Binding affinity analysis of the interaction between Homer EVH domain and ryanodine receptor with biosensors based on imaging ellipsometry

2016 ◽  
Vol 8 (14) ◽  
pp. 2936-2940
Author(s):  
Tengfei Kang ◽  
Kaiming Zhang ◽  
Changcheng Yin ◽  
Yu Niu ◽  
Gang Jin
Keyword(s):  
Calcium Signaling ◽  
Binding Affinity ◽  
Ryanodine Receptor ◽  
Skeletal Muscles ◽  
Imaging Ellipsometry

The interaction between the Homer EVH domain and RyR plays an important role in calcium signaling channels in the heart and the skeletal muscles. A biosensor based on imaging ellipsometry was used to analyze the binding affinity between the Homer EVH domain and RyR.

scholarly journals Skeletal Muscle Type Ryanodine Receptor Is Involved in Calcium Signaling in Human B Lymphocytes

1999 ◽  
Vol 274 (9) ◽  
pp. 5995-6002 ◽  
Author(s):  
Yoshitatsu Sei ◽  
Kathleen L. Gallagher ◽  
Anthony S. Basile
Keyword(s):  
Skeletal Muscle ◽  
Calcium Signaling ◽  
B Lymphocytes ◽  
Ryanodine Receptor ◽  
Muscle Type

scholarly journals Control of Neuronal Ryanodine Receptor-Mediated Calcium Signaling by Calsenilin

2018 ◽  
Vol 56 (1) ◽  
pp. 525-534 ◽  
Author(s):  
Michael A. Grillo ◽  
Stephanie L. Grillo ◽  
Bryan C. Gerdes ◽  
Jacob G. Kraus ◽  
Peter Koulen
Keyword(s):  
Calcium Signaling ◽  
Ryanodine Receptor

Vesl/Homer proteins regulate ryanodine receptor type 2 function and intracellular calcium signaling

Cell Calcium ◽  
2003 ◽  
Vol 34 (3) ◽  
pp. 261-269 ◽  
Author(s):  
Jens H Westhoff ◽  
Sung-Yong Hwang ◽  
R Scott Duncan ◽  
Fumiko Ozawa ◽  
Pompeo Volpe ◽  
...  
Keyword(s):  
Calcium Signaling ◽  
Intracellular Calcium ◽  
Ryanodine Receptor ◽  
Receptor Type ◽  
Intracellular Calcium Signaling ◽  
Homer Proteins

scholarly journals Evidence for the transport of glutathione through ryanodine receptor channel type 1

2003 ◽  
Vol 376 (3) ◽  
pp. 807-812 ◽  
Author(s):  
Gábor BÁNHEGYI ◽  
Miklós CSALA ◽  
Gábor NAGY ◽  
Vincenzo SORRENTINO ◽  
Rosella FULCERI ◽  
...  
Keyword(s):  
Ryanodine Receptor ◽  
Skeletal Muscles ◽  
Ruthenium Red ◽  
Lanthanum Chloride ◽  
Human Embryonic Kidney ◽  
Hek 293 ◽  
Channel Type ◽  
Receptor Channel

In the present study, we have investigated the role of RyR1 (ryanodine receptor calcium channel type 1) in glutathione (GSH) transport through the sarcoplasmic reticulum (SR) membrane of skeletal muscles. Lanthanum chloride, a prototypic blocker of cation channels, inhibited the influx and efflux of GSH in SR vesicles. Using a rapid-filtration-based assay and lanthanum chloride as a transport blocker, an uptake of radiolabelled GSH into SR vesicles was observed. Pretreatment of SR vesicles with the RyR1 antagonists Ruthenium Red and ryanodine as well as with lanthanum chloride blocked the GSH uptake. An SR-like GSH uptake appeared in microsomes obtained from an HEK-293 (human embryonic kidney 293) cell line after transfection of RyR1. These observations strongly suggest that RyR1 mediates GSH transport through the SR membranes of skeletal muscles.

Implication of the ryanodine receptor in TRPV4-induced calcium response in pulmonary arterial smooth muscle cells from normoxic and chronically hypoxic rats

2012 ◽  
Vol 303 (9) ◽  
pp. L824-L833 ◽  
Author(s):  
Diana Dahan ◽  
Thomas Ducret ◽  
Jean-François Quignard ◽  
Roger Marthan ◽  
Jean-Pierre Savineau ◽  
...  
Keyword(s):  
Smooth Muscle ◽  
Pulmonary Artery ◽  
Smooth Muscle Cells ◽  
Calcium Signaling ◽  
Ryanodine Receptor ◽  
Muscle Cells ◽  
Pulmonary Vasculature ◽  
Release Mechanism ◽  
Patch Clamp Technique ◽  
Calcium Response

There is a growing body of evidence indicating that transient receptor potential (TRP) channels are implicated in calcium signaling and various cellular functions in the pulmonary vasculature. The aim of this study was to investigate the expression, functional role, and coupling to reticulum calcium channels of the type 4 vanilloid TRP subfamily (TRPV4) in the pulmonary artery from both normoxic (Nx) and chronically hypoxic (CH) rats. Activation of TRPV4 with the specific agonist 4α-phorbol-12,13-didecanoate (4α-PDD, 5 μM) increased the intracellular calcium concentration ([Ca2+]i). This effect was significantly reduced by a high concentration of ryanodine (100 μM) or chronic caffeine (5 mM) that blocked ryanodine receptor (RyR) but was insensitive to xestospongin C (10 μM), an inositol trisphosphate receptor antagonist. Inhibition of RyR1 and RyR3 only with 10 μM of dantrolene did not attenuate the 4α-PDD-induced [Ca2+]i increase. Western blotting experiments revealed the expression of TRPV4 and RyR2 with an increase in both receptors in pulmonary arteries from CH rats vs. Nx rats. Accordingly, the 4α-PDD-activated current, measured with patch-clamp technique, was increased in pulmonary artery smooth muscle cells (PASMC) from CH rats vs. Nx rats. 4α-PDD increased isometric tension in artery rings, and this response was also potentiated under chronic hypoxia conditions. 4α-PDD-induced calcium response, current, and contraction were all inhibited by the selective TRPV4 blocker HC-067047. Collectively, our findings provide evidence of the interplay between TRPV4 and RyR2 in the Ca2+ release mechanism and contraction in PASMC. This study provides new insights onto the complex calcium signaling in PASMC and point out the importance of the TRPV4-RyR2 signaling pathway under hypoxic conditions that may lead to pulmonary hypertension.

Ryanodine receptor Ca2+ release channels: does diversity in form equal diversity in function?

1996 ◽  
Vol 76 (4) ◽  
pp. 1027-1071 ◽  
Author(s):  
J. L. Sutko ◽  
J. A. Airey
Keyword(s):  
Intracellular Calcium ◽  
Ryanodine Receptor ◽  
Skeletal Muscles ◽  
Calcium Release ◽  
Cell Types ◽  
Calcium Transients ◽  
Eukaryotic Cells ◽  
Calcium Release Channels ◽  
Primary Focus ◽  
Fast Twitch

Complexities in calcium signaling in eukaryotic cells require diversity in the proteins involved in generating these signals. In this review, we consider the ryanodine receptor (RyR) family of intracellular calcium release channels. This includes species, tissue, and cellular distributions of the RyRs and mechanisms of activation, deactivation, and inactivation of RyR calcium release events. In addition, as first observed in nonmammalian vertebrate skeletal muscles, it is now clear that more than one RyR isoform is frequently coexpressed within many cell types. How multiple ryanodine receptor release channels are used to generate intracellular calcium transients is unknown. Therefore, a primary focus of this review is why more than one RyR is required for this purpose, particularly in a tissue, such as vertebrate fast-twitch skeletal muscles, where a relatively simple and straightforward change in calcium would appear to be required to elicit contraction. Finally, the roles of the RyR isoforms and the calcium release events they mediate in the development of embryonic skeletal muscle are considered.

scholarly journals MG53 suppresses interferon-β and inflammation via regulation of ryanodine receptor-mediated intracellular calcium signaling

2020 ◽  
Vol 11 (1) ◽  
Author(s):  
Matthew Sermersheim ◽  
Adam D. Kenney ◽  
Pei-Hui Lin ◽  
Temet M. McMichael ◽  
Chuanxi Cai ◽  
...  
Keyword(s):  
Calcium Signaling ◽  
Intracellular Calcium ◽  
Ryanodine Receptor ◽  
Interferon Β ◽  
Intracellular Calcium Signaling

scholarly journals Unitary Ca2+ Current through Mammalian Cardiac and Amphibian Skeletal Muscle Ryanodine Receptor Channels under Near-physiological Ionic Conditions

2003 ◽  
Vol 122 (4) ◽  
pp. 407-417 ◽  
Author(s):  
Claudia Kettlun ◽  
Adom González ◽  
Eduardo Ríos ◽  
Michael Fill
Keyword(s):  
Skeletal Muscle ◽  
Charge Carrier ◽  
Lipid Bilayers ◽  
Ryanodine Receptor ◽  
Skeletal Muscles ◽  
Planar Lipid Bilayers ◽  
High Concentrations

Ryanodine receptor (RyR) channels from mammalian cardiac and amphibian skeletal muscle were incorporated into planar lipid bilayers. Unitary Ca2+ currents in the SR lumen-to-cytosol direction were recorded at 0 mV in the presence of caffeine (to minimize gating fluctuations). Currents measured with 20 mM lumenal Ca2+ as exclusive charge carrier were 4.00 and 4.07 pA, respectively, and not significantly different. Currents recorded at 1–30 mM lumenal Ca2+ concentrations were attenuated by physiological [K+] (150 mM) and [Mg2+] (1 mM), in the same proportion (∼55%) in mammalian and amphibian channels. Two amplitudes, differing by ∼35%, were found in amphibian channel studies, probably corresponding to α and β RyR isoforms. In physiological [Mg2+], [K+], and lumenal [Ca2+] (1 mM), the Ca2+ current was just less than 0.5 pA. Comparison of this value with the Ca2+ flux underlying Ca2+ sparks suggests that sparks in mammalian cardiac and amphibian skeletal muscles are generated by opening of multiple RyR channels. Further, symmetric high concentrations of Mg2+ substantially reduced the current carried by 10 mM Ca2+ (∼40% at 10 mM Mg2+), suggesting that high Mg2+ may make sparks smaller by both inhibiting RyR gating and reducing unitary current.

Sign in / Sign up

Export Citation Format

Share Document