Lipoxin A4 inhibits phosphoinositide hydrolysis in human neutrophils

Beatrice M. Grandordy; Helene Lacroix; Elie Mavoungou; Steven Krilis; Attilio E.G. Crea; Bernd W. Spur; Tak H. Lee

doi:10.1016/0006-291X(90)90625-W

Lipoxin A₄ inhibits phosphoinositide hydrolysis in human neutrophils

Beatrice M. Grandordy, Helene Lacroix, Elie Mavoungou, Steven Krilis, Attilio E.G. Crea, Bernd W. Spur, Tak H. Lee

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Abstract

Lipoxins (LX) are trihydroxytetraene metabolites derived from arachidonic acid via an interaction between the 5- and 15-lipoxygenases. Preincubation of [³H] myo-inositol labeled PMN with 10^-7M and 10^-5M LXA₄ for 1 minute at 37°C resulted in a concentration dependent inhibition of the generation of [³H] IP3 and [³H] IP in cells subsequently stimulated by increasing doses of LTB₄ or FMLP for 1 minute at 37°C. Preincubation of PMN with LXA₄ did not inhibit specific binding of [³H] LTB₄ to PMN. These results indicate that LXA₄ inhibits chemotactic factor-induced phosphoinositide hydrolysis at a post-receptor level.

Original language	English (US)
Pages (from-to)	1022-1029
Number of pages	8
Journal	Biochemical and Biophysical Research Communications
Volume	167
Issue number	3
DOIs	https://doi.org/10.1016/0006-291X(90)90625-W
State	Published - Mar 30 1990
Externally published	Yes

All Science Journal Classification (ASJC) codes

Biophysics
Biochemistry
Molecular Biology
Cell Biology

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10.1016/0006-291X(90)90625-W

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title = "Lipoxin A4 inhibits phosphoinositide hydrolysis in human neutrophils",

abstract = "Lipoxins (LX) are trihydroxytetraene metabolites derived from arachidonic acid via an interaction between the 5- and 15-lipoxygenases. Preincubation of [3H] myo-inositol labeled PMN with 10-7M and 10-5M LXA4 for 1 minute at 37°C resulted in a concentration dependent inhibition of the generation of [3H] IP3 and [3H] IP in cells subsequently stimulated by increasing doses of LTB4 or FMLP for 1 minute at 37°C. Preincubation of PMN with LXA4 did not inhibit specific binding of [3H] LTB4 to PMN. These results indicate that LXA4 inhibits chemotactic factor-induced phosphoinositide hydrolysis at a post-receptor level.",

author = "Grandordy, {Beatrice M.} and Helene Lacroix and Elie Mavoungou and Steven Krilis and Crea, {Attilio E.G.} and Spur, {Bernd W.} and Lee, {Tak H.}",

year = "1990",

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doi = "10.1016/0006-291X(90)90625-W",

language = "English (US)",

volume = "167",

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TY - JOUR

T1 - Lipoxin A4 inhibits phosphoinositide hydrolysis in human neutrophils

AU - Grandordy, Beatrice M.

AU - Lacroix, Helene

AU - Mavoungou, Elie

AU - Krilis, Steven

AU - Crea, Attilio E.G.

AU - Spur, Bernd W.

AU - Lee, Tak H.

PY - 1990/3/30

Y1 - 1990/3/30

N2 - Lipoxins (LX) are trihydroxytetraene metabolites derived from arachidonic acid via an interaction between the 5- and 15-lipoxygenases. Preincubation of [3H] myo-inositol labeled PMN with 10-7M and 10-5M LXA4 for 1 minute at 37°C resulted in a concentration dependent inhibition of the generation of [3H] IP3 and [3H] IP in cells subsequently stimulated by increasing doses of LTB4 or FMLP for 1 minute at 37°C. Preincubation of PMN with LXA4 did not inhibit specific binding of [3H] LTB4 to PMN. These results indicate that LXA4 inhibits chemotactic factor-induced phosphoinositide hydrolysis at a post-receptor level.

AB - Lipoxins (LX) are trihydroxytetraene metabolites derived from arachidonic