scholarly journals G-protein modulation of N-type calcium channel gating current in human embryonic kidney cells (HEK 293).

1997 ◽  
Vol 498 (3) ◽  
pp. 601-610 ◽  
Author(s):  
L P Jones ◽  
P G Patil ◽  
T P Snutch ◽  
D T Yue
Keyword(s):  
Calcium Channel ◽  
G Protein ◽  
Channel Gating ◽  
Kidney Cells ◽  
Gating Current ◽  
Human Embryonic Kidney ◽  
Hek 293 ◽  
Human Embryonic Kidney Cells

scholarly journals Caffeine induces Ca2+ release by reducing the threshold for luminal Ca2+ activation of the ryanodine receptor

2008 ◽  
Vol 414 (3) ◽  
pp. 441-452 ◽  
Author(s):  
Huihui Kong ◽  
Peter P. Jones ◽  
Andrea Koop ◽  
Lin Zhang ◽  
Henry J. Duff ◽  
...  
Keyword(s):  
Ryanodine Receptor ◽  
Cardiac Arrhythmias ◽  
Single Channel ◽  
Kidney Cells ◽  
Human Embryonic Kidney ◽  
Activation Threshold ◽  
Hek 293 ◽  
Human Embryonic Kidney Cells ◽  
293 Cells ◽  
High Concentrations

Caffeine has long been used as a pharmacological probe for studying RyR (ryanodine receptor)-mediated Ca2+ release and cardiac arrhythmias. However, the precise mechanism by which caffeine activates RyRs is elusive. In the present study, we investigated the effects of caffeine on spontaneous Ca2+ release and on the response of single RyR2 (cardiac RyR) channels to luminal or cytosolic Ca2+. We found that HEK-293 cells (human embryonic kidney cells) expressing RyR2 displayed partial or ‘quantal’ Ca2+ release in response to repetitive additions of submaximal concentrations of caffeine. This quantal Ca2+ release was abolished by ryanodine. Monitoring of endoplasmic reticulum luminal Ca2+ revealed that caffeine reduced the luminal Ca2+ threshold at which spontaneous Ca2+ release occurs. Interestingly, spontaneous Ca2+ release in the form of Ca2+ oscillations persisted in the presence of 10 mM caffeine, and was diminished by ryanodine, demonstrating that unlike ryanodine, caffeine, even at high concentrations, does not hold the channel open. At the single-channel level, caffeine markedly reduced the threshold for luminal Ca2+ activation, but had little effect on the threshold for cytosolic Ca2+ activation, indicating that the major action of caffeine is to reduce the luminal, but not the cytosolic, Ca2+ activation threshold. Furthermore, as with caffeine, the clinically relevant, pro-arrhythmic methylxanthines aminophylline and theophylline potentiated luminal Ca2+ activation of RyR2, and increased the propensity for spontaneous Ca2+ release, mimicking the effects of disease-linked RyR2 mutations. Collectively, our results demonstrate that caffeine triggers Ca2+ release by reducing the threshold for luminal Ca2+ activation of RyR2, and suggest that disease-linked RyR2 mutations and RyR2-interacting pro-arrhythmic agents may share the same arrhythmogenic mechanism.

scholarly journals Evaluation of the effect of montelukast on cadmium induced toxicity in human embryonic kidney cells (HEK-293)

2019 ◽  
Vol 24 (4) ◽  
pp. 125-137
Author(s):  
Farnoosh Kaviani ◽  
Seyedeh Missagh Jalali ◽  
Elham Hoveizi ◽  
Javad Jamshidian ◽  
Masoomeh Ahmadizadeh ◽  
...  
Keyword(s):  
Kidney Cells ◽  
Human Embryonic Kidney ◽  
Hek 293 ◽  
Human Embryonic Kidney Cells

scholarly journals A novel UBA and UBX domain protein that binds polyubiquitin and VCP and is a substrate for SAPKs

2004 ◽  
Vol 384 (2) ◽  
pp. 391-400 ◽  
Author(s):  
Helen McNEILL ◽  
Axel KNEBEL ◽  
J. Simon C. ARTHUR ◽  
Ana CUENDA ◽  
Philip COHEN
Keyword(s):  
Kidney Cells ◽  
Human Embryonic Kidney ◽  
Glutathione S Transferase ◽  
Hek 293 ◽  
Human Embryonic Kidney Cells ◽  
Extracellular Signal Regulated Kinase ◽  
Cell Extracts ◽  
Extracellular Signal ◽  
Sb 203580

