191 TRANSIENT RECEPTOR POTENTIAL SUPERFAMILY OF ION CHANNELS, TRPV6, IS CONSTITUTIVELY EXPRESSED AND REGULATED BY ESTROGEN IN THE HUMAN UTERUS DURING THE MENSTRUAL CYCLE

2011 ◽  
Vol 23 (1) ◽  
pp. 196
Author(s):  
Y.-K. Kim ◽  
H. Yang ◽  
E.-B. Jeung
Keyword(s):  
Ion Channels ◽  
Menstrual Cycle ◽  
Brush Border Membrane ◽  
Transient Receptor Potential ◽  
Prostate Gland ◽  
Receptor Potential ◽  
Human Uterus ◽  
Proximal Small Intestine ◽  
Transient Receptor ◽  
Human Menstrual Cycle

Two highly selective calcium channels at the apical sides of cells, members of the transient receptor potential (TRP) superfamily of ion channels (TRPV6 and TRPV5), are the main calcium ion entry channels. Previously, the location of TRPV6 has been described in the intestine in several species, including humans. It is located in the apical brush-border membrane of the intestinal enterocyte, where it regulates calcium entry into the cell. It is most abundant in the proximal small intestine (duodenum and jejunum), where calbindin and the calcium-pumping ATPase are also found. The TRPV6 calcium transporter is also found in the human placenta, pancreas, and prostate gland in some species. However, TRPV6 expression and its potential roles remain to be clarified in the endometrium of humans during the menstrual cycle. In this study, we used a human endometrial model to examine the expression of TRPV6 and its potential roles in the human menstrual cycle. A significant increase (1.5-fold) in the TRPV6 transcript and protein was observed in the human uterus at the proliferation phase compared with other phases. In addition, the spatial localization of TRPV6 in the human uterus was determined by immunohistochemistry. Uterine TRPV6 was abundantly localised in the cytoplasm of the endometrial and glandular epithelial cells in the menstrual phases. Overall, these results demonstrate that TRPV6 is abundantly expressed in human uterine tissue, suggesting that this protein may be involved in reproductive functions during the menstrual cycle in humans.

scholarly journals The transient receptor potential, TRP4, cation channel is a novel member of the family of calmodulin binding proteins

2001 ◽  
Vol 355 (3) ◽  
pp. 663-670 ◽  
Author(s):  
Claudia TROST ◽  
Christiane BERGS ◽  
Nina HIMMERKUS ◽  
Veit FLOCKERZI
Keyword(s):  
Amino Acid ◽  
Ion Channels ◽  
Transient Receptor Potential ◽  
Direct Interaction ◽  
Receptor Potential ◽  
Amino Acid Residues ◽  
Glutathione S Transferase ◽  
Calmodulin Binding ◽  
Transient Receptor

The mammalian gene products, transient receptor potential (trp)1 to trp7, are related to the Drosophila TRP and TRP-like ion channels, and are candidate proteins underlying agonist-activated Ca2+-permeable ion channels. Recently, the TRP4 protein has been shown to be part of native store-operated Ca2+-permeable channels. These channels, most likely, are composed of other proteins in addition to TRP4. In the present paper we report the direct interaction of TRP4 and calmodulin (CaM) by: (1) retention of in vitro translated TRP4 and of TRP4 protein solubilized from bovine adrenal cortex by CaM–Sepharose in the presence of Ca2+, and (2) TRP4–glutathione S-transferase pull-down experiments. Two domains of TRP4, amino acid residues 688–759 and 786–848, were identified as being able to interact with CaM. The binding of CaM to both domains occurred only in the presence of Ca2+ concentrations above 10µM, with half maximal binding occurring at 16.6µM (domain 1) and 27.9µM Ca2+ (domain 2). Synthetic peptides, encompassing the two putative CaM binding sites within these domains and covering amino acid residues 694–728 and 829–853, interacted directly with dansyl–CaM with apparent Kd values of 94–189nM. These results indicate that TRP4/Ca2+-CaM are parts of a signalling complex involved in agonist-induced Ca2+ entry.

scholarly journals Alternative Splicing of a Protein Domain Indispensable for Function of Transient Receptor Potential Melastatin 3 (TRPM3) Ion Channels

2012 ◽  
Vol 287 (44) ◽  
pp. 36663-36672 ◽  
Author(s):  
Julia Frühwald ◽  
Julia Camacho Londoño ◽  
Sandeep Dembla ◽  
Stefanie Mannebach ◽  
Annette Lis ◽  
...  
Keyword(s):  
Alternative Splicing ◽  
Ion Channels ◽  
Transient Receptor Potential ◽  
Receptor Potential ◽  
Protein Domain ◽  
Transient Receptor Potential Melastatin ◽  
Transient Receptor

scholarly journals Calcium-permeable ion channels in the kidney

2016 ◽  
Vol 310 (11) ◽  
pp. F1157-F1167 ◽  
Author(s):  
Yiming Zhou ◽  
Anna Greka
Keyword(s):  
Ion Channels ◽  
Ion Channel ◽  
Transient Receptor Potential ◽  
Kidney Development ◽  
Kidney Diseases ◽  
Receptor Potential ◽  
Transient Receptor Potential Channels ◽  
Cellular Functions ◽  
Potential Channels ◽  
Transient Receptor

Calcium ions (Ca2+) are crucial for a variety of cellular functions. The extracellular and intracellular Ca2+ concentrations are thus tightly regulated to maintain Ca2+ homeostasis. The kidney, one of the major organs of the excretory system, regulates Ca2+ homeostasis by filtration and reabsorption. Approximately 60% of the Ca2+ in plasma is filtered, and 99% of that is reabsorbed by the kidney tubules. Ca2+ is also a critical signaling molecule in kidney development, in all kidney cellular functions, and in the emergence of kidney diseases. Recently, studies using genetic and molecular biological approaches have identified several Ca2+-permeable ion channel families as important regulators of Ca2+ homeostasis in kidney. These ion channel families include transient receptor potential channels (TRP), voltage-gated calcium channels, and others. In this review, we provide a brief and systematic summary of the expression, function, and pathological contribution for each of these Ca2+-permeable ion channels. Moreover, we discuss their potential as future therapeutic targets.

scholarly journals Carboxamido steroids inhibit the opening properties of transient receptor potential ion channels by lipid raft modulation

2018 ◽  
Vol 59 (10) ◽  
pp. 1851-1863 ◽  
Author(s):  
Éva Sághy ◽  
Maja Payrits ◽  
Tünde Bíró-Sütő ◽  
Rita Skoda-Földes ◽  
Eszter Szánti-Pintér ◽  
...  
Keyword(s):  
Ion Channels ◽  
Lipid Raft ◽  
Transient Receptor Potential ◽  
Receptor Potential ◽  
Transient Receptor

scholarly journals Confined Dynamics of Water in Transmembrane Pore of TRPV1 Ion Channel

2019 ◽  
Vol 20 (17) ◽  
pp. 4285
Author(s):  
Yury A. Trofimov ◽  
Nikolay A. Krylov ◽  
Roman G. Efremov
Keyword(s):  
Ion Channels ◽  
Transient Receptor Potential ◽  
3D Structure ◽  
Receptor Potential ◽  
Md Simulations ◽  
Transient Receptor Potential Vanilloid ◽  
Free Energy Barrier ◽  
Transmembrane Pores ◽  
Ion Conducting ◽  
Transient Receptor

Solvation effects play a key role in chemical and biological processes. The microscopic properties of water near molecular surfaces are radically different from those in the bulk. Furthermore, the behavior of water in confined volumes of a nanometer scale, including transmembrane pores of ion channels, is especially nontrivial. Knowledge at the molecular level of structural and dynamic parameters of water in such systems is necessary to understand the mechanisms of ion channels functioning. In this work, the results of molecular dynamics (MD) simulations of water in the pore and selectivity filter domains of TRPV1 (Transient Receptor Potential Vanilloid type 1) membrane channel are considered. These domains represent nanoscale volumes with strongly amphiphilic walls, where physical behavior of water radically differs from that of free hydration (e.g., at protein interfaces) or in the bulk. Inside the pore and filter domains, water reveals a very heterogeneous spatial distribution and unusual dynamics: It forms compact areas localized near polar groups of particular residues. Residence time of water molecules in such areas is at least 1.5 to 3 times larger than that observed for similar groups at the protein surface. Presumably, these water “blobs” play an important role in the functional activity of TRPV1. In particular, they take part in hydration of the hydrophobic TRPV1 pore by localizing up to six waters near the so-called “lower gate” of the channel and reducing by this way the free energy barrier for ion and water transport. Although the channel is formed by four identical protein subunits, which are symmetrically packed in the initial experimental 3D structure, in the course of MD simulations, hydration of the same amino acid residues of individual subunits may differ significantly. This greatly affects the microscopic picture of the distribution of water in the channel and, potentially, the mechanism of its functioning. Therefore, reconstruction of the full picture of TRPV1 channel solvation requires thorough atomistic simulations and analysis. It is important that the naturally occurring porous volumes, like ion-conducting protein domains, reveal much more sophisticated and fine-tuned regulation of solvation than, e.g., artificially designed carbon nanotubes.

Sign in / Sign up

Export Citation Format

Share Document