Technology ID
TAB-399

Clones Encoding Mammalian ADP-Ribosylarginine Hydrolases

E-Numbers
E-076-1992-0
Co-Inventors
Moss, Joel
Stanley, Sally
Nightingale, Maria
Murtagh, James
Monaco, Lucia
Takada, Tatsuyuki
Applications
Therapeutics
Diagnostics
Therapeutic Areas
Infectious Disease
ADP-ribosylation of arginine residues in proteins may be involved in cell adhesion and is crucial for the action of cholera toxin and E. coli heat-labile enterotoxin, agents involved in the pathogenesis of cholera and traveller's diarrhoea, respectively. ADP-ribosylation is reversed by ADP-ribosylarginine hydrolases, which cleave the ADP-ribose-arginine bond. ADP-ribosylarginine hydrolases from a variety of mammalian species and tissues were isolated, and the coding regions for the hydrolases were cloned and expressed. The availability of this new hydrolase cDNA and expression system provides a novel molecular approach for studying the role of ADP-ribosylation in cell function. The gene products may be useful in treating or preventing a variety of bacterial diseases, including cholera, that appear to be mediated via ADP-ribosylation.
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