Interactions of the cytotoxic RNase A dimers with the cytosolic ribonuclease inhibitor

Mariarosaria Naddeo; Luigi Vitagliano; Aniello Russo; Giovanni Gotte; Giuseppe D'Alessio; Salvatore Sorrentino

doi:10.1016/j.febslet.2005.03.087

Interactions of the cytotoxic RNase A dimers with the cytosolic ribonuclease inhibitor

FEBS Lett. 2005 May 9;579(12):2663-8. doi: 10.1016/j.febslet.2005.03.087. Epub 2005 Apr 9.

Authors

Mariarosaria Naddeo¹, Luigi Vitagliano, Aniello Russo, Giovanni Gotte, Giuseppe D'Alessio, Salvatore Sorrentino

Affiliation

¹ Dipartimento di Biologia Strutturale e Funzionale, Università di Napoli Federico II, Italy.

PMID: 15862306
DOI: 10.1016/j.febslet.2005.03.087

Abstract

Ribonuclease A (RNase A) dimers have been recently found to be endowed with some of the special, i.e., non-catalytic biological activities of RNases, such as antitumor and aspermatogenic activities. These activities have been so far attributed to RNases which can escape the neutralizing action of the cytosolic RNase inhibitor (cRI). However, when the interactions of the two cytotoxic RNase A dimers with cRI were investigated in a quantitative fashion and at the molecular level, the dimers were found to bind cRI with high affinity and to form tight complexes.

Publication types

Comparative Study
Research Support, Non-U.S. Gov't

MeSH terms

Animals
Cattle
Cytosol / enzymology*
Cytotoxins / genetics*
Cytotoxins / metabolism*
Dimerization
Electrophoresis, Polyacrylamide Gel
Enzyme Inhibitors / metabolism*
Hydrogen-Ion Concentration
Kinetics
Models, Molecular
Protein Binding
Ribonuclease, Pancreatic / antagonists & inhibitors
Ribonuclease, Pancreatic / chemistry
Ribonuclease, Pancreatic / genetics*
Ribonuclease, Pancreatic / metabolism*
Spectrophotometry

Substances

Cytotoxins
Enzyme Inhibitors
angiogenin
Ribonuclease, Pancreatic