Two-Color Visualization of Cholesterol Fluctuation in Plasma Membranes by Spatial Distribution-Controllable Single Fluorescent Probes

2021 ◽  
Author(s):  
Xuechen Li ◽  
Guangle Niu ◽  
Minggang Tian ◽  
Qing Lu ◽  
Yuezhi Cui ◽  
...  
Keyword(s):  
Spatial Distribution ◽  
Fluorescent Probes ◽  
Plasma Membranes ◽  
Color Visualization

Membrane microdomains: lessons from microscopy

1995 ◽  
Vol 53 ◽  
pp. 776-777
Author(s):  
J.M. Robinson ◽  
J.M Oliver
Keyword(s):  
Spatial Distribution ◽  
Plasma Membrane ◽  
Epithelial Cells ◽  
Plasma Membranes ◽  
Cell Types ◽  
Imaging Modalities ◽  
Membrane Microdomains ◽  
Membrane Domains ◽  
Lateral Heterogeneity ◽  
Functional Importance

Specialized regions of plasma membranes displaying lateral heterogeneity are the focus of this Symposium. Specialized membrane domains are known for certain cell types such as differentiated epithelial cells where lateral heterogeneity in lipids and proteins exists between the apical and basolateral portions of the plasma membrane. Lateral heterogeneity and the presence of microdomains in membranes that are uniform in appearance have been more difficult to establish. Nonetheless a number of studies have provided evidence for membrane microdomains and indicated a functional importance for these structures.This symposium will focus on the use of various imaging modalities and related approaches to define membrane microdomains in a number of cell types. The importance of existing as well as emerging imaging technologies for use in the elucidation of membrane microdomains will be highlighted. The organization of membrane microdomains in terms of dimensions and spatial distribution is of considerable interest and will be addressed in this Symposium.

scholarly journals Pore Helix Domain Is Critical to Camphor Sensitivity of Transient Receptor Potential Vanilloid 1 Channel

2012 ◽  
Vol 116 (4) ◽  
pp. 903-917 ◽  
Author(s):  
Lenka Marsakova ◽  
Filip Touska ◽  
Jan Krusek ◽  
Viktorie Vlachova
Keyword(s):  
Spatial Distribution ◽  
Plasma Membranes ◽  
Transient Receptor Potential ◽  
Receptor Potential ◽  
Structural Basis ◽  
Transient Receptor Potential Vanilloid ◽  
Trpv1 Channel ◽  
Patch Clamp Technique ◽  
Trpv1 Channels ◽  
Transient Receptor

Background The recent discovery that camphor activates and strongly desensitizes the capsaicin-sensitive and noxious heat-sensitive channel transient receptor potential vanilloid subfamily member 1 (TRPV1) has provided new insights and opened up new research paths toward understanding why this naturally occurring monoterpene is widely used in human medicine for its local counter-irritant, antipruritic, and anesthetic properties. However, the molecular basis for camphor sensitivity remains mostly unknown. The authors attempt to explore the nature of the activation pathways evoked by camphor and narrow down a putative interaction site at TRPV1. Methods The authors transiently expressed wild-type or specifically mutated recombinant TRPV1 channels in human embryonic kidney cells HEK293T and recorded cation currents with the whole cell, patch clamp technique. To monitor changes in the spatial distribution of phosphatidylinositol 4,5-bisphosphate, they used fluorescence resonance energy transfer measurements from cells transfected with the fluorescent protein-tagged pleckstrin homology domains of phospholipase C. Results The results revealed that camphor modulates TRPV1 channel through the outer pore helix domain by affecting its overall gating equilibrium. In addition, camphor, which generally is known to decrease the fluidity of cell plasma membranes, may also regulate the activity of TRPV1 by inducing changes in the spatial distribution of phosphatidylinositol-4,5-bisphosphate on the inner leaflet of the plasma membrane. Conclusions The findings of this study provide novel insights into the structural basis for the modulation of TRPV1 channel by camphor and may provide an explanation for the mechanism by which camphor modulates thermal sensation in vivo.

scholarly journals Interaction of fluorescent probes with plasma membranes from rat liver and morris hepatoma 3924A

