Involvement of A 3 receptors in the potentiation by adenosine of the inhibitory effect of theophylline on human eosinophil degranulation: possible novel mechanism of the anti-inflammatory action of theophylline 1 1Abbreviations: C5a, complement fragment 5a; ECP, eosinophil cationic protein; EDN, eosinophil-derived neurotoxin; EPO, eosinophil peroxidase; OPD, O-phenylenediamine; CGS 21680, 2-[[2-[4-(2-carboxyethyl)phenyl]ethyl]amino]-N-ethylcarboxamidoadenosine; CPA, N-cyclopentyladenosine; DMPX, 3,7-dimethyl-1-propargylxanthine; DPCPX, 1,3-dipropyly-8-cyclo-pentylxanthine; IB-MECA, N6-(3-iodobenzyl)-5′-N-methylcarbamoyladen-osine; MBP, major basic protein; MRS1220, 9-chloro-2-(2-furyl)-5-phenyl-actylamino[1,2,4]triazolo[1,5-c]quinazoline; PDE, phosphodiesterase; cAMP, adenosine 3′,5′-cyclic monophosphate.

2001 ◽  
Vol 61 (12) ◽  
pp. 1551-1559 ◽  
Author(s):  
Charles I. Ezeamuzie
Keyword(s):  
Basic Protein ◽  
Eosinophil Cationic Protein ◽  
Inhibitory Effect ◽  
Major Basic Protein ◽  
Cationic Protein ◽  
Human Eosinophil ◽  
Cyclic Monophosphate ◽  
Cgs 21680 ◽  
Inflammatory Action ◽  
Eosinophil Degranulation

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 Peptides of major basic protein and eosinophil cationic protein activate human mast cells

2020 ◽  
Vol 21 ◽  
pp. 100719 ◽  
Author(s):  
Hiroyuki Ogasawara ◽  
Masahiro Furuno ◽  
Koji Edamura ◽  
Masato Noguchi
Keyword(s):  
Mast Cells ◽  
Basic Protein ◽  
Eosinophil Cationic Protein ◽  
Major Basic Protein ◽  
Cationic Protein ◽  
Human Mast Cells

scholarly journals Helicobacter pyloriOuter Membrane Vesicle Proteins Induce Human Eosinophil Degranulation via aβ2 Integrin CD11/CD18- and ICAM-1-Dependent Mechanism

2015 ◽  
Vol 2015 ◽  
pp. 1-12 ◽  
Author(s):  
Su Hyuk Ko ◽  
Jong Ik Jeon ◽  
Young-Jeon Kim ◽  
Ho Joo Yoon ◽  
Hyeyoung Kim ◽  
...  
Keyword(s):  
Epithelial Cells ◽  
Inflammatory Responses ◽  
Membrane Vesicle ◽  
Eosinophil Cationic Protein ◽  
Outer Membrane Vesicles ◽  
Gastric Epithelial Cells ◽  
Cationic Protein ◽  
Human Eosinophil ◽  
H Pylori ◽  
Eosinophil Degranulation

Eosinophil cationic protein (ECP), a cytotoxic protein contained in eosinophils granules, can contribute to various inflammatory responses. AlthoughHelicobacter pyloriinfection increases infiltration of eosinophils, the mechanisms of eosinophil degranulation byH. pyloriinfection are largely unknown. The goal of this study was to investigate the role ofH. pyloriouter membrane vesicles (OMVs) in modulating eosinophil degranulation. We found that eosinophils treated withH. pyloriOMVs released significantly more ECP compared with untreated controls. In addition, eosinophils cocultured with OMV-preexposed primary gastric epithelial cells exhibited significantly increased ECP release. Similarly, eosinophils cocultured with culture supernatant (CM) from primary gastric epithelial cells exposed to OMVs (OMV-CM) released significantly higher amounts of ECP compared with eosinophils cocultured with CM from unexposed control cells. Furthermore, OMVs and OMV-CM both induced the upregulation of ICAM-1 on gastric epithelial cells andβ2 integrin CD11b on eosinophils. In addition, both transduction ofICAM-1shRNA into gastric epithelial cells and treatment with neutralizing mAbs to CD18 significantly decreased OMV-mediated or OMV-CM-mediated release of ECP. These results suggest that the eosinophil degranulation response toH. pyloriOMVs occurs via a mechanism that is dependent on bothβ2 integrin CD11/CD18 and ICAM-1.

scholarly journals Decreased expression of eosinophil peroxidase and major basic protein messenger RNAs during eosinophil maturation

Blood ◽  
1992 ◽  
Vol 79 (10) ◽  
pp. 2592-2597 ◽  
Author(s):  
V Gruart ◽  
MJ Truong ◽  
J Plumas ◽  
M Zandecki ◽  
JP Kusnierz ◽  
...  
Keyword(s):  
Time Course ◽  
Basic Protein ◽  
Blot Hybridization ◽  
Eosinophil Cationic Protein ◽  
Northern Blot Hybridization ◽  
Messenger Rnas ◽  
Major Basic Protein ◽  
Regulation Of Expression ◽  
Cationic Protein ◽  
Eosinophil Peroxidase

Abstract We evaluated the levels of mRNAs encoding cationic proteins in peripheral blood eosinophils (PBE) purified from patients with eosinophilia and in eosinophils differentiated from cord blood cells (CBC) by culture with recombinant human interleukin-3 (rhIL-3), rhGM- CSF, and rhIL-5. Messenger RNAs encoding eosinophil peroxidase (EPO), major basic protein (MBP), eosinophil-derived neurotoxin (EDN), and eosinophil cationic protein (ECP) were detected by Northern blot hybridization with the respective specific oligonucleotide probes. In mature PBE, MBP mRNA appeared to be absent, whereas EPO mRNA was barely detectable in only 5 of the 19 patients. In contrast, EDN and ECP mRNAs were observed in the PBE of all patients. In CE, EPO, and MBP, mRNAs were abundant in immature eosinophils and their amounts decreased after differentiation toward eosinophils. ECP and EDN mRNAs followed the same patterns, but mRNAs were less abundant at all timepoints studied. Study of mRNA t1/2 during the time course of differentiation indicated that changes in the stability of the different mRNAs were not responsible for the variations observed in the steady-state levels. Together, these results suggest that regulation of expression differs among EPO, MBP, EDN, and ECP mRNAs during the time course of eosinophil differentiation.

scholarly journals Localization of eosinophil cationic protein, major basic protein, and eosinophil peroxidase in human eosinophils by immunoelectron microscopic technique.

1986 ◽  
Vol 34 (11) ◽  
pp. 1399-1403 ◽  
Author(s):  
A Egesten ◽  
J Alumets ◽  
C von Mecklenburg ◽  
M Palmegren ◽  
I Olsson
Keyword(s):  
Basic Protein ◽  
Intracellular Localization ◽  
Protein A ◽  
Eosinophil Cationic Protein ◽  
Specific Marker ◽  
Microscopic Technique ◽  
Major Basic Protein ◽  
Cationic Protein ◽  
Eosinophil Peroxidase ◽  
The Matrix

An immunoelectron microscopic technique using protein A-gold as a specific marker was used for precise intracellular localization of eosinophil granule proteins. Eosinophils from healthy individuals were isolated in metrizamide gradients. Eosinophil cationic protein (ECP) and eosinophil peroxidase (EPO) were clearly located in the matrix of the large crystalloid-containing granules. In addition, ECP was probably present in the small granules of eosinophils. Major basic protein (MBP) was present in the crystalloid structure of specific granules. This method can be applied in studies of eosinophil degranulation to trace the release of biological effector molecules.

scholarly journals Major basic protein, but not eosinophil cationic protein or eosinophil protein X, is related to atopy in cystic fibrosis

Allergy ◽  
1999 ◽  
Vol 54 (10) ◽  
pp. 1094-1099 ◽  
Author(s):  
D.Y. Koller ◽  
G. Halmerbauer ◽  
J. Müller ◽  
T. Frischer ◽  
M. Schierl
Keyword(s):  
Cystic Fibrosis ◽  
Basic Protein ◽  
Eosinophil Cationic Protein ◽  
Major Basic Protein ◽  
Cationic Protein ◽  
Protein X
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