Lucifer Yellow and Fluorescein Isothiocyanate uptake by Cells of Morinda Citrifolia in Suspension Cultures is not Confined to the Endocytotic Pathway

1991 ◽  
Vol 100 (1) ◽  
pp. 237-241
Author(s):  
D. O'DRISCOLL ◽  
G. WILSON ◽  
M. W. STEER
Keyword(s):  
Lucifer Yellow ◽  
Fluorescein Isothiocyanate ◽  
Anion Transport ◽  
Suspension Cultures ◽  
Morinda Citrifolia ◽  
Central Vacuole ◽  
Cell Plasma Membrane ◽  
Transport Inhibitor ◽  
Lucifer Yellow Ch ◽  
Cell Plasma

On the basis of previous reports that the uptake of Lucifer Yellow-CH (LYCH) is restricted to the endocytotic pathway in plant cells, it was anticipated that the probe would provide an estimate of endocytotic activity in suspension cultures of Morinda citrifolia. The uptake of LYCH and fluorescein isothiocyanate (FITC) have been examined in whole cell and protoplast forms of M. citrifolia. Rapid staining of the general cytoplasm and nucleus was observed with both fluorochrome treatments, while both markers were excluded from the central vacuole. In addition, treatment of cells with Probenecid, an anion transport inhibitor, prevented LYCH from entering cells. It is suggested that LYCH utilizes an anion transport mechanism to cross the plant cell plasma membrane. Furthermore, LYCH and FITC are excluded from the central vacuole due to the absence of such a mechanism on the tonoplast.

The drug probenecid inhibits the vacuolar accumulation of fluorescent anions in onion epidermal cells

1991 ◽  
Vol 99 (3) ◽  
pp. 557-563
Author(s):  
K. J. OPARKA ◽  
E. A. MURANT ◽  
K. M. WEIGHT ◽  
D. A. M. PRIOR ◽  
N. HARRIS
Keyword(s):  
Structural Changes ◽  
Lucifer Yellow ◽  
Plant Cells ◽  
Epidermal Cells ◽  
Drug Uptake ◽  
Central Vacuole ◽  
Endosomal Membrane ◽  
Lucifer Yellow Ch ◽  
Net Uptake ◽  
Onion Epidermal Cells

The drug probenecid has been shown to inhibit the vacuolar accumulation of a range of fluorescent anions with differing pKa values (Lucifer Yellow CH, Cascade Blue hydrazide, sulphorhodamine G, carboxyfluorescein, FITC) in onion epidermal cells. In the absence of the drug, uptake occurred into the vacuole and was sensitive to extracellular pH. In the presence of the drug, the dyes accumulated exclusively in the cytoplasm and nucleus. Probenecid also induced vesiculation of the tonoplast and caused the cytoplasm to become polar, both of these structural changes being reversible by removal of the drug. In the case of the permeant FITC molecule, probenecid inhibited net uptake into the epidermal cells, and addition of the drug to cells that had already accumulated dye in the central vacuole resulted in rapid dye leakage across the tonoplast. However, the other more impermeant probes failed to leak to the cytoplasm once they had accumulated in the vacuole, even after prolonged exposures to probenecid. The data are discussed in the light of recent evidence for probenecid-sensitive carriers capable of transporting fluorescent anions across the endosomal membrane of macrophages and in relation to the concept of a detoxification system for the sequestration of xenobiotic anions by plant cells

Multimodal Atomic Force Imaging of Open Hemichannelinduced Modulation of Cell Volume and Viscoelastic Properties

1999 ◽  
Vol 5 (S2) ◽  
pp. 998-999
Author(s):  
Seung K. Rhee ◽  
Arjan P. Quist ◽  
Hai Lin ◽  
Nils Almqvist ◽  
Ratneshx Lai
Keyword(s):  
Plasma Membrane ◽  
Cell Volume ◽  
Lucifer Yellow ◽  
Single Cells ◽  
Dye Uptake ◽  
Aortic Endothelial Cells ◽  
Atomic Force ◽  
Cell Plasma ◽  
Uptake Assay ◽  
Gap Junctional

Hemichannels from two single cells can join upon contact between these cells to form gap junctions - an intercellular pathway for the direct exchange of ions and small metabolites. Using techniques of fluorescent dye-uptake assay, laser confocal fluorescence imaging and atomic force microscopy (AFM), we have examined the role of hemichannels, present in the non-junctional regions of single cell plasma membrane, in the modulation of cell volume.Antibodies against a gap junctional protein connexin43, were immunolocalized to nonjunctional plasma membrane regions of single BICR-MlRk k (breast tumor epithelial) cells, KOM-1 (bovine aortic endothelial) cells, and GM04260 (AD-free human) fibroblast cells. In the absence of extracellular calcium, cytoplasmic uptake of Lucifer yellow (LY) but not of dextran-conjugated LY was observed in single cells. Dye uptake was prevented by gap junctional inhibitors, ẞ-glycyrrhetinic acid (ẞGCA) and oleamide.

Stimulation of Tumor-Specific Immunity Using Tumor Cell Plasma Membrane Antigen

Methods ◽  
1997 ◽  
Vol 12 (2) ◽  
pp. 155-164 ◽  
Author(s):  
Matthew F Mescher ◽  
Elena Savelieva
Keyword(s):  
Plasma Membrane ◽  
Tumor Cell ◽  
Cell Plasma Membrane ◽  
Specific Immunity ◽  
Cell Plasma ◽  
Stimulation Of

PROTEIN KINASE ACTIVITY ASSOCIATED WITH THE FAT CELL PLASMA MEMBRANE

1981 ◽  
Vol 9 (2) ◽  
pp. 232P-232P
Author(s):  
G. J. Belsham ◽  
R. W. Brownsey ◽  
R. M. Denton
Keyword(s):  
Plasma Membrane ◽  
Protein Kinase ◽  
Kinase Activity ◽  
Protein Kinase Activity ◽  
Fat Cell ◽  
Cell Plasma Membrane ◽  
Cell Plasma

scholarly journals Immunocytochemical identification of dye-injected cells.

1982 ◽  
Vol 30 (2) ◽  
pp. 189-191 ◽  
Author(s):  
R L Michaels
Keyword(s):  
Pancreatic Islet ◽  
Islet Cells ◽  
Lucifer Yellow ◽  
Immunofluorescent Staining ◽  
Pancreatic Islet Cells ◽  
Lucifer Yellow Ch ◽  
Before And After ◽  
Coupled Cells ◽  
Indirect Immunofluorescent

Lucifer Yellow CH may be injected into pancreatic islet cells and visualized in Epon sections of the embedded tissue both before and after plastic removal and immunocyto-chemical staining. The dye retains its fluorescence, clearly marking the injected cell and adjacent dye-coupled cells, but does not interfere with the indirect immunofluorescent staining patterns that are characteristic of the islet cells

Gastrointestinal Cell Plasma Membrane Wounding and Resealing In Vivo

1989 ◽  
Vol 96 (5) ◽  
pp. 1238-1248 ◽  
Author(s):  
Paul L. McNeil ◽  
Susumu Ito
Keyword(s):  
Plasma Membrane ◽  
Cell Plasma Membrane ◽  
Cell Plasma

scholarly journals A murine model of Charcot-Marie-Tooth disease 4F reveals a role for the C-terminus of periaxin in the formation and stabilization of Cajal bands

2018 ◽  
Vol 3 ◽  
pp. 20 ◽  
Author(s):  
Diane L. Sherman ◽  
Peter J. Brophy
Keyword(s):  
Plasma Membrane ◽  
Schwann Cell ◽  
Laminin Receptor ◽  
Cell Plasma Membrane ◽  
Charcot Marie Tooth ◽  
Charcot Marie Tooth Disease ◽  
C Terminus ◽  
Cell Plasma ◽  
Inherited Neuropathies ◽  
Tooth Disease

Charcot-Marie-Tooth (CMT) disease comprises up to 80 monogenic inherited neuropathies of the peripheral nervous system (PNS) that collectively result in demyelination and axon degeneration. The majority of CMT disease is primarily either dysmyelinating or demyelinating in which mutations affect the ability of Schwann cells to either assemble or stabilize peripheral nerve myelin. CMT4F is a recessive demyelinating form of the disease caused by mutations in the Periaxin (PRX) gene. Periaxin (Prx) interacts with Dystrophin Related Protein 2 (Drp2) in an adhesion complex with the laminin receptor Dystroglycan (Dag). In mice the Prx/Drp2/Dag complex assembles adhesive domains at the interface between the abaxonal surface of the myelin sheath and the cytoplasmic surface of the Schwann cell plasma membrane. Assembly of these appositions causes the formation of cytoplasmic channels called Cajal bands beneath the surface of the Schwann cell plasma membrane. Loss of either Periaxin or Drp2 disrupts the appositions and causes CMT in both mouse and man. In a mouse model of CMT4F, complete loss of Periaxin first prevents normal Schwann cell elongation resulting in abnormally short internodal distances which can reduce nerve conduction velocity, and subsequently precipitates demyelination. Distinct functional domains responsible for Periaxin homodimerization and interaction with Drp2 to form the Prx/Drp2/Dag complex have been identified at the N-terminus of Periaxin. However, CMT4F can also be caused by a mutation that results in the truncation of Periaxin at the extreme C-terminus with the loss of 391 amino acids. By modelling this in mice, we show that loss of the C-terminus of Periaxin results in a surprising reduction in Drp2. This would be predicted to cause the observed instability of both appositions and myelin, and contribute significantly to the clinical phenotype in CMT4F.

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