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Related Concept Videos

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Calcium is an essential signaling molecule required for various cellular functions. Calcium pumps and ion channels on cell and organellar membranes, such as those on the endoplasmic reticulum (ER), regulate calcium concentrations inside the cell. They remain closed, keeping the cytosolic calcium levels low at a resting state.
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Calmodulin (CaM) is a calcium-binding protein in eukaryotes that controls various calcium-regulated cellular processes. It has four calcium-binding sites that bind calcium to form the calcium-calmodulin ( Ca2+-CaM) complex. GPCR stimulation increases the calcium levels in the cells that bind to CaM and induces a conformational change.
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Related Experiment Video

Updated: Apr 30, 2026

Cytosolic Calcium Measurements in Renal Epithelial Cells by Flow Cytometry
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DA-6034 Induces [Ca(2+)]i Increase in Epithelial Cells.

Yu-Mi Yang1, Soonhong Park1, Hyewon Ji1

  • 1Department of Oral Biology, BK21 PLUS Project, Yonsei University College of Dentistry, Seoul 120-752, Korea.

The Korean Journal of Physiology & Pharmacology : Official Journal of the Korean Physiological Society and the Korean Society of Pharmacology
|April 24, 2014
PubMed
Summary

DA-6034, a flavonoid derivative, activates calcium signaling in human eye and salivary gland epithelial cells. This occurs through extracellular calcium entry and ryanodine receptor-sensitive calcium release, suggesting potential for dry eye treatment.

Keywords:
Calcium signalingDA-6034Epithelial cellsEupatilin

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Area of Science:

  • Ophthalmology
  • Cell Biology
  • Pharmacology

Background:

  • DA-6034, a eupatilin derivative, shows promise for dry eye treatment due to its effects on ocular surface cells.
  • The precise mechanism by which DA-6034 influences calcium (Ca2+) signaling in epithelial cells remains unclear.

Purpose of the Study:

  • To investigate the mechanism of DA-6034-induced Ca2+ signaling in human conjunctival, corneal, and mouse salivary gland epithelial cells.

Main Methods:

  • Primary cultured human conjunctival, corneal epithelial cells, and mouse salivary gland epithelial cells were used.
  • Intracellular calcium concentrations ([Ca2+]i) were measured.
  • The roles of extracellular Ca2+ entry, internal Ca2+ stores, ryanodine receptors (RyRs), and phospholipase C/inositol 1,4,5-triphosphate (IP3) pathways were examined.

Main Results:

  • DA-6034 activated Ca2+-activated Cl- channels (CaCCs) and increased [Ca2+]i in human conjunctival cells.
  • Increased [Ca2+]i was observed in human corneal and mouse salivary gland epithelial cells.
  • DA-6034-induced [Ca2+]i increase depended on extracellular Ca2+ influx and RyRs-mediated Ca2+ release, not the IP3 pathway or lysosomal stores.

Conclusions:

  • DA-6034 triggers Ca2+ signaling in epithelial cells via extracellular Ca2+ entry and RyRs-sensitive intracellular Ca2+ release.
  • These findings elucidate the mechanism of DA-6034 action and support its potential as a therapeutic agent for dry eye.