FEBS Letters ◽  
1975 ◽  
Vol 49 (3) ◽  
pp. 346-349 ◽  
Author(s):  
Ornella Dionisi ◽  
Tommaso Galeotti ◽  
Tullio Terranova ◽  
Paola Arslan ◽  
Angelo Azzi
Keyword(s):  
Rat Liver ◽  
Fluorescent Probes ◽  
Plasma Membranes ◽  
Morris Hepatoma

scholarly journals The mammalian plasma membrane is defined by transmembrane asymmetries in lipid unsaturation, leaflet packing, and protein shape

2019 ◽  
Author(s):  
JH Lorent ◽  
KR Levental ◽  
L Ganesan ◽  
G Rivera-Longsworth ◽  
E. Sezgin ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Fluorescent Probes ◽  
Plasma Membranes ◽  
Atomistic Simulations ◽  
Biophysical Properties ◽  
Fundamental Feature ◽  
Structural Asymmetry ◽  
Asymmetric Structures ◽  
Lipid Unsaturation ◽  
Protein Shape

SUMMARYA fundamental feature of cellular plasma membranes (PM) is asymmetric lipid distribution between the bilayer leaflets. However, neither the detailed, comprehensive compositions of individual PM leaflets, nor how these contribute to structural membrane asymmetries have been defined. We report the distinct lipidomes and biophysical properties of both monolayers in living mammalian PMs. Phospholipid unsaturation is dramatically asymmetric, with the cytoplasmic leaflet being ∼2-fold more unsaturated than the exoplasmic. Atomistic simulations and spectroscopy of leaflet-selective fluorescent probes reveal that the outer PM leaflet is more packed and less diffusive than the inner leaflet, with this biophysical asymmetry maintained in the endocytic system. The structural asymmetry of the PM is reflected in asymmetric structures of protein transmembrane domains (TMD). These structural asymmetries are conserved throughout Eukaryota, suggesting fundamental cellular design principles.

ZO-1 maintains its spatial distribution but dissociates from junctional fibrils during tight junction regulation

1993 ◽  
Vol 264 (5) ◽  
pp. C1096-C1101 ◽  
Author(s):  
J. L. Madara ◽  
S. Carlson ◽  
J. M. Anderson
Keyword(s):  
Spatial Distribution ◽  
Tight Junction ◽  
Tight Junctions ◽  
Plasma Membranes ◽  
Freeze Fracture ◽  
Cell Junctions ◽  
Absorptive Cell ◽  
Physiological Regulation ◽  
Functional Relationships ◽  
Tight Junction Regulation

Tight junctions restrict diffusion of hydrophilic solutes through the paracellular pathways of columnar epithelia. It is now apparent that the barrier function of tight junctions is physiologically regulated. Current models of the tight junction envisage junctional subunits consisting of extracellular "kisses" between plasma membranes of adjacent cells, intramembrane components represented by freeze-fracture fibrils, and cytoplasmic elements of the cytoskeleton. Insights into functional relationships between these various components of tight junctions should be provided by mapping component interrelationships in states of altered junctional permeability. Here we define the spatial distribution of ZO-1 during a state of physiological regulation of intestinal absorptive cell tight junctions. Enhanced permeation of absorptive cell junctions in response to activation of apical membrane Na(+)-solute cotransporters does not lead to redistribution of the ZO-1 pool, as judged from quantitative ultrastructural immunolocalization studies employing two different ZO-1 antibodies. Surprisingly, ZO-1, which normally localizes under junctional kisses/fibrils, focally persists at sites where junctional kisses/fibrils are cleared. These findings suggest that 1) spatial redistribution of ZO-1 does not contribute to physiological regulation of junctions elicited by activation of Na(+)-solute cotransport and 2) ZO-1 and junctional fibrils may spatially dissociate during such regulated states.

scholarly journals Membrane Domain Specificity in the Spatial Distribution of Aquaporins 5, 7, 9, and 11 in Efferent Ducts and Epididymis of Rats

2008 ◽  
Vol 56 (12) ◽  
pp. 1121-1135 ◽  
Author(s):  
Louis Hermo ◽  
Morgan Schellenberg ◽  
Lauren Ye Liu ◽  
Bama Dayanandan ◽  
Tong Zhang ◽  
...  
Keyword(s):  
Spatial Distribution ◽  
Plasma Membranes ◽  
Water Channel ◽  
Wide Field ◽  
Membrane Domains ◽  
Efferent Ducts ◽  
Specific Manner ◽  
Basal Plasma ◽  
A Cell ◽  
Specific Membrane

