Characterization of plasma membrane redox activity from ehrlich cells

1994 ◽  
Vol 12 (2) ◽  
pp. 149-152 ◽  
Author(s):  
Antonio Del Castillo-Olivares ◽  
Javier Márquez ◽  
Ignacio Núñez De Castro ◽  
Miguel Angel Medina
Keyword(s):  
Plasma Membrane ◽  
Redox Activity ◽  
Ehrlich Cells ◽  
Plasma Membrane Redox

scholarly journals Plasma membrane redox activity correlates with N-myc expression in neuroblastoma cells

FEBS Letters ◽  
1992 ◽  
Vol 311 (2) ◽  
pp. 99-101 ◽  
Author(s):  
Miguel Angel Medina ◽  
Antonio del Castillo-Olivares ◽  
Lothar Schweigerer
Keyword(s):  
Plasma Membrane ◽  
Neuroblastoma Cells ◽  
Redox Activity ◽  
Plasma Membrane Redox

PHYTOPLANKTON PLASMA MEMBRANE REDOX ACTIVITY: EFFECT OF IRON LIMITATION AND INTERACTION WITH PHOTOSYNTHESIS1

2003 ◽  
Vol 39 (6) ◽  
pp. 1132-1144 ◽  
Author(s):  
Margaret S. Davey ◽  
David J. Suggett ◽  
Richard J. Geider ◽  
Alison R. Taylor
Keyword(s):  
Plasma Membrane ◽  
Iron Limitation ◽  
Redox Activity ◽  
Plasma Membrane Redox ◽  
Activity Effect

scholarly journals Fluorescence Fluctuation Spectroscopy enables quantification of potassium channel subunit dynamics and stoichiometry

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Giulia Tedeschi ◽  
Lorenzo Scipioni ◽  
Maria Papanikolaou ◽  
Geoffrey W. Abbott ◽  
Michelle A. Digman
Keyword(s):  
Plasma Membrane ◽  
Protein Diffusion ◽  
Ion Diffusion ◽  
Fluorescence Fluctuation Spectroscopy ◽  
Biophysical Characterization ◽  
Kv Channels ◽  
Subunit Stoichiometry ◽  
Spatio Temporal ◽  
Voltage Sensing Domain

AbstractVoltage-gated potassium (Kv) channels are a family of membrane proteins that facilitate K+ ion diffusion across the plasma membrane, regulating both resting and action potentials. Kv channels comprise four pore-forming α subunits, each with a voltage sensing domain, and they are regulated by interaction with β subunits such as those belonging to the KCNE family. Here we conducted a comprehensive biophysical characterization of stoichiometry and protein diffusion across the plasma membrane of the epithelial KCNQ1-KCNE2 complex, combining total internal reflection fluorescence (TIRF) microscopy and a series of complementary Fluorescence Fluctuation Spectroscopy (FFS) techniques. Using this approach, we found that KCNQ1-KCNE2 has a predominant 4:4 stoichiometry, while non-bound KCNE2 subunits are mostly present as dimers in the plasma membrane. At the same time, we identified unique spatio-temporal diffusion modalities and nano-environment organization for each channel subunit. These findings improve our understanding of KCNQ1-KCNE2 channel function and suggest strategies for elucidating the subunit stoichiometry and forces directing localization and diffusion of ion channel complexes in general.

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