Endoplasmic Reticulum Ca<sup>2+</sup>Handling in Excitable Cells in Health and Disease

Wound healing is essential for survival. We took advantage of the Xenopus embryo, which exhibits remarkable capacities to repair wounds quickly and efficiently, to investigate the mechanisms responsible for wound healing. Previous work has shown that injury triggers a rapid calcium response, followed by the activation of Ras homolog (Rho) family guanosine triphosphatases (GTPases), which regulate the formation and contraction of an F-actin purse string around the wound margin. How these processes are coordinated following wounding remained unclear. Here we show that inositol-trisphosphate 3-kinase B (Itpkb) via its enzymatic product inositol 1,3,4,5-tetrakisphosphate (InsP 4 ) plays an essential role during wound healing by modulating the activity of Rho family GTPases and F-actin ring assembly. Furthermore, we show that Itpkb and InsP 4 modulate the speed of the calcium wave, which propagates from the site of injury into neighboring uninjured cells. Strikingly, both overexpression of itpkb and exogenous application of InsP 4 accelerate the speed of wound closure, a finding that has potential implications in our quest to find treatments that improve wound healing in patients with acute or chronic wounds.

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“…2D). These embryos were raised until the tailbud stages (stages [20][21][22][23][24][25] and wounded in the epidermis (Fig. 2D).…”

Section: Resultsmentioning

confidence: 99%

Inositol kinase and its product accelerate wound healing by modulating calcium levels, Rho GTPases, and F-actin assembly

Soto

Lea

et al. 2013

Proc. Natl. Acad. Sci. U.S.A.

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“…Ryanodine inhibits Ca 2ϩ mobilization either by blocking Ca 2ϩ release channels or by promoting the leakage of Ca 2ϩ from the SR (38). To distinguish between these possibilities, we treated neonatal cardiomyocytes with thapsigargin (1 M in Ca 2ϩ -free saline), an inhibitor of the sarco/endoplasmic reticulum Ca 2ϩ ATPase, conditions which deplete both ryanodineand IP 3 -sensitive Ca 2ϩ pools (39). As shown in Fig.…”

Section: Extracellular Administration Of Lpi Elicits Gpr55-dependent mentioning

confidence: 99%

Differential Activation of Cultured Neonatal Cardiomyocytes by Plasmalemmal Versus Intracellular G Protein-coupled Receptor 55

Deliu²,

Zhang

et al. 2013

Journal of Biological Chemistry

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Background:The LPI-sensitive receptor GPR55 signals through Ca 2ϩ . Results: Activation of sarcolemmal versus intracellular GPR55 mobilizes Ca 2ϩ from distinct pools and associates with cardiomyocyte depolarization and hyperpolarization, respectively. Conclusion: GPR55 location critically affects LPI-induced modulation of cardiomyocyte function. Significance: We identify GPR55 as a new receptor regulating cardiac function at two cellular sites.

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“…A recurring theme in many of these studies is that depletion of ER Ca 2+ stores, contributed through activation of RyRs and IP 3 Rs as well as impaired SERCA function, is an important trigger for ER stress. Consistent with this, depletion of ER Ca 2+ stores through inhibition of SERCA activity is sufficient to initiate ER stress and cell death in a variety of cell types [108] . Typically, ER stress is operationally defined on the basis of UPR induction.…”

Section: Er-initiated Cell Death Cascadesmentioning

confidence: 62%

Loss of endoplasmic reticulum Ca2+ homeostasis: contribution to neuronal cell death during cerebral ischemia

Bodalia

Jackson

2012

Acta Pharmacol Sin

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The loss of Ca 2+ homeostasis during cerebral ischemia is a hallmark of impending neuronal demise. Accordingly, considerable cellular resources are expended in maintaining low resting cytosolic levels of Ca 2+ . These include contributions by a host of proteins involved in the sequestration and transport of Ca 2+ , many of which are expressed within intracellular organelles, including lysosomes, mitochondria as well as the endoplasmic reticulum (ER homeostasis is an important trigger of pathological processes. Here we review a growing body of evidence suggesting that ER dysfunction is an important factor contributing to neuronal injury and loss post-ischemia. Specifically, the contribution of the ER to cytosolic Ca 2+ elevations during ischemia will be considered, as will the signalling cascades recruited as a consequence of disrupting ER homeostasis and function.

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Endoplasmic Reticulum Ca²⁺Handling in Excitable Cells in Health and Disease

Cited by 205 publications

References 346 publications

Inositol kinase and its product accelerate wound healing by modulating calcium levels, Rho GTPases, and F-actin assembly

Inositol kinase and its product accelerate wound healing by modulating calcium levels, Rho GTPases, and F-actin assembly

Differential Activation of Cultured Neonatal Cardiomyocytes by Plasmalemmal Versus Intracellular G Protein-coupled Receptor 55

Loss of endoplasmic reticulum Ca2+ homeostasis: contribution to neuronal cell death during cerebral ischemia

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Endoplasmic Reticulum Ca2+Handling in Excitable Cells in Health and Disease

Cited by 205 publications

References 346 publications

Inositol kinase and its product accelerate wound healing by modulating calcium levels, Rho GTPases, and F-actin assembly

Inositol kinase and its product accelerate wound healing by modulating calcium levels, Rho GTPases, and F-actin assembly

Differential Activation of Cultured Neonatal Cardiomyocytes by Plasmalemmal Versus Intracellular G Protein-coupled Receptor 55

Loss of endoplasmic reticulum Ca2+ homeostasis: contribution to neuronal cell death during cerebral ischemia

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Resources

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Endoplasmic Reticulum Ca²⁺Handling in Excitable Cells in Health and Disease