Abstract
Endothelialization repairs the lining of damaged vasculature and is a key process in preventing thrombosis and restenosis. It has been demonstrated that extracellular calcium ([Ca2+](o)) influx is important for subsequent endothelialization. The role of intracellular Ca2+ stores in mechanical denudation induced intracellular calcium ([Ca2+](i)) rise and endothelialization remains to be demonstrated. Using monolayer culture of a human endothelial cell line (human umbilical vein endothelial cell, HUVEC), we investigated [Ca2+, wave propagation and re-endothelialization following mechanical denudation. Consistent with previous reports for other types of cells, mechanical denudation induces calcium influx, which is essential for [Ca2+](i) rise and endothelialization. Moreover, we found that intracellular Ca2+ stores are also essential for denudation induced[Ca2+](i) wave initiation and propagation, and the subsequent endothelialization. Thapsigargin which depletes intracellular Ca2+ stores completely abolished [Ca2+](i) wave generation and endothelialization. Xestospongin C (XeC), which prevents Ca2+ release from intracellular Ca2+ stores by inhibition of inositol 1,4,5-trisphosphate (IP3) receptor, inhibited intercellular Ca2+ wave generation and endothelialization following denudation. Purinergic signaling through a suramin sensitive mechanism and gap junction communication also contribute to in intercellular Ca2+ wave propagation and re-endothelialization. We conclude that intracellular Ca2+ stores, in addition to extracellular Ca2+, are essential for intracellular Ca2+ signaling and subsequent endothelialization following mechanical denudation.
Original language | English |
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Pages (from-to) | 595-603 |
Number of pages | 9 |
Journal | Journal of Cellular Physiology |
Volume | 214 |
Issue number | 3 |
Early online date | 16 Oct 2007 |
DOIs | |
Publication status | Published - Mar 2008 |
Keywords
- Calcium Channel Blockers
- Calcium Channels, L-Type
- Calcium Signaling
- Cobalt
- Endothelial Cells
- Gap Junctions
- Humans
- Receptors, Purinergic