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Skeletal Mechanobiology
Published in Jiro Nagatomi, Eno Essien Ebong, Mechanobiology Handbook, 2018
Alesha B. Castillo, Christopher R. Jacobs
The α subunit of G-proteins exist as monomers known as Rho and Ras GTPases, which are active when bound to GTP.231 Flow-activated G-protein recruit and activate phospholipase C (PLC), which hydrolyzes phophatidylinositol 4,5-bisphophonate and generates the second messengers DAG and IP3.232 IP3 then induces calcium release from intracellular stores, which acts as a second messenger in bone cells.233 Flow-activated G-protein also activate PKA, which phosphorylates the cAMP response element (CRE)-binding protein (CREB), a transcription factor that can bind the promoter of Cox-2.234 Mechanical stimuli have been shown to activate G-proteins in vascular endothelial235,236 and multipotent stromal120 cells. Frangos and colleagues showed that G-protein activation leads to an increase in PGE-2 release, whereas G-protein inhibitors block the response.237 They also showed that G-protein activation was initiated independent of a protein receptor,238 which suggests that changes in membrane structure alone can activate G-proteins. Finally, flow-induced osteogenic differentiation as measured by Runx2 was significantly reduced in multipotent stromal cells treated with a RhoA inhibitor,120 suggesting that G-proteins plays an important role in both early and late events in osteoblastic signaling.
Downstream Signaling 2
Published in James E. Ferrell, Systems Biology of Cell Signaling, 2021
Another famous example of coherent feed-forward regulation, this time from eukaryotic signaling, is the activation of classical protein kinase C (Figure 5.14b). The activation of a phospholipase C (PLC) brings about the conversion of the inner leaflet phospholipid PIP2 into diacylglycerol (DG) and IP3. DG acts as a stoichiometric regulator of PKC, helping to recruit it to the plasma membrane. IP3 acts as a regulator of Ca2+ release from the endoplasmic reticulum, and cytosolic Ca2+ in turn acts as a stoichiometric activator of DG-bound PKC.
Cadmium stress in plants: A critical review of the effects, mechanisms, and tolerance strategies
Published in Critical Reviews in Environmental Science and Technology, 2022
Taoufik El Rasafi, Abdallah Oukarroum, Abdelmajid Haddioui, Hocheol Song, Eilhann E. Kwon, Nanthi Bolan, Filip M. G. Tack, Abin Sebastian, M. N. V. Prasad, Jörg Rinklebe
Cadmium accumulation in plants leads to the activation of the calcium-calmodulin pathway, phytohormone synthesis, and ROS-mediated signaling (Bali et al., 2019; Dobrikova & Apostolova, 2019; Ghosh & Roy, 2019; Hameed et al., 2015). The different signaling pathways in response to Cd stress in plants are presented in Figure 1. Several authors have indicated the crucial role of Ca2+ and calmodulin interactions as a messenger of external stimuli and signaling pathway that respond to potential toxic elements (PTE) (Dalcorso et al., 2010; Hameed et al., 2015; Maksymiec, 2007; Mei et al., 2018; Verma et al., 2016; Vishwakarma et al., 2017). Entrance of Cd into plant cells leads to the increase of cytosolic calcium levels due to the perturbation of the activity of phospholipase C and various channels such as inositol-3-phosphate-stimulated calcium channels and ADP ribose-gated channels (Chmielowska-Bąk et al., 2014). This increase of Ca2+ leads to signal transduction associated with ion transport and regulation of gene expression involved in plant metabolism and stress tolerance, respectively (Ghosh & Roy, 2019; Hameed et al., 2015; Shanmugaraj et al., 2019). For example, ectopic expression of CAXcd transporter involved in Ca2+/H+ transport in petunia under Cd stress (50 or 100 µM CdCl2 for 6 weeks) results in Cd tolerance and increase in accumulation of Cd (Wu et al., 2011).
Optimization using response surface methodology of phospholipase C production from Bacillus cereus suitable for soybean oil degumming
Published in Preparative Biochemistry & Biotechnology, 2023
Ines Abdelkader, Sameh Ben Mabrouk, Bilel Hadrich, Mohammed Refai, Ahmed Fendri, Adel Sayari
During enzymatic treatment, B. cereus phospholipase C hydrolyzes phospholipids present in the soybean crude oil to soluble DAG and water-soluble phosphate esters. The DAG remains in the refined oil. Therefore, PLC causes less oil to be preserved by the gums by decreasing the quantity of gums which contribute to ameliorate oil yield.[35,36]