Biochemical and Biophysical Research Communications
The calcium mobilizing and tumor promoting agent, thapsigargin elevates the platelet cytoplasmic free calcium concentration to a higher steady state level. A possible mechanism of action for the tumor promotion
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Cited by (124)
Transient receptor potential ankyrin-1 (TRPA1) modulates store-operated Ca<sup>2+</sup> entry by regulation of STIM1-Orai1 association
2013, Biochimica et Biophysica Acta - Molecular Cell ResearchCitation Excerpt :Hence, we have investigated the role of TRPA1 in store-operated Ca2 + entry (SOCE) in MEG01 cells. In a Ca2 +-free medium, TG, a specific inhibitor of the sarco/endoplasmic-reticulum Ca2 +-ATPase [43], evoked a sustained elevation of [Ca2 +]i in MEG01 cells owing to the release of Ca2 + from intracellular pools, which was insensitive to treatment of MEG01 cells with the TRPA1 inhibitor HC-030031 (the integral of the rise in fura-2 fluorescence 340/380 nm ratio for 2 min after the addition of TG in the absence or presence of HC-030031 was 1207 ± 201 and 1170 ± 112, respectively; Fig. 4E and F). In the presence of 1 mM extracellular Ca2 + TG-evoked a prolonged and greater increase in [Ca2 +]i due to both Ca2 + release from internal stores and the subsequent activation of SOCE.
Intracellular calcium chelation and pharmacological SERCA inhibition of Ca <sup>2+</sup> pump in the insular cortex differentially affect taste aversive memory formation and retrieval
2011, Neurobiology of Learning and MemoryCitation Excerpt :It has a high affinity (high nM–low μM range) for SERCA, initially causing a rise in cytoplasmic calcium and some minutes later an emptying of the internal stores. A consequence of thapsigargin treatment is that ER function is deregulated, which affects calcium release from internal deposits and activates the store-operated calcium influx (Thastrup, Foder, & Scharff, 1987). BAPTA-AM, thapsigargin, and other well accepted modulators of calcium dynamics have been used extensively to interfere with intracellular calcium fluxes in a variety of experimental systems, including signaling-disrupting protocols in cerebral-associated phenomena (Lohr, Heil, & Deitmer, 2005; Martin, Rogers, Chagneau, & Brulet, 2007a; Martin, Torres, & Sanchez-Prieto, 2007b; Tonkikh et al., 2006; Tymianski, Charlton, Carlen, & Tator, 1994).
Passive Ca<sup>2+</sup> overload in H9c2 cardiac myoblasts: Assessment of cellular damage and cytosolic Ca<sup>2+</sup> transients
2011, Archives of Biochemistry and BiophysicsCitation Excerpt :The effect of Ca2+ overloading on cell damage was analyzed by performing preincubation treatments in the presence of Ca2+. The sensitivity to cell damage induced by internal Ca2+ was then evaluated by adding TG or BHQ to provoke the irreversible discharge of the SR Ca2+ pool [24–26]. In a set of experiments, cells were preincubated for 2 h in serum-free DMEM with 1.8 mM Ca2+.
FRET peptides reveal differential proteolytic activation in intraerythrocytic stages of the malaria parasites Plasmodium berghei and Plasmodium yoelii
2011, International Journal for ParasitologyCitation Excerpt :These results are similar to those of Farias and colleagues (2005) for two other Plasmodium spp., P. falciparum and P. chabaudi. The ER, is an important compartment for intracellular Ca2+ storage in eukaryotic cells (Thastrup et al., 1987; Sagara et al., 1992), including protozoan parasites (Sibley, 2004; Berridge, 2006). These results indicate the importance of Ca2+ release from the ER in stimulating protease activity in different Plasmodium spp.
TRPC3 regulates agonist-stimulated Ca<sup>2+</sup> mobilization by mediating the interaction between type I inositol 1,4,5-trisphosphate receptor, RACK1, and Orai1
2010, Journal of Biological ChemistryCitation Excerpt :We have investigated the possible association between the plasma membrane protein Orai1 and the type I IP3R in two unrelated human cell lines, HEK293 and HeLa cells, by looking for co-immunoprecipitation from cell lysates. Immunoprecipitation and subsequent SDS-PAGE and Western blotting were conducted using resting cells and cells treated with TG, a specific inhibitor of SERCA (40) that promotes passive Ca2+ efflux from the endoplasmic reticulum and, subsequently, rises in [Ca2+]i. As depicted in Fig. 1, A and B, upper panels, our results show detectable association between Orai1 and type I IP3R in resting HEK293 and HeLa cells.