Role of guanine nucleotide regulatory protein in polyphosphoinositide degradation and activation of phagocytic leukocytes by chemoattractants

1986 ◽  
Vol 32 (1) ◽  
pp. 59-69 ◽  
Author(s):  
Margrith W. Verghese ◽  
Charles D. Smith ◽  
Ralph Snyderman
1990 ◽  
Vol 1990 (Supplement 13) ◽  
pp. 43-56 ◽  
Author(s):  
E. ROZENGURT ◽  
I. FABREGAT ◽  
A. COFFER ◽  
J. GIL ◽  
J. SINNETT-SMITH

1986 ◽  
Vol 239 (1) ◽  
pp. 97-102 ◽  
Author(s):  
P G Bradford ◽  
R P Rubin

Rabbit neutrophils labelled with [3H]inositol and permeabilized with saponin produced [3H]inositol trisphosphate (InsP3) when incubated with stable analogues of GTP or millimolar concentrations of Ca2+. [3H]InsP3 production elicited by guanosine 5′-[gamma-thio]triphosphate was enhanced by the chemoattractant formylmethionyl-leucyl-phenylalanine and inhibited by pertussis-toxin pretreatment. A pertussis-toxin-sensitive stimulation of [3H]InsP3 concentration was also observed with guanosine 5′-[beta gamma-imido]triphosphate, but not with guanosine 5′-[beta-thio]diphosphate or GTP. Millimolar Ca2+ alone was sufficient to stimulate [3H]InsP3 production; however, in the presence of guanosine 5′-[gamma-thio]triphosphate, the Ca2+ dose-response curve was shifted to submicromolar concentrations. These findings directly confirm the role of a pertussis-toxin-sensitive guanine nucleotide regulatory protein (G protein) in chemoattractant-stimulated phospholipase C activity in rabbit neutrophils. Moreover, the ability of guanine nucleotides to sensitize phospholipase C to physiologically relevant Ca2+ concentrations suggests that the role of the activated G protein may be to enhance the apparent affinity of phospholipase C for Ca2+ and thus to activate the enzyme without an increase in the Ca2+ concentration.


1989 ◽  
Vol 65 (8) ◽  
pp. 743-749
Author(s):  
Takashi MATOZAKI ◽  
Choitsu SAKAMOTO ◽  
Munehiko NAGAO ◽  
Hogara NISHISAKI ◽  
Yoshitaka KONDA ◽  
...  

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