Ribonuclease Activity of Cationic Structures Conjugated to Lipophilic Groups

2004 ◽  
Vol 23 (6-7) ◽  
pp. 977-981 ◽  
Author(s):  
N. Koval'ov ◽  
I. Kuznetsova ◽  
E. Burakova ◽  
V. Sil'nikov ◽  
M. Zenkova ◽  
...  
Keyword(s):  
Ribonuclease Activity ◽  
Lipophilic Groups

Ribonuclease Activity of Cationic Structures Conjugated to Lipophilic Groups

ChemInform ◽  
2005 ◽  
Vol 36 (6) ◽  
Author(s):  
N. Koval'ov ◽  
I. Kuznetsova ◽  
E. Burakova ◽  
V. Sil'nikov ◽  
M. Zenkova ◽  
...  
Keyword(s):  
Ribonuclease Activity ◽  
Lipophilic Groups

THE HORMONAL CONTROL OF RIBONUCLEASE ACTIVITY IN THE LYMPHATIC TISSUE OF MICE

1973 ◽  
Vol 74 (1) ◽  
pp. 201-208 ◽  
Author(s):  
D. Maor ◽  
E. Eylan ◽  
P. Alexander
Keyword(s):  
Growth Hormone ◽  
Lymph Nodes ◽  
Hormonal Control ◽  
Ribonuclease Activity ◽  
Lymphatic Tissue

ABSTRACT Ribonuclease activity in thymus and lymph nodes is stimulated by cortisone; insulin increases ribonuclease activity only in the thymus. Growth hormone and theophylline do not cause changes in thymus and lymph nodes ribonuclease levels. Injections of cortisone combined with growth hormone or with theophylline increase the activity more than cortisone alone. Insulin does not enhance the action of cortisone on ribonuclease activity. A synergistic loss in weight of thymus and spleen was found after administration of cortisone in combination with either growth hormone or with theophylline.

Serum ribonuclease activity in the diagnosis of prostate cancer in men with serum prostate-specific antigen levels between 2.5 and 20 ng/mL

2006 ◽  
Vol 39 (4) ◽  
pp. 363-366 ◽  
Author(s):  
Saadettin Yilmaz Eskicorapci ◽  
H. Asuman Özkara ◽  
Evren Önder ◽  
Bulent Akdogan ◽  
İlhan Erkan ◽  
...  
Keyword(s):  
Prostate Cancer ◽  
Prostate Specific Antigen ◽  
Specific Antigen ◽  
Ribonuclease Activity ◽  
Serum Prostate Specific Antigen ◽  
Serum Ribonuclease

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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