A widely expressed protein containing UBA (ubiquitin-associated) and UBX (ubiquitin-like) domains was identified as a substrate of SAPKs (stress-activated protein kinases). Termed SAKS1 (SAPK substrate-1), it was phosphorylated efficiently at Ser200in vitro by SAPK3/p38γ, SAPK4/p38δ and JNK (c-Jun N-terminal kinase), but weakly by SAPK2a/p38α, SAPK2b/p38β2 or ERK (extracellular-signal-regulated kinase) 2. Ser200, situated immediately N-terminal to the UBX domain, became phosphorylated in HEK-293 (human embryonic kidney) cells in response to stressors. Phosphorylation was not prevented by SB 203580 (an inhibitor of SAPK2a/p38α and SAPK2b/p38β2) and/or PD 184352 (which inhibits the activation of ERK1 and ERK2), and was similar in fibroblasts lacking both SAPK3/p38γ and SAPK4/p38δ or JNK1 and JNK2. SAKS1 bound ubiquitin tetramers and VCP (valosin-containing protein) in vitro via the UBA and UBX domains respectively. The amount of VCP in cell extracts that bound to immobilized GST (glutathione S-transferase)–SAKS1 was enhanced by elevating the level of polyubiquitinated proteins, while SAKS1 and VCP in extracts were coimmunoprecipitated with an antibody raised against S5a, a component of the 19 S proteasomal subunit that binds polyubiquitinated proteins. PNGase (peptide N-glycanase) formed a 1:1 complex with VCP and, for this reason, also bound to immobilized GST–SAKS1. We suggest that SAKS1 may be an adaptor that directs VCP to polyubiquitinated proteins, and PNGase to misfolded glycoproteins, facilitating their destruction by the proteasome.

scholarly journals Cellular gene expression survey of PseudoRabies Virus (PRV) infected Human Embryonic Kidney cells (HEK-293)

2006 ◽  
Vol 37 (5) ◽  
pp. 705-723 ◽  
Author(s):  
Yannick Blanchard ◽  
Nolwenn Le Meur ◽  
Martine Le Cunff ◽  
Philippe Blanchard ◽  
Jean Léger ◽  
...  
Keyword(s):  
Gene Expression ◽  
Pseudorabies Virus ◽  
Kidney Cells ◽  
Human Embryonic Kidney ◽  
Cellular Gene ◽  
Cellular Gene Expression ◽  
Hek 293 ◽  
Human Embryonic Kidney Cells

Hyperthermia with Magnetic Nanowires for Inactivating Living Cells

2008 ◽  
Vol 8 (5) ◽  
pp. 2323-2327 ◽  
Author(s):  
D. S. Choi ◽  
J. Park ◽  
S. Kim ◽  
D. H. Gracias ◽  
M. K. Cho ◽  
...  
Keyword(s):  
Cell Death ◽  
Magnetic Moments ◽  
Magnetic Hysteresis ◽  
Kidney Cells ◽  
Magnetic Nanowires ◽  
Human Embryonic Kidney ◽  
Lower Field ◽  
Hek 293 ◽  
Human Embryonic Kidney Cells

We describe a method to induce hyperthermia in cells, in-vitro, by remotely heating Ni nanowires (NWs) with radio frequency (RF) electromagnetic fields. Ni NWs were internalized by human embryonic kidney cells (HEK-293). Only cells proximal to NWs or with internalized NWs changed shape on exposure to RF fields indicative of cell death. The cell death occurs as a result of hyperthermia, since the RF field remotely heats the NWs as a result of magnetic hysteresis. This is the first demonstration of hyperthermia induced by NWs; since the NWs have anisotropic and strong magnetic moments, our experiments suggest the possibility of performing hyperthermia at lower field strengths in order to minimize damage to untargeted cells in applications such as the treatment of cancer.

scholarly journals A magzatok és embriók kereskedelmi és ipari célú felhasználásának morális és jogi kérdései

Pro Futuro ◽  
2015 ◽  
Vol 5 (2) ◽  
pp. 55-69
Author(s):  
Petra Lea Lánczos
Keyword(s):  
Kidney Cells ◽  
Human Embryonic Kidney ◽  
Hek 293 ◽  
Human Embryonic Kidney Cells ◽  
Skin Cell

Napjainkra a kereskedelmi forgalomban kapható egyes fogyasztási cikkek magzatok sejtjeinek, szöveteinek felhasználásával készülnek. Ilyen termékek különösen egyes vakcinák, kozmetikai cikkek vagy akár élelmiszerek. A védőoltások körében számos vakcina, így például a hazánkban is kötelező védőoltás, a mumpsz- kanyaró-rubeola (MMR) ellen kifejlesztett, Magyarországon engedélyezett és forgalomban lévő oltóanyag (MMR-VAXPRO) művi abortuszból származó sejtvonalak felhasználásával készült. A kozmetikai termékek körében a neocutis svájci kozmetikai cég PSP® (Processed Skin Cell Proteins) fejlesztésével kapcsolatban láttak napvilágot olyan hírek, miszerint a PSP®-összetevő abortumból származó sejtvonalakkal készült. Végül, az élelmiszergyártás területén az Egyesült Államokbeli Senomyx vállalat került reflektorfénybe a HEK 293 (Human Embryonic Kidney cells) sejtvonalak miatt, mellyel élelmiszergyártó cégek termékeihez fejlesztettek ízfokozókat.

Sign in / Sign up

Export Citation Format

Share Document