Chemotactic peptide, calcium and guanine nucleotide regulation of phospholipase C activity in membranes from DMSO-differentiated HL60 cells

1987 ◽  
Vol 145 (2) ◽  
pp. 825-833 ◽  
Author(s):  
John C. Anthes ◽  
M.Motasim Billah ◽  
Ann Cali ◽  
Robert W. Egan ◽  
Marvin I. Siegel
Author(s):  
J. L. Boyer ◽  
M. W. Martin ◽  
C. L. Cooper ◽  
G. L. Waldo ◽  
A. J. Morris ◽  
...  

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.


1988 ◽  
Vol 262 (2) ◽  
pp. 532-542 ◽  
Author(s):  
Russell J. Wyborski ◽  
Edwin M. Horwitz ◽  
W. Terry Jenkins ◽  
Jeffrey S. Mormol ◽  
Ruth S. Gurd

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