Analysis of Biological Functions of a 60-kD IgE-Binding Component Derived from Sera of Patients with Atopic Dermatitis

1992 ◽  
Vol 99 (2-4) ◽  
pp. 377-379 ◽  
Author(s):  
J. Bujanowski-Weber ◽  
A. Fischer ◽  
W. König
Keyword(s):  
Atopic Dermatitis ◽  
Biological Functions ◽  
Ige Binding ◽  
Binding Component

Detection of IgE binding component to infliximab in a patient with infliximab-induced anaphylaxis

2014 ◽  
Vol 112 (4) ◽  
pp. 393-394 ◽  
Author(s):  
Sun Hyuk Hwang ◽  
Hye-Soo Yoo ◽  
Moon Kyung Yoon ◽  
Hae-Sim Park
Keyword(s):  
Ige Binding ◽  
Binding Component

scholarly journals The Role of Galectin-9 as Mediator of Atopic Dermatitis: Effect on Keratinocytes

Cells ◽  
2021 ◽  
Vol 10 (4) ◽  
pp. 947
Author(s):  
Mab P. Corrêa ◽  
Libnah L. Areias ◽  
Rebeca D. Correia-Silva ◽  
Solange C. G. P. D’Ávila ◽  
Andréia M. Leopoldino ◽  
...  
Keyword(s):  
Atopic Dermatitis ◽  
Human Keratinocytes ◽  
Allergic Diseases ◽  
Control Group ◽  
Biological Functions ◽  
Experimental Conditions ◽  
Control Growth ◽  
Tnf Α ◽  
Ifn Γ

Galectin-9 (Gal-9) is a beta-galactoside-binding protein with a variety of biological functions related to immune response. However, in allergic diseases, its mechanism of action is not fully understood. This study evaluates the expression pattern of Gal-9 in patients with atopic dermatitis (AD), in ovalbumin (OVA)-induced experimental atopic dermatitis (AD) in mice, as well as its effect on human keratinocytes. The skin of OVA-immunized BALB/c mice was challenged with drops containing OVA on days 11, 14–18, and 21–24. HaCaT cells were cultured in the following experimental conditions: control (growth medium only) or stimulated with TNF-α/IFN-γ, or IL-4, or IL-17 with or without Gal-9 treatment. AD was characterized by increased levels of Gal-9 in mouse and human skin, especially in the epidermis, and with a marked influx of Gal-9 positive eosinophils and mast cells compared to the control group. Gal-9 showed an immunomodulatory effect on keratinocytes by decreasing the release of IL-6 by IL-4-stimulated keratinocytes or increasing the IL-6 and RANTES levels by IL-17- or TNF-α/IFN-γ-stimulated cells, respectively. Under IL-17, Gal-9 treatment also altered the proliferation rate of cells. Overall, increased levels of Gal-9 in AD skin contribute to the control of inflammatory response and the proliferative process of keratinocytes, suggesting this lectin as a relevant therapeutic target.

Relationship of cholecystokinin receptor binding to regulation of biological functions in pancreatic acini

1982 ◽  
Vol 242 (3) ◽  
pp. G250-G257 ◽  
Author(s):  
H. Sankaran ◽  
I. D. Goldfine ◽  
A. Bailey ◽  
V. Licko ◽  
J. A. Williams
Keyword(s):  
Binding Sites ◽  
Acid Uptake ◽  
Biological Functions ◽  
Amylase Release ◽  
Pancreatic Acini ◽  
Lower Affinity ◽  
Cck Receptors ◽  
Aminoisobutyric Acid ◽  
Stimulation Of ◽  
Binding Component

Cholecystokinin (CCK) was conjugated to 125I-Bolton-Hunter reagent (125I-BH-CCK), and the binding of this ligand to CCK receptors in isolated mouse pancreatic acini was correlated with the regulation by CCK of both amylase release and the transport of 2-deoxyglucose and alpha-aminoisobutyric acid. Stimulation of amylase release by CCK was biphasic. At low CCK concentrations (less than 200 pM), amylase release was progressively stimulated, whereas at higher CCK concentrations (greater than 200 pM), amylase release was progressively reduced. In contrast, stimulation of 2-[3H]deoxyglucose transport and inhibition of alpha-[3H]aminoisobutyric acid transport were monophasic, being one-half maximal at 0.85 and 0.44 nM, respectively. Under incubation conditions identical to those employed for measuring biological functions, the binding of 125I-BH-CCK to receptors in acini was rapid and reversible. Competition-inhibition curves and Scatchard plots of equilibrium binding were compatible with two orders of binding sites. Employing a computer program for analysis of multiple binding sites, a high-affinity, low-capacity binding component having a Kd of 26 pM and a lower-affinity, higher-capacity binding component having a component Kd of 2.2 nM were resolved. Regulation of 2-[3H]deoxyglucose and alpha-[3H]aminoisobutyric acid uptake appeared, therefore, to be the result of fractional occupancy of the lower-affinity CCK receptors. Regulation of amylase released was more complex and appeared to be due to the concomitant occupancy of both the high- and low-affinity CCK receptors.

Dioscorea batatas (Sanyak) Allergy, Identification of an IgE-binding Component

2007 ◽  
Vol 119 (1) ◽  
pp. S195
Author(s):  
G. Hur ◽  
S. Shin ◽  
H. Park ◽  
H. Kim ◽  
Y. Ye ◽  
...  
Keyword(s):  
Ige Binding ◽  
Dioscorea Batatas ◽  
Binding Component

scholarly journals The High-Affinity Receptor for IgE Is the Predominant IgE-Binding Structure in Lesional Skin of Atopic Dermatitis Patient

1997 ◽  
Vol 108 (3) ◽  
pp. 336-342 ◽  
Author(s):  
Radek Klubal ◽  
Birgit Osterhoff ◽  
Binghe Wang ◽  
Jean-Pierre Kinet ◽  
Dieter Maurer ◽  
...  
Keyword(s):  
Atopic Dermatitis ◽  
Atopic Dermatitis Patient ◽  
Lesional Skin ◽  
High Affinity ◽  
Ige Binding ◽  
High Affinity Receptor ◽  
Affinity Receptor ◽  
Binding Structure

Detection of at least one high-molecular-mass, IgE-binding component of the dust mite Lepidoglyphus destructor

Allergy ◽  
1994 ◽  
Vol 49 (8) ◽  
pp. 620-625 ◽  
Author(s):  
S. Olsson ◽  
B. Härfast ◽  
S. G. O. Johansson ◽  
M. Hage-Hamsten
Keyword(s):  
Molecular Mass ◽  
High Molecular Mass ◽  
Ige Binding ◽  
Dust Mite ◽  
Binding Component
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