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Ion Channels in Immune Cells
Published in Shyam S. Bansal, Immune Cells, Inflammation, and Cardiovascular Diseases, 2022
Devasena Ponnalagu, Shridhar Sanghvi, Shyam S. Bansal, Harpreet Singh
The mammalian TRP channel superfamily comprises 28 cation-selective channels57. On the basis of their sequence and structural homology, TRP channel family members are classified into six main groups, which include canonical (TRPC), melastatin (TRPM), vanilloid (TRPV), mucolipin (TRPM), polycystin (TRPP), and ankyrin (TRPA) channel proteins57. All of the members of the TRP channel family of proteins comprise six transmembrane helices that combine as tetramers to form a cation-selective pore58. They exhibit polymodal activation properties and, therefore, become activated upon alteration in temperature, pH, and osmolarity12. A body of evidence shows their importance not only in the sensory system but also in various physiological and pathophysiological conditions like cancer, neural development, and cardiac and renal physiology.
Genetics and genomics of exposure to high altitude
Published in Andrew M. Luks, Philip N. Ainslie, Justin S. Lawley, Robert C. Roach, Tatum S. Simonson, Ward, Milledge and West's High Altitude Medicine and Physiology, 2021
Andrew M. Luks, Philip N. Ainslie, Justin S. Lawley, Robert C. Roach, Tatum S. Simonson
Alveolar hypoxia (for example, as occurs at high altitude) causes hypoxic pulmonary vasoconstriction, which, if present for sufficient duration, leads to pulmonary vascular remodeling, including thickening of the vessel wall due to the proliferation of smooth muscle and fibroblasts and extension of smooth muscle cells into previously nonmuscular precapillary arterioles. Recently, a role for HIF-1α and HIF-2α in the development of hypoxic pulmonary hypertension has been investigated. It is known that increases in intracellular calcium ion concentration and intracellular pH contribute to the growth and contraction of pulmonary artery smooth muscle cells under hypoxic conditions. There is evidence that the increase in intracellular pH is related to an increased activity and expression of the sodium/hydrogen ion exchanger isoform 1 (NHE1) (Rios et al. 2005). In addition, the increase in intracellular calcium ion concentration is due to the increased expression of canonical transient receptor potential (TRPC) proteins and enhanced calcium ion entry through nonselective cation channels (Wang et al. 2006). Both the increase in intracellular pH and calcium ion concentration are mediated by HIF-1 (Shimoda et al. 2001).
Structural Determination of the Polycystin-2 Channel by Electron Cryo-Microscopy
Published in Jinghua Hu, Yong Yu, Polycystic Kidney Disease, 2019
The TRP channels conduct cations and are grouped into seven subfamilies according to the relatedness of their protein sequences: TRPC (canonical), TRPM (melastatin), TRPA (ankyrin), TRPV (vanilloid), TRPN (NOMPC-like), TRPML (mucolipin), and TRPP (polycystin).44,61 All TRP channel subfamilies, except for TRPN, are present in mammals. In humans, 27 TRP proteins have been identified, making the TRP family the second largest ion channel family, only outnumbered by the potassium-channel family. The TRP channels are sensory proteins that detect and integrate numerous environmental and endogenous stimuli to elicit proper cellular responses. Some TRP channels operate downstream of, or retain the ability to be regulated by, phospholipase C (PLC)-coupled receptors, as first discovered in the ancestral fly TRPs.62,63 However, for most mammalian TRP channels, the in vivo activation mechanisms are yet to be determined.64
Plasma long non-coding RNAs ASMTL-AS1, AP001363.1, AC005730.3 and AL133415.1 as a potential biomarker for Alzheimer’s disease
Published in Neurological Research, 2023
Yi Cheng, Xiaohui Zhou, Ting Zou, Lei Zhang, Lihua Li, Chang Yang, Long Ma
To reveal the potential roles of these lncRNAs, we performed GO analysis based on the differentially expressed lncRNAs in the plasma. In agreement, our findings also showed that the peripheral blood of AD patients and control groups exhibited differential expression of protein-coding genes. GO enrichment analyses of lncRNAs indicated that homologous recombination, glycine, serine, and threonine metabolism, inflammatory mediator regulation of TRP channels, mismatch repair, and Alzheimer’s disease were significantly affected in the two groups. Transient receptor potential (TRP) channels are divided into 28 members that serve as non-selective calcium channels located on the cell membrane and are highly expressed in brain neurons. Research has shown that TRPC channels are involved in proliferation, intracellular Ca2+ and Mg2+ homeostasis, differentiation, apoptosis, degeneration, and synaptic plasticity in the nervous system [46].
Transient receptor potential canonical 6 knockdown ameliorated diabetic kidney disease by inhibiting nuclear factor of activated T cells 2 expression in glomerular mesangial cells
Published in Renal Failure, 2022
Jian Yu, Chunchun Li, Lisha Ma, Bin Zhai, Aiping Xu, Decui Shao
Transient receptor potential (TRPC) 6, a Ca2+-conductive cation channel, is one member of the seven-member family of TRPCs [7]. Transient receptor potential canonical 6 (TRPC6) is extensively expressed in kidneys, including GMCs, podocytes, and kidney tubular epithelial cells [8]. TRPC6 plays an important role in kidney function control, and TRPC6 dysregulation is associated with kidney pathophysiological changes. TRPC6 mutation results in hereditary focal segmental glomerulosclerosis [9]. The upregulation of TRPC6 is a common feature of patients with proteinuria, and overexpression of TRPC6 in mice causes proteinuria [10]. TRPC6 activation also plays a crucial role in podocyte injury by regulating actin cytoskeleton dynamics [11,12]. Inhibition of TRPC6 in podocytes and kidney tubular epithelial cells can attenuate DKD [13,14]. Previous studies have also shown that TRPC6 regulates the contractile function and proliferation of GMCs [15,16].
The light-activated TRP channel: the founding member of the TRP channel superfamily
Published in Journal of Neurogenetics, 2022
The trp gene was subsequently cloned and molecularly characterized by Montell and Rubin (Montell & Rubin, 1989) and shortly afterward by Wong et al. (1989, for a detailed outline of these studies see (Minke, 2010)). This was an important achievement for it allowed cloning of mammalian genes of the TRP channels superfamily, ultimately leading to the identification of a new subfamily of mammalian trp genes (the TRPC subfamily). However, cloning of the Drosophila trp gene did not lead immediately to the recognition of its function as a light-activated ion channel. Sequencing revealed that the Drosophila trp gene encodes a1275 amino-acid transmembrane protein with no homologies to any known protein in the data base at that time. It had eight transmembrane domains that were later on revised to six trans-membrane segments (S1-6) with a pore region composed of S5-S6 and a pore helix (see Figure 3) and displayed many topological features reminiscent of receptor-transporter-channel proteins. However, the possibility that it might encode a light-activated channel was initially ruled out because light responses were present in trp mutants that showed no protein product in Western blot analyses (Montell & Rubin, 1989). Similarly, Wong et al. (1989) also concluded that ‘functions of the elements in the primary path of excitation … are not dependent on the trp protein’.