Two Distinct States of Crosslinked IgE Receptors That May Trigger and Terminate Secretion from RBL-2H3 Mast Cells

2018 ◽  
pp. 61-82
Author(s):  
J. M. Oliver ◽  
J. C. Seagrave ◽  
R. F. Stump
Keyword(s):  
Mast Cells ◽  
Ige Receptors

IgE Receptors from Rat Intestinal Mucosal and Peritoneal Mast Cells Show Mast Cell Subtype-Specific Differences

1989 ◽  
Vol 88 (1-2) ◽  
pp. 200-202
Author(s):  
M. Swieter ◽  
B.M.C. Chan ◽  
T.D.G. Lee ◽  
C.J. Rimmer ◽  
A. Froese ◽  
...  
Keyword(s):  
Mast Cell ◽  
Mast Cells ◽  
Cell Subtype ◽  
Ige Receptors ◽  
Peritoneal Mast Cells

83. Histamine release from rat mast cells by antibodies against IgE-receptors

1978 ◽  
Vol 61 (3) ◽  
pp. 153 ◽  
Author(s):  
T ISHIZAKA ◽  
K ISHIZAKA ◽  
D CONRAD ◽  
A FROESE
Keyword(s):  
Mast Cells ◽  
Histamine Release ◽  
Ige Receptors ◽  
Rat Mast Cells

Isolation and characterization of ige receptors from rat intestinal mucosal mast cells

1989 ◽  
Vol 19 (10) ◽  
pp. 1879-1885 ◽  
Author(s):  
Mark Swieter ◽  
Bosco M. C. Chan ◽  
Carol Rimmer ◽  
Karol Mcneill ◽  
Arnold Froese ◽  
...  
Keyword(s):  
Mast Cells ◽  
Isolation And Characterization ◽  
Mucosal Mast Cells ◽  
Ige Receptors

182 Biochemical analysis of early membrane events induced by bridging of IgE receptors on human mast cells

1983 ◽  
Vol 71 (1) ◽  
pp. 134 ◽  
Author(s):  
T ISHIZAKA ◽  
D CONRAD ◽  
E SCHULMAN ◽  
A STERK ◽  
K ISHIZAKA
Keyword(s):  
Mast Cells ◽  
Biochemical Analysis ◽  
Human Mast Cells ◽  
Ige Receptors

scholarly journals Lipid-based and protein-based interactions synergize transmembrane signaling stimulated by antigen clustering of IgE receptors

2021 ◽  
Vol 118 (35) ◽  
pp. e2026583118
Author(s):  
Nirmalya Bag ◽  
Alice Wagenknecht-Wiesner ◽  
Allan Lee ◽  
Sophia M. Shi ◽  
David A. Holowka ◽  
...  
Keyword(s):  
Mast Cells ◽  
Immunoglobulin E ◽  
Tyrosine Phosphatase ◽  
Correlation Spectroscopy ◽  
Current Evidence ◽  
Structural Variants ◽  
Fluorescence Correlation ◽  
Ige Receptors ◽  
Liquid Ordered ◽  
Lyn Tyrosine Kinase

Antigen (Ag) crosslinking of immunoglobulin E–receptor (IgE-FcεRI) complexes in mast cells stimulates transmembrane (TM) signaling, requiring phosphorylation of the clustered FcεRI by lipid-anchored Lyn tyrosine kinase. Previous studies showed that this stimulated coupling between Lyn and FcεRI occurs in liquid ordered (Lo)-like nanodomains of the plasma membrane and that Lyn binds directly to cytosolic segments of FcεRI that it initially phosphorylates for amplified activity. Net phosphorylation above a nonfunctional threshold is achieved in the stimulated state but not in the resting state, and current evidence supports the hypothesis that this relies on Ag crosslinking to disrupt a balance between Lyn and tyrosine phosphatase activities. However, the structural interactions that underlie the stimulation process remain poorly defined. This study evaluates the relative contributions and functional importance of different types of interactions leading to suprathreshold phosphorylation of Ag-crosslinked IgE-FcεRI in live rat basophilic leukemia mast cells. Our high-precision diffusion measurements by imaging fluorescence correlation spectroscopy on multiple structural variants of Lyn and other lipid-anchored probes confirm subtle, stimulated stabilization of the Lo-like nanodomains in the membrane inner leaflet and concomitant sharpening of segregation from liquid disordered (Ld)-like regions. With other structural variants, we determine that lipid-based interactions are essential for access by Lyn, leading to phosphorylation of and protein-based binding to clustered FcεRI. By contrast, TM tyrosine phosphatase, PTPα, is excluded from these regions due to its Ld-preference and steric exclusion of TM segments. Overall, we establish a synergy of lipid-based, protein-based, and steric interactions underlying functional TM signaling in mast cells.

scholarly journals Activation of Human Peripheral Basophils in Response to High IgE Antibody Concentrations without Antigens

2018 ◽  
Vol 20 (1) ◽  
pp. 45 ◽  
Author(s):  
Yuhki Yanase ◽  
Yoshimi Matsuo ◽  
Tomoko Kawaguchi ◽  
Kaori Ishii ◽  
Akio Tanaka ◽  
...  
Keyword(s):  
Atopic Dermatitis ◽  
Mast Cells ◽  
Pollen Allergy ◽  
Allergic Diseases ◽  
Ige Antibodies ◽  
Ige Antibody ◽  
High Affinity ◽  
Ige Receptors ◽  
Healthy Donors

Basophils and mast cells have high affinity IgE receptors (FcεRI) on their plasma membrane and play important roles in FcεRI-associated allergic diseases, such as pollen allergy, food allergy, chronic spontaneous urticarial (CSU), and atopic dermatitis (AD). To date, several reports have revealed that high IgE antibody concentrations activate mast cells—which reside in tissue—in the absence of any antigens (allergens). However, IgE antibody-induced activation of basophils—which circulate in blood—has not been reported. Here, we investigated whether IgE antibodies may regulate functions of human peripheral basophils without antigens in vitro. We successfully removed IgE antibodies bound to FcεRI on the surface of human peripheral basophils by treating with 0.1% lactic acid. We also demonstrated that high IgE antibody concentrations (>1 μM) induced histamine release, polarization, and CD203c upregulation of IgE antibody-stripped basophils. Thus, high IgE antibody concentrations directly activate basophils, which express IgE-free FcεRI on the cell surface. This mechanism may contribute to the pathogenesis of patients with AD and CSU who have higher serum IgE concentrations compared to healthy donors.

scholarly journals Localized mast cell degranulation induced by concanavalin A-sepharose beads. Implications for the Ca2+ hypothesis of stimulus-secretion coupling.

1978 ◽  
Vol 79 (2) ◽  
pp. 394-400 ◽  
Author(s):  
D Lawson ◽  
C Fewtrell ◽  
M C Raff
Keyword(s):  
Mast Cell ◽  
Mast Cells ◽  
Concanavalin A ◽  
Mast Cell Degranulation ◽  
Con A ◽  
Ige Receptors ◽  
Stimulus Secretion Coupling ◽  
Covalently Linked ◽  
Sepharose 4B ◽  
Ca2 Channels

Concanavalin A (Con A) covalently linked to Sepharose 4B beads induced localized degranulation of sensitized rat peritoneal mast cells in regions of contact between beads and cells. This degranulation was Ca2+ dependent and was not seen when sensitized mast cells bound to beads conjugated with a nonstimulating lectin, wheat germ agglutinin, or when unsensitized mast cells bound to Con A-Sepharose. The finding that sensitized mast cells which had adhered to Con A-Sepharose beads degranulated in regions of the cell away from the area of bead contact if exposed to soluble Con A excluded the possibility that the localized release was due to a redistribution of the IgE receptors or putative Ca2+ channels to the region of bead contact. The results suggest that, if an influx of Ca2+ is the mechanism for initiating mast cell degranulation, then the opening of Ca2+ channels in the plasma membrane of activated mast cells is a localized event and that Ca2+ acts locally within the cell to initiate exocytosis.

scholarly journals Mapping gold-labeled IgE receptors on mast cells by scanning electron microscopy: receptor distributions revealed by silver enhancement, backscattered electron imaging, and digital image analysis.

1988 ◽  
Vol 36 (5) ◽  
pp. 493-502 ◽  
Author(s):  
R F Stump ◽  
J R Pfeiffer ◽  
J Seagrave ◽  
J M Oliver
Keyword(s):  
Electron Microscopy ◽  
Image Analysis ◽  
Mast Cells ◽  
Digital Image ◽  
Protein A ◽  
Ige Receptor ◽  
Silver Enhancement ◽  
Receptor Complexes ◽  
Ige Receptors ◽  
Electron Imaging

Immunogold labeling and silver enhancement techniques are widely used to determine density and distribution of cell membrane receptors by light and transmission electron microscopy. However, these techniques have not been widely used for receptor detection by scanning electron microscopy. We used antigen- or protein A-conjugated colloidal gold particles, together with silver enhancement, sequential secondary and back-scattered electron imaging (SEI and BEI), and digital image processing, to explore cell surface distribution of IgE-receptor complexes on RBL-2H3 cells, a rat leukemia line that provides a model for the study of mucosal mast cells. Cells were first incubated with a monoclonal antidinitrophenol IgE (anti-DNP-IgE) that binds with high affinity to cell surface IgE receptors. The resulting IgE-receptor complexes were cross-linked either with the multivalent antigen, DNP-BSA-gold, or with a polyclonal anti-IgE antibody. Antibody-treated cells were labeled after fixation with protein A-gold. Fixed, gold-labeled cell monolayers were silver enhanced (or not), dehydrated, critical point-dried, and coated with gold-palladium (for SEI analysis) or carbon (for combined SEI/BEI analysis). They were observed in an Hitachi S800 SEM equipped with a field emission tip and a Robinson backscattered electron detector. An image processor (MegaVision 1024XM) digitized images directly from the S800 microscope at 500-1000 line resolution. Silver enhancement significantly improves detection of gold particles in both SEI and BEI modes of SEM. On gold-palladium-coated samples, 20-nm particles are resolved by SEI after enhancement. BEI resolves 15-nm particles without enhancement and 5- or 10-nm particles are resolved by BEI on silver-enhanced, carbon-coated samples. Neither BEI nor SEI alone can yield high resolution topographical maps of receptor distribution (BEI forms images on the basis of atomic number contrast which reveals gold but not surface features). Image analysis techniques were therefore introduced to digitize, enhance, and process BEI and SEI images of the same field of view. The resulting high-contrast, high-resolution images were superimposed, yielding well-resolved maps of the distribution of antigen-IgE-receptor complexes on the surface of RBL-2H3 mast cells. The maps are stored in digital form, as required for computer-based quantitative morphometric analyses. These techniques of silver enhancement, combined BEI/SEI imaging, and digital image analysis can be applied to analyze density and distribution of any gold-labeled ligand on its target cell.

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