleksandr Platoshyn and Vera A. Golovina and Lan Liu and Tongtong Zou and Bernard S. Marasa and Douglas J. Turner and Jason X.-J. Yuan and Jian-Ying Wang},
  journal={American journal of physiology. Gastrointestinal and liver physiology},
  volume={290 4},
An increase in cytosolic free Ca(2+) concentration ([Ca(2+)](cyt)) results from Ca(2+) release from intracellular stores and extracellular Ca(2+) influx through Ca(2+)-permeable ion channels and is crucial for initiating intestinal epithelial restitution to reseal superficial wounds after mucosal injury. Capacitative Ca(2+) entry (CCE) induced by Ca(2+) store depletion represents a major Ca(2+) influx mechanism, but the exact molecular components constituting this process remain elusive. This… 

Figures and Tables from this paper

RhoA enhances store-operated Ca2+ entry and intestinal epithelial restitution by interacting with TRPC1 after wounding.

Early mucosal restitution occurs as a consequence of epithelial cell migration to resealing of superficial wounds after injury. Our previous studies show that canonical transient receptor potential-1

Caveolin‐1 enhances rapid mucosal restitution by activating TRPC1‐mediated Ca2+ signaling

Results indicate that Cav1 physically interacts with and activates TRPC1, thus stimulatingTRPC1‐mediated Ca2+ signaling and rapid mucosal restitution after injury.

STIM1 translocation to the plasma membrane enhances intestinal epithelial restitution by inducing TRPC1-mediated Ca2+ signaling after wounding.

It is demonstrated that induced STIM1 translocation to the plasma membrane promotes IEC migration after wounding by enhancing TRPC1-mediated Ca2+ signaling and provide new insight into the mechanism of intestinal epithelial restitution.

Molecular mechanisms underlying Ca2+-mediated motility of human pancreatic duct cells.

TGF-β induces Ca(2+) entry likely via TRPC1 and NCX1 and raises [Ca(2+)](cyt) in pancreatic cancer cells, which is essential for PKCα activation and subsequent tumor cell invasion.

Contribution of TRPC1 and Orai1 to Ca(2+) entry activated by store depletion.

This chapter summarizes recent studies and concepts regarding the contributions of Orai1 and TRPC1 to SOCE as well as possible mechanisms involved in the regulation of TRPC channels by store depletion.

Ca2+-Permeable Channels/Ca2+ Signaling in the Regulation of Ileal Na+/Gln Co-Transport in Mice

It is concluded that Ca2+ signaling is critical for intestinal Gln transport, and multiple plasma membrane Ca2-permeable channels and transporters play roles in this process.

STIM-TRP Pathways and Microdomain Organization: Contribution of TRPC1 in Store-Operated Ca2+ Entry: Impact on Ca2+ Signaling and Cell Function.

It is now clearly established that regulation of TRPC1 trafficking can change plasma membrane levels of the channel, the phenotype of the store-operated Ca2+ current, as well as pattern of SOCE-mediated [Ca2+]i signals.

Metabotropic receptor-activated calcium increases and store-operated calcium influx in mouse Müller cells.

PURPOSE Metabotropic receptor agonists that signal through G(q)-coupled pathways increase Ca(2+) in mammalian Müller cells by release from intracellular stores and Ca(2+) influx pathways that have



Upregulated TRP and enhanced capacitative Ca(2+) entry in human pulmonary artery myocytes during proliferation.

Examination of whether CCE, activity of store-operated Ca(2+) channels, and human TRP1 (hTRP1) expression are essential in human pulmonary arterial smooth muscle cell (PASMC) proliferation suggests that elevated [Ca(2+)](cyt) and intracellularly stored [Ca-2+] play an important role in pulmonary vascular smooth Muscle cell growth.

Enhanced capacitative calcium entry and TRPC channel gene expression in human LES smooth muscle.

In LES cells, enhanced CCE and expression of TRPC3 and TRPC4 may contribute to the physiological characteristics that distinguish LES from EB, as demonstrated by measurement of fura 2 Ca(2+) fluorescence and transcriptional expression.

Na(+) entry via store-operated channels modulates Ca(2+) signaling in arterial myocytes.

It is demonstrated that the SOC are a major Na(+) entry route in arterial myocytes and has unexpectedly large effects on cell-wide Ca(2+) signaling.

Store depletion and calcium influx.

The electrophysiological properties of the prototype store-operated current ICRAC are focused on, the regulatory mechanisms that control it are discussed, and recent advances toward the identification of molecular mechanisms involved in this ubiquitous and important Ca2+ entry pathway are considered.

Inhibition of endogenous TRP1 decreases capacitative Ca2+ entry and attenuates pulmonary artery smooth muscle cell proliferation.

Results indicate that TRP1 may encode a store-operated Ca2+ channel that plays a critical role in PASMC proliferation by regulating CCE and intracellular [Ca2+](cyt).

Activation of K(+) channels and increased migration of differentiated intestinal epithelial cells after wounding.

Results suggest that increased migration of differentiated intestinal epithelial cells is mediated, at least partially, by increasing Kv channel activity and Ca(2+) influx during restitution.

Store-operated calcium entry promotes shape change in pulmonary endothelial cells expressing Trp1.

This study indicates that Ca2+ entry in pulmonary endothelial cells through SOCs produces cell shape change that is dependent on site-specific rearrangement of the microfilamentous cytoskeleton and Trp1 may be a component of pulmonary arterial endothelial SOCs.

Ion channels in vascular endothelium.

Different types of ion channels in ECs are described and their role in electrogenesis, Ca2+ signaling, vessel permeability, cell-cell communication, mechano-sensor functions, and pH and volume regulation is described.

TRPC1, a human homolog of a Drosophila store-operated channel.

The molecular characterization of a human homolog of trp, TRPC1, was described, which was 40% identical to Drosophila TRP over most of the protein and lacked the charged residues in the S4 transmembrane region proposed to be required for the voltage sensor in many voltage-gated ion channels.

Polyamines regulate Rho-kinase and myosin phosphorylation during intestinal epithelial restitution.

Increase in GTP-bound RhoA by polyamines via [Ca(2+)](cyt) can interact with and activate Rho-kinase during intestinal epithelial restitution and is associated with the stimulation of myosin stress fiber formation and cell migration.