Water content within the epididymis of the male reproductive system is stringently regulated to promote sperm maturation. Several members of the aquaporin (AQP) family of water channel-forming integral membrane proteins have been identified in epididymal cells, but expression profiling for this epithelium is presently incomplete, and no AQP isoform has yet been identified on basolateral plasma membranes of these cells. In this study, we explored AQP expression by RT-PCR and light microscopy immunolocalizations using peroxidase and wide-field fluorescence techniques. The results indicate that several AQPs are coexpressed in the epididymis including AQP 5, 7, 9, and 11. Immunolocalizations suggested complex patterns in the spatial distribution of these AQPs. In principal cells, AQP 9 and 11 were present mainly on microvilli, whereas AQP 7 was localized primarily to lateral and then to basal plasma membranes in a region-specific manner. AQP 5 was also expressed regionally but was associated with membranes of endosomes. Additionally, AQPs were expressed by some but not all basal (AQP 7 and 11), clear (AQP 7 and 9), and halo (AQP 7 and 11) cells. These findings indicate unique associations of AQPs with specific membrane domains in a cell type- and region-specific manner within the epididymis of adult animals.

Targetable, two-photon fluorescent probes for local nitric oxide capture in the plasma membranes of live cells and brain tissues

The Analyst ◽  
2018 ◽  
Vol 143 (17) ◽  
pp. 4180-4188 ◽  
Author(s):  
Xinfu Zhang ◽  
Benlei Wang ◽  
Yi Xiao ◽  
Chao Wang ◽  
Ling He
Keyword(s):  
Nitric Oxide ◽  
Plasma Membrane ◽  
Fluorescent Probe ◽  
Fluorescent Probes ◽  
Plasma Membranes ◽  
Live Cells ◽  
Two Photon ◽  
In Cells ◽  
Brain Tissues

A plasma membrane-targetable two-photon fluorescent probe for capturing nitric oxide in cells and brain tissues.

scholarly journals Two-color fluorescent probes for imaging the dipole potential of cell plasma membranes

2005 ◽  
Vol 1712 (2) ◽  
pp. 128-136 ◽  
Author(s):  
Vasyl V. Shynkar ◽  
Andrey S. Klymchenko ◽  
Guy Duportail ◽  
Alexander P. Demchenko ◽  
Yves Mély
Keyword(s):  
Fluorescent Probes ◽  
Plasma Membranes ◽  
Dipole Potential ◽  
Cell Plasma

scholarly journals Amphipathic Fluorescent Dyes for Sensitive and Long-Term Monitoring of Plasma Membranes

2020 ◽  
Author(s):  
Masataka Takahashi ◽  
Ryo Seino ◽  
Takatoshi Ezoe ◽  
Munetaka Ishiyama ◽  
Yuichiro Ueno
Keyword(s):  
Fluorescent Probes ◽  
Plasma Membranes ◽  
Fluorescent Dyes ◽  
Imaging Techniques ◽  
Critical Role ◽  
Strong Acid ◽  
Endocytic Pathway ◽  
Polycyclic Aromatic ◽  
Low Cytotoxicity ◽  
High Cytotoxicity

ABSTRACTThe plasma membrane (PM) plays a critical role in many cellular processes, and PM dysfunction is a key biomarker related to the cell status and several diseases. Imaging techniques using small fluorescent probes have become increasingly important tools for visualizing living cells, particularly their PMs. Among the commercially available PM-specific probes, PKH dyes are widely used; however, the utility of these dyes is limited by their short membrane retention times and high cytotoxicity. Herein, PlasMem Bright Green and Red are implemented as new PM-specific fluorescent probes, which employ a polycyclic aromatic fluorophore to improve their retention ability and a strong acid moiety to reduce their transmembrane diffusion and cytotoxicity. We demonstrate that the long retention and low cytotoxicity of the PlasMem Bright dyes enable them to be applied for observing neuronal PMs and monitoring PM dynamics involving the endocytic pathway. Furthermore, we successfully detected mitochondria in nerve axons over long periods using PlasMem Bright dyes. Finally, the combined use of exosome staining probes and PlasMem Bright dyes allowed clear visualization of the endocytic pathway.TOC graphic

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