scholarly journals Frizzled-5: a high affinity receptor for secreted frizzled-related protein-2 activation of nuclear factor of activated T-cells c3 signaling to promote angiogenesis

Angiogenesis ◽  
2017 ◽  
Vol 20 (4) ◽  
pp. 615-628 ◽  
Author(s):  
Yuri K. Peterson ◽  
Patrick Nasarre ◽  
Ingrid V. Bonilla ◽  
Eleanor Hilliard ◽  
Jennifer Samples ◽  
...  

This chapter is divided into two sections, the first dealing with a novel immune activation gene, denoted Act -2. This gene encodes a secreted protein that may represent a new cytokine. The Act-2 protein shares significant homology with proteins in two related families of small secreted proteins. Act-2 is rapidly synthesized by activated T cells, B cells and monocytes. The second section deals with interleukin-2 receptors. These receptors are now known to be comprised of three distinct classes of receptors, formed by various combinations of two IL-2 binding proteins, the α and β chains. The low-affinity receptors contain α, but not β chains; the intermediate-affinity receptors contain β, but not α chains, and the high-affinity receptors contain both α and β chains. The β chain appears to be tyrosine phosphorylated. We discuss evidence for the existence of another protein of relative molecular mass 100 000, which appears to be a subunit of at least the high-affinity receptor.


1988 ◽  
Vol 167 (3) ◽  
pp. 1265-1270 ◽  
Author(s):  
M Sharon ◽  
J P Siegel ◽  
G Tosato ◽  
J Yodoi ◽  
T L Gerrard ◽  
...  

IL-2 binds to high- and low-affinity receptors on activated T cells. The high-affinity receptor was hypothesized to consist of the noncovalent association between the alpha chain (IL-2-R-alpha, p55) and a beta chain (IL-2-R-beta, p70), whereas the low-affinity receptor consists of p55 without p70. We now directly identify p70 as a 65-77-kD glycoprotein doublet. Preparative quantities of the IL-2/p70 complex have been isolated. Further, we demonstrate that p70 is the principal IL-2 binding protein on both resting CD4+ and CD8+ T cells and that both p70 and p55 can be induced on normal B cells and monocytes.


Cells ◽  
2021 ◽  
Vol 10 (1) ◽  
pp. 145
Author(s):  
Leonardo Cristinziano ◽  
Remo Poto ◽  
Gjada Criscuolo ◽  
Anne Lise Ferrara ◽  
Maria Rosaria Galdiero ◽  
...  

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.


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