Biotherapeutics for human eosinophil associated disorders

2015 ◽  
Vol 5 ◽  
pp. 1
Author(s):  
Anubha Singh ◽  
Deepak Kumar Singh ◽  
Usha Bhoria
Keyword(s):  
Human Eosinophil

Sequential degranulation of eosinophils induced by antigen or autocoids in allergic humans

1986 ◽  
Vol 44 ◽  
pp. 354-355
Author(s):  
Kate W. Sjoerdsma ◽  
W. James Metzger
Keyword(s):  
Allergic Rhinitis ◽  
Bronchoalveolar Lavage ◽  
Allergic Asthma ◽  
Skin Test ◽  
Positive Skin Test ◽  
Positive Skin ◽  
Human Eosinophil ◽  
Asthmatic Patients ◽  
Allergic Asthmatic ◽  
History Of

Eosinophils are important to the pathogenesis of allergic asthma, and are increased in bronchoalveolar lavage within four hours after bronchoprovocation of allergic asthmatic patients, and remain significantly increased up to 24 hours later. While the components of human eosinophil granules have been recently isolated and purified, the mechanisms of degranulation have yet to be elucidated.We obtained blood from two volunteers who had a history of allergic rhinitis and asthma and a positive skin test (5x5mm wheal) to Alternaria and Ragweed. Eosinophils were obtained using a modification of the method described by Roberts and Gallin.

scholarly journals Biochemical and amino acid sequence analysis of human eosinophil granule major basic protein.

1988 ◽  
Vol 263 (25) ◽  
pp. 12559-12563
Author(s):  
T L Wasmoen ◽  
M P Bell ◽  
D A Loegering ◽  
G J Gleich ◽  
F G Prendergast ◽  
...  
Keyword(s):  
Amino Acid ◽  
Sequence Analysis ◽  
Amino Acid Sequence ◽  
Basic Protein ◽  
Major Basic Protein ◽  
Amino Acid Sequence Analysis ◽  
Human Eosinophil ◽  
Eosinophil Granule

scholarly journals A Novel and Highly Divergent Homolog of Human Eosinophil Granule Major Basic Protein

1999 ◽  
Vol 274 (20) ◽  
pp. 14464-14473 ◽  
Author(s):  
Douglas A. Plager ◽  
David A. Loegering ◽  
Deborah A. Weiler ◽  
James L. Checkel ◽  
Jill M. Wagner ◽  
...  
Keyword(s):  
Basic Protein ◽  
Major Basic Protein ◽  
Human Eosinophil ◽  
Eosinophil Granule

scholarly journals Human eosinophil cationic protein. Molecular cloning of a cytotoxin and helminthotoxin with ribonuclease activity.

1989 ◽  
Vol 170 (1) ◽  
pp. 163-176 ◽  
Author(s):  
H F Rosenberg ◽  
S J Ackerman ◽  
D G Tenen
Keyword(s):  
Amino Acid ◽  
Cellular Localization ◽  
Basic Protein ◽  
Eosinophil Cationic Protein ◽  
Ribonuclease Activity ◽  
Monocytic Differentiation ◽  
Cationic Protein ◽  
Human Eosinophil ◽  
Reading Frame ◽  
The Matrix

We have isolated a 725-bp full-length cDNA clone for the human eosinophil cationic protein (ECP). ECP is a small, basic protein found in the matrix of the eosinophil's large specific granule that has cytotoxic, helminthotoxic, and ribonuclease activity, and is a member of the ribonuclease multigene family. The cDNA sequence shows 89% sequence identity with that reported for the related granule protein, eosinophil-derived neurotoxin (EDN). The open reading frame encodes a previously unidentified 27-amino acid leader sequence preceding a 133-residue mature ECP polypeptide with a molecular mass of 15.6 kD. The encoded amino acid sequence of ECP shows 66% identity to that of EDN and 31% identity to that of human pancreatic ribonuclease, including conservation of the essential structural cysteine and cataytic lysine and histidine residues. mRNA for ECP was detected in eosinophil-enriched peripheral granulocytes and in a subclone of the promyelocytic leukemia line, HL-60, induced toward eosinophilic differentiation with IL-5. No ECP mRNA was detected in uninduced HL-60 cells, or in HL-60 cells induced toward monocytic differentiation with vitamin D3 or toward neutrophilic differentiation with DMSO. In contrast, mRNA for EDN was detected in uninduced HL-60 cells and was upregulated in HL-60 cells induced with DMSO. Despite similarities in sequence and cellular localization, these results suggest that ECP and EDN are subject to different regulatory mechanisms.

