Mimicking of discontinuous epitopes by phage-displayed peptides, II. Selection of clones recognized by a protective monoclonal antibody against the Bordetella pertussis toxin from phage peptide libraries

Gene ◽  
1993 ◽  
Vol 128 (1) ◽  
pp. 21-27 ◽  
Author(s):  
Franco Felici ◽  
Alessandra Luzzago ◽  
Antonella Folgori ◽  
Riccardo Cortese
1988 ◽  
Vol 152 (3) ◽  
pp. 1185-1192 ◽  
Author(s):  
Philippe Brabet ◽  
Colette Pantaloni ◽  
Bruce Rouot ◽  
Madeleine Toutant ◽  
Adolfo Garcia-Sainz ◽  
...  

2006 ◽  
Vol 65 (1) ◽  
pp. 153-158 ◽  
Author(s):  
Martin Storm ◽  
Abdolreza Advani ◽  
Monica Pettersson ◽  
Hans O. Hallander ◽  
Kåre Bondeson

1989 ◽  
Vol 258 (3) ◽  
pp. 669-675 ◽  
Author(s):  
S J Persaud ◽  
P M Jones ◽  
S L Howell

Noradrenaline- and clonidine-induced inhibition of insulin release from intact and electrically permeabilized rat islets was markedly relieved by prior exposure to 100 ng of Bordetella pertussis toxin/ml. The reversal of catecholamine inhibition of insulin secretion by this toxin was not associated with a decrease in specific binding of the alpha 2-adrenergic ligand [3H]yohimbine, and could not be fully explained by an increase in intracellular cyclic AMP. Exposure of intact islets to 1 microgram of pertussis toxin/ml for 2 h, followed by electrical permeabilization and incubation with 5 microCi of [alpha-32P]NAD+, resulted in the ADP-ribosylation in situ of a protein of molecular mass approx. 41 kDa. These results suggest that pertussis toxin alleviates catecholamine inhibition of beta-cell secretory responses by ADP-ribosylating at least one protein of molecular mass 41 kDa. In analogous systems the 41 kDa substrate of pertussis toxin has been shown to be the alpha subunit of Gi, but catecholamine-activated G proteins linked to effector systems other than adenylate cyclase might also be modified by this toxin in pancreatic beta-cells.


Sign in / Sign up

Export Citation Format

Share Document