Eosinophil cationic protein (ECP) can bind heparin and other glycosaminoglycans through its RNase active site

2010 ◽  
Vol 24 (1) ◽  
pp. 90-100 ◽  
Author(s):  
Marc Torrent ◽  
M. Victòria Nogués ◽  
Ester Boix
Keyword(s):  
Active Site ◽  
Eosinophil Cationic Protein ◽  
Cationic Protein ◽  
Rnase Active Site

The Crystal Structure of Eosinophil Cationic Protein in Complex with 2‘,5‘-ADP at 2.0 Å Resolution Reveals the Details of the Ribonucleolytic Active Site†,‡

Biochemistry ◽  
2002 ◽  
Vol 41 (40) ◽  
pp. 12100-12106 ◽  
Author(s):  
C. Gopi Mohan ◽  
Ester Boix ◽  
Hazel R. Evans ◽  
Zoran Nikolovski ◽  
M. Victòria Nogués ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Active Site ◽  
Eosinophil Cationic Protein ◽  
Cationic Protein

scholarly journals Blood eosinophils and serum eosinophil cationic protein in patients with acute and chronic urticaria

1996 ◽  
Vol 5 (2) ◽  
pp. 113-115 ◽  
Author(s):  
G. Di Lorenzo ◽  
P. Mansueto ◽  
M. Melluso ◽  
G. Candore ◽  
D. Cigna ◽  
...  
Keyword(s):  
Chronic Urticaria ◽  
Eosinophil Cationic Protein ◽  
Chronic Idiopathic Urticaria ◽  
Blood Eosinophil ◽  
Cationic Protein ◽  
Acute Urticaria ◽  
Asymptomatic Patients ◽  
The Moment ◽  
Blood Eosinophils ◽  
Eosinophil Counts

We have analysed the relationship of blood eosinophil count and serum eosinophil cationic protein (ECP) levels in patients with acute and chronic idiopathic urticaria. The ECP levels and eosinophil counts were measured in the peripheral blood of 15 patients with acute urticaria, 25 with chronic idiopathic urticaria and 10 normal healthy subjects. Blood eosinophil counts and serum ECP levels increased in all patients with acute urticaria. Concerning patients affected by chronic urticaria, taking into account the recrudescence of the disease at the moment of taking the blood sample, only symptomatic patients showed increased eosinophil blood values whereas serum ECP levels were increased both in symptomatic and asymptomatic patients. Furthermore, serum ECP levels in chronic urticaria did not correlate with the peripheral eosinophil counts, as they did in acute urticaria. The results of the present study indicate that eosinophils may play a role in the inflammatory mechanisms in patients with acute and chronic urticaria showing a positive correlation between serum ECP levels and disease activity.

Eosinophil cationic protein in atopic dermatitis: changes of serum levels by the anti-allergic agent ketotifen *

1994 ◽  
Vol 3 (1) ◽  
pp. 59-62 ◽  
Author(s):  
Kouichi Ikai ◽  
Atsuhiko Ogino ◽  
Ikuko Furukawa ◽  
Motoaki Ozaki ◽  
Mayumi Fujita ◽  
...  
Keyword(s):  
Atopic Dermatitis ◽  
Eosinophil Cationic Protein ◽  
Serum Levels ◽  
Cationic Protein

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.

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