Resveratrol augments nitric oxide generation and causes store calcium release in chromaffin cells

Conformational changes and translocation of tissue-transglutaminase to the plasma membranes: role in cancer cell migration

“…Therefore we did not get synchronized calcium labeling. The effect on the cells away from the scratch may be due to the secondary response of the cells near to scratch, also shown in some previous studies [36,37]. Similar increase in fluorescence intensity of Ca 2+ was not observed when SHY TG2 cells were incubated with a Ca 2+ -chelator, BAPTA-AM (10 μM), in the presence of either concentration of resveratrol (1 or 10 μM) (Figure 6Ai and j).…”

“…The observation that BAPTA-AM reduced the level of the slower mobility form of TG2 in resveratrol treated cells (Figure 6E, lanes 5 and 6) further support the requirement of Ca 2+ ions in the structural modification of TG2. Resveratrol induced calcium release is supported by recent studies in myotubes and chromaffin cells [35,37]. Previous reports suggest the existence of two forms of TG2 depending on the Ca 2+ ion concentrations in cells with a compact closed form at low Ca 2+ concentration and an open extended form at higher Ca 2+ concentration [34,39-44].…”

Resveratrol neuroprotection in stroke and traumatic CNS injury

“…Also, there is evidence that persistent oxidative stress can cause eNOS uncoupling, resulting in superoxide production instead of vasoprotective NO (Li and Förstermann, 2013). Resveratrol has been shown to increase NO production in several systems (Elíes et al, 2011; Klinge et al, 2008; Padín et al, 2012). However, the bulk of investigations into resveratrol-mediated NO regulation have been performed in the context of the vasculature (Simao et al, 2012c).…”

Relationship between nitric oxide- and calcium-dependent signal transduction pathways in growth hormone release from dispersed goldfish pituitary cells

“…These tissues include adipocytes (Turovsky et al, 2013), neurons (Kakizawa et al, 2012, adrenal chromaffin cells (Padin et al, 2012), endothelial cells (Evangelista et al, 2012), cardiac (Donoso et al, 2011) and skeletal muscles (Pouvreau and Jacquemond, 2005). In addition, NOS and ryanodine receptors can be co-precipitated from cardiomyocytes indicating a tight physical association of the NO-generating system with the ryanodine-sensitive intracellular Ca 2+ release mechanisms, at least in some tissues (Lim et al, 2008).…”

“…The functional relationship between NO and SERCA is also controversial. While NO has been shown to inhibit SERCA pumps in skeletal muscles (Ishii et al, 1998) and to prevent Ca 2+ release from SERCArefilled stores in pulmonary artery smooth muscles (Yuan et al, 1997), NO action in mammalian endocrine cells (e.g., pituitary cells, Duvilanski et al, 1998; adrenal chromaffin cells, Padin et al, 2012) and mouse and rabbit aorta (Cohen et al, 1999) depends on Ca 2+ mobilization from these pools. Thus, interactions between NO-and Ca 2+ -dependent signalling mechanisms can occur in different ways and these two pathways are interdependent.…”