scholarly journals Regulation of human eosinophil viability, density, and function by granulocyte/macrophage colony-stimulating factor in the presence of 3T3 fibroblasts.

1987 ◽  
Vol 166 (1) ◽  
pp. 129-141 ◽  
Author(s):  
W F Owen ◽  
M E Rothenberg ◽  
D S Silberstein ◽  
J C Gasson ◽  
R L Stevens ◽  
...  
Keyword(s):  
Maximal Response ◽  
Maximal Effect ◽  
Primary Role ◽  
Colony Stimulating Factor ◽  
Human Eosinophil ◽  
Gm Csf ◽  
3T3 Fibroblasts ◽  
Macrophage Colony Stimulating Factor ◽  
Macrophage Colony ◽  
Stimulating Factor

Normodense human peripheral blood eosinophils were isolated under sterile conditions from the 22/23 and 23/24% interfaces and the cell pellet of metrizamide gradients. After culture for 7 d in RPMI media in the presence of 50 pM biosynthetic (recombinant) human granulocyte/macrophage colony-stimulating factor (rH GM-CSF), 43 +/- 7% (mean +/- SEM, n = 8) of the cells were viable; in the absence of rH GM-CSF, no eosinophils survived. The rH GM-CSF-mediated viability was concentration dependent; increased survival began at a concentration of 1 pM, a 50% maximal response was attained at approximately 3 pM, and a maximal effect was reached at concentrations of greater than or equal to 10 pM rH GM-CSF. In the presence of rH GM-CSF and mouse 3T3 fibroblasts, 67 +/- 6% (mean +/- SEM, n = 8) of the eosinophils survived for 7 d. In a comparative analysis, there was no difference in eosinophil viability after 7 and 14 d (n = 3) in the presence of 50 pM GM-CSF and fibroblasts. Culture with fibroblasts alone did not support eosinophil survival. The addition of fibroblast-conditioned media to rH GM-CSF did not further improve eosinophil viability, indicating a primary role for GM-CSF in supporting these eosinophil cell suspensions ex vivo and a supplementary role for 3T3 fibroblasts. Eosinophils cultured for 7 d localized on density gradient sedimentation at the medium/18, 18/20, and 20/21 interfaces of metrizamide gradients, indicating a change to the hypodense phenotype from their original normodense condition. In addition, the cultured eosinophils generated approximately 2.5-fold more LTC4 than freshly isolated cells when stimulated with the calcium ionophore A23187 and manifested sevenfold greater antibody-dependent killing of S. mansoni larvae than the freshly isolated, normodense cells from the same donor. Thus we demonstrate the rH GM-CSF dependent conversion in vitro of normodense human eosinophils to hypodense cells possessing the augmented biochemical and biological properties characteristic of the hypodense eosinophils associated with a variety of hypereosinophilic syndromes. In addition, these studies provide a culture model of at least 14 d suitable for the further characterization of hypodense eosinophils.

The Effect of Nedocromil Sodium on Human Eosinophil Activation

Drugs ◽  
1989 ◽  
Vol 37 (Supplement 1) ◽  
pp. 19-22 ◽  
Author(s):  
R. Moqbel ◽  
O. Cromwell ◽  
A. B. Kay
Keyword(s):  
Nedocromil Sodium ◽  
Human Eosinophil ◽  
Eosinophil Activation
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