High-Affinity Receptor for Interferon-Gamma (IFN-γ), a Ubiquitous Protein Occurring in Different Molecular Forms on Human Cells: Blood Monocytes and Eleven Different Cell Lines Have the Same IFN-γ Receptor Protein

1991 ◽  
Vol 49 (5) ◽  
pp. 462-473 ◽  
Author(s):  
Adolphus P.G.M. van Loon ◽  
Laurence Ozmen ◽  
Michael Fountoulakis ◽  
Malgosia Kania ◽  
Monika Haiker ◽  
...  
Keyword(s):  
Cell Lines ◽  
Interferon Gamma ◽  
Human Cells ◽  
Receptor Protein ◽  
Molecular Forms ◽  
Blood Monocytes ◽  
High Affinity ◽  
High Affinity Receptor ◽  
Affinity Receptor ◽  
Ifn Γ

scholarly journals Effects of Midgut-Protein-Preparative and Ligand Binding Procedures on the Toxin Binding Characteristics of BT-R1, a Common High-Affinity Receptor in Manduca sexta for Cry1A Bacillus thuringiensis Toxins

1998 ◽  
Vol 64 (6) ◽  
pp. 2158-2165 ◽  
Author(s):  
Timothy P. Keeton ◽  
Brian R. Francis ◽  
Walid S. A. Maaty ◽  
Lee A. Bulla
Keyword(s):  
Ligand Binding ◽  
Manduca Sexta ◽  
Protein S ◽  
Receptor Protein ◽  
Common Mechanism ◽  
Binding Characteristics ◽  
Toxin Binding ◽  
High Affinity ◽  
High Affinity Receptor ◽  
Affinity Receptor

ABSTRACT The identity of the physiologically important Cry1A receptor protein(s) in the lepidopteran Manduca sexta has been a matter of dispute due to the multiple proteins which bind the Cry1Ac toxin. Cry1Aa, Cry1Ab, and Cry1Ac exhibit essentially identical toxicities toward M. sexta larvae and show a high degree of sequence and presumed structural identities. These similarities make it likely that there is a common mechanism of toxicity in these lepidopteran-specific toxins in terms of both mode of action and the receptor proteins through which these toxins exert their lepidopteran-specific toxicity. Investigators in our laboratory previously demonstrated that the cloned 210-kDa glycoprotein BT-R1 binds all three Cry1A toxins (T. P. Keeton and L. A. Bulla, Jr., Appl. Environ. Microbiol. 63:3419–3425, 1997). This protein remains a common binding protein even after being subjected to various midgut membrane preparation and processing protocols. The method used to isolate proteins from the M. sexta larval midgut in no significant way affects the results of ligand binding and vacuum blotting experiments, and we have been unable to detect specific, high-affinity binding of any Cry1A toxin to Cry1Ac binding proteins other than BT-R1. Alterations in blot substrate and blocking, hybridization, and washing buffers support these conclusions. Collectively, these results indicate that inM. sexta the cadherin-like BT-R1 protein is a common high-affinity receptor protein for the Cry1A family of toxins.

Interferon gamma induces in human neutrophils and macrophages expression of the mRNA for the high affinity receptor for monomeric IgG (FcγR-I or CD64)

1990 ◽  
Vol 170 (2) ◽  
pp. 582-588 ◽  
Author(s):  
Marco A. Cassatella ◽  
Rebecca M. Flynn ◽  
Miguel Aste Amezaga ◽  
Flavia Bazzoni ◽  
Federica Vicentini ◽  
...  
Keyword(s):  
Interferon Gamma ◽  
Human Neutrophils ◽  
High Affinity ◽  
High Affinity Receptor ◽  
Affinity Receptor

scholarly journals IL-33 and Superantigenic Activation of Human Lung Mast Cells Induce the Release of Angiogenic and Lymphangiogenic Factors

Cells ◽  
2021 ◽  
Vol 10 (1) ◽  
pp. 145
Author(s):  
Leonardo Cristinziano ◽  
Remo Poto ◽  
Gjada Criscuolo ◽  
Anne Lise Ferrara ◽  
Maria Rosaria Galdiero ◽  
...  
Keyword(s):  
Mast Cells ◽  
Human Lung ◽  
Protein A ◽  
Protein L ◽  
Variable Regions ◽  
Prolonged Incubation ◽  
High Affinity ◽  
High Affinity Receptor ◽  
Affinity Receptor ◽  
Pleiotropic Functions

Human lung mast cells (HLMCs) express the high-affinity receptor FcεRI for IgE and are strategically located in different compartments of human lung, where they play a role in several inflammatory disorders and cancer. Immunoglobulin superantigens (e.g., protein A of Staphylococcus aureus and protein L of Peptostreptococcus magnus) bind to the variable regions of either the heavy (VH3) or light chain (κ) of IgE. IL-33 is a cytokine expressed by epithelial cells that exerts pleiotropic functions in the lung. The present study investigated whether immunoglobulin superantigens protein A and protein L and IL-33 caused the release of inflammatory (histamine), angiogenic (VEGF-A) and lymphangiogenic (VEGF-C) factors from HLMCs. The results show that protein A and protein L induced the rapid (30 min) release of preformed histamine from HLMCs. By contrast, IL-33 did not induce the release of histamine from lung mast cells. Prolonged incubation (12 h) of HLMCs with superantigens and IL-33 induced the release of VEGF-A and VEGF-C. Preincubation with IL-33 potentiated the superantigenic release of histamine, angiogenic and lymphangiogenic factors from HLMCs. Our results suggest that IL-33 might enhance the inflammatory, angiogenic and lymphangiogenic activities of lung mast cells in pulmonary disorders.

The Temporal Distribution of the 1α,25-Dihydroxycholecalciferol Receptor in the Rat Jejunal Villus

1984 ◽  
Vol 67 (3) ◽  
pp. 285-290 ◽  
Author(s):  
S. D. H. Chan ◽  
D. Atkins
Keyword(s):  
Vitamin D ◽  
Vitamin D Deficiency ◽  
Calcium Absorption ◽  
Sedimentation Coefficient ◽  
Temporal Distribution ◽  
High Affinity ◽  
High Affinity Receptor ◽  
Affinity Receptor ◽  
Cell Fractions ◽  
Crypt Cells

1. The distribution of the 1α,25-dihydroxycholecalciferol receptor was studied in enterocytes isolated from the upper, mid and lower villus and crypt cells of the jejunum of normal and rachitic rats. 2. In all cell fractions a high-affinity receptor (KD ⋍ 0.07 nmol/l) with a sedimentation coefficient of 3.5S was demonstrated. 3. In normal rats there was a 60% reduction in receptor numbers in crypt cells compared with the mid and upper villous cells. 4. Vitamin D deficiency led to a reduction in receptor numbers in all cell fractions (45% upper villus, 78% crypt cells). 5. The data are compatible with the concept of calcium absorption occurring in the differentiated villous cells and also account for the reduction in absorption in rachitic animals.

scholarly journals Neuropilin-2, a Novel Member of the Neuropilin Family, Is a High Affinity Receptor for the Semaphorins Sema E and Sema IV but Not Sema III

Neuron ◽  
1997 ◽  
Vol 19 (3) ◽  
pp. 547-559 ◽  
Author(s):  
Hang Chen ◽  
Alain Chédotal ◽  
Zhigang He ◽  
Corey S Goodman ◽  
Marc Tessier-Lavigne
Keyword(s):  
High Affinity ◽  
High Affinity Receptor ◽  
Affinity Receptor
Sign in / Sign up

Export Citation Format

Share Document