PMID- 2552991
OWN - NLM
STAT- MEDLINE
DCOM- 19891109
LR  - 20190501
IS  - 0264-6021 (Print)
IS  - 1470-8728 (Electronic)
IS  - 0264-6021 (Linking)
VI  - 261
IP  - 3
DP  - 1989 Aug 1
TI  - Activation of electropermeabilized neutrophils by adenosine 
      5'-[gamma-thio]triphosphate (ATP[S]). Role of phosphatases in stimulus-response 
      coupling.
PG  - 755-9
AB  - Electrically permeabilized human neutrophils were used to study the mechanism of 
      activation of the NADPH oxidase by chemotactic factors. The respiratory burst 
      elicited by formyl-methionyl-leucyl-phenylalanine (fMLP) was strictly dependent 
      on the addition of ATP. The response was also supported by adenosine 
      5'-[gamma-thio]triphosphate (ATP[S]), but not by the non-hydrolysable analogue 
      (p[NH]ppA). In the presence of ATP, displacement of fMLP from its receptor by 
      antagonist peptides resulted in the abrupt termination of the O2-consumption 
      burst. In contrast, the response persisted after displacement of fMLP when ATP[S] 
      was present. This finding is consistent with the formation of biologically active 
      thiophosphoproteins which are resistant to cleavage by cellular phosphatases. 
      Accordingly, lower concentrations of ATP[S], as compared with ATP, were required 
      to support the fMLP response. The data indicate that protein phosphatases control 
      the extent and duration of the response in cells stimulated with 
      chemoattractants. Unlike ATP, sub-millimolar concentrations of ATP[S] elicited a 
      spontaneous respiratory burst in the absence of fMLP or other stimuli. This 
      effect was inhibited by p[NH]ppA and was not observed in intact 
      (non-permeabilized) cells, indicating interaction of ATP[S] with an intracellular 
      adenine-nucleotide-binding site, possibly a protein kinase. These results suggest 
      that protein kinases are active in neutrophils in the absence of exogenous 
      stimuli, but that accumulation of the essential phosphoprotein(s) is normally 
      prevented by the ongoing vigorous phosphatase activity. It is conceivable that 
      control of the respiratory burst is exerted by inhibition of phosphatase 
      activity, instead of or in addition to the more commonly postulated activation of 
      protein kinases.
FAU - Grinstein, S
AU  - Grinstein S
AD  - Division of Cell Biology, Hospital for Sick Children, Toronto, Canada.
FAU - Hill, M
AU  - Hill M
FAU - Furuya, W
AU  - Furuya W
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - England
TA  - Biochem J
JT  - The Biochemical journal
JID - 2984726R
RN  - 35094-46-3 (adenosine 5'-O-(3-thiotriphosphate))
RN  - 59880-97-6 (N-Formylmethionine Leucyl-Phenylalanine)
RN  - 8L70Q75FXE (Adenosine Triphosphate)
RN  - EC 3.1.3.16 (Phosphoprotein Phosphatases)
SB  - IM
MH  - Adenosine Triphosphate/pharmacology
MH  - *Cell Membrane Permeability
MH  - Humans
MH  - N-Formylmethionine Leucyl-Phenylalanine
MH  - Neutrophils/drug effects/*metabolism
MH  - Oxygen Consumption/*drug effects
MH  - Phosphoprotein Phosphatases/*physiology
PMC - PMC1138896
EDAT- 1989/08/01 00:00
MHDA- 1989/08/01 00:01
PMCR- 1990/02/01
CRDT- 1989/08/01 00:00
PHST- 1989/08/01 00:00 [pubmed]
PHST- 1989/08/01 00:01 [medline]
PHST- 1989/08/01 00:00 [entrez]
PHST- 1990/02/01 00:00 [pmc-release]
AID - 10.1042/bj2610755 [doi]
PST - ppublish
SO  - Biochem J. 1989 Aug 1;261(3):755-9. doi: 10.1042/bj2610755.