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Calcium plays a crucial role in excitation-contraction coupling (ECC), but it is also a pivotal second messenger activating Ca(2+)-dependent transcription factors in a process termed excitation-transcription coupling (ETC). Evidence accumulated over the past decade indicates a pivotal role of inositol 1,4,5-trisphosphate receptor (IP3R)-mediated Ca(2+) release in the regulation of cytosolic and nuclear Ca(2+) signals. IP3 is generated by stimulation of plasma membrane receptors that couple to phospholipase C (PLC), liberating IP3 from phosphatidylinositol 4,5-bisphosphate (PIP2). An intriguing aspect of IP3 signaling is the presence of the entire PIP2-PLC-IP3 signaling cascade as well as the presence of IP3Rs at the inner and outer membranes of the nuclear envelope (NE) which functions as a Ca(2+) store. The observation that the nucleus is surrounded by its own putative Ca(2+) store raises the possibility that nuclear IP3-dependent Ca(2+) release plays a critical role in ETC. This provides a potential mechanism of regulation that acts locally and autonomously from the global cytosolic Ca(2+) signal underlying ECC. Moreover, there is evidence that: (i) the sarcoplasmic reticulum (SR) and NE are a single contiguous Ca(2+) store; (ii) the nuclear pore complex is the major gateway for Ca(2+) and macromolecules to pass between the cytosol and the nucleoplasm; (iii) the inner membrane of the NE hosts key Ca(2+) handling proteins including the Na(+)/Ca(2+) exchanger (NCX)/GM1 complex, ryanodine receptors (RyRs), nicotinic acid adenine dinucleotide phosphate receptors (NAADPRs), Na(+)/K(+) ATPase, and Na(+)/H(+) exchanger. Thus, it appears that the nucleus represents a Ca(2+) signaling domain equipped with its own ion channels and transporters that allow for complex local Ca(2+) signals. Many experimental and modeling approaches have been used for the study of intracellular Ca(2+) signaling but the key to the understanding of the dual role of Ca(2+) mediating ECC and ECT lays in quantitative differences of local [Ca(2+)] in the nuclear and cytosolic compartment. In this review, we discuss the state of knowledge regarding the origin and the physiological implications of nuclear Ca(2+) transients in different cardiac cell types (adult atrial and ventricular myocytes) as well as experimental and mathematical approaches to study Ca(2+) and IP3 signaling in the cytosol and nucleus. In particular, we focus on the concept that highly localized Ca(2+) signals are required to translocate and activate Ca(2+)-dependent transcription factors (e.g., nuclear factor of activated T-cells, NFAT; histone deacetylase, HDAC) through phosphorylation/dephosphorylation processes.
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http://dx.doi.org/10.3389/fphar.2014.00035 | DOI Listing |
J Phys Chem B
December 2024
Shanghai Engineering Research Center of Molecular Therapeutics and New Drug Development, Shanghai Frontiers Science Center of Molecule Intelligent Syntheses, School of Chemistry and Molecular Engineering, East China Normal University, Shanghai 200062, China.
The high activity of water in aqueous battery electrolytes can trigger side reactions, limiting their large-scale application. Additives that form contact pairs (CPs) with cations by coordinating with them can effectively reduce water's activity. However, due to the complex interactions between ions, additives, and solvent molecules and the fact that current strategies for additive screening primarily rely on static physical parameters, the dynamic mechanisms that govern the modulation of ion solvation sheaths are still poorly understood.
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Department of Pharmaceutics, School of Pharmacy, Qingdao University, Qingdao 266021, China. Electronic address:
Platinum (Pt)-based anticancer agents exhibit a lack of selectivity in the treatment of osteosarcoma, resulting in significant toxicity. Furthermore, immune surveillance withinthe tumor microenvironment impedes the uptake of platinum drugs by osteosarcoma cells. To overcome these challenges, an oxaliplatin-based Pt prodrug amphiphile (Lipo-OXA-ALN) was designed and synthesized by incorporatingan osteosarcoma-targeting alendronate (ALN) alongside a lipid tail.
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Department of Biochemistry, College of Medicine, Jeju Research Center for Natural Medicine, Jeju National University, Jeju 63243, Republic of Korea. Electronic address:
Particulate matter 2.5 (PM) exposure is responsible for skin inflammation, aging, and disruption of skin homeostasis. The objective of this investigation was to assess the potential of myricetin in protecting against skin damage caused by PM.
View Article and Find Full Text PDFCurr Microbiol
December 2024
College of Agriculture and Life Sciences, Kunming University, 2 Pu Xin Road, Kunming, 650214, Yunnan, China.
β-Glucosidase plays a pivotal role in transforming ginsenosides into specific minor ginsenosides. In this study, total ginsenosides from Panax notoginseng leaves were used as substrates to stimulate the growth of Aspergillus niger NG1306. Transcriptome analysis identified a β-glucosidase gene, Anglu04478 (1455 bp, 484 amino acids, 54.
View Article and Find Full Text PDFElife
December 2024
Experimental Otology Group, InnerEarLab, Department of Otolaryngology, University Medical Center Göttingen, Göttingen, Germany.
To encode continuous sound stimuli, the inner hair cell (IHC) ribbon synapses utilize calcium-binding proteins (CaBPs), which reduce the inactivation of their Ca1.3 calcium channels. Mutations in the gene underlie non-syndromic autosomal recessive hearing loss DFNB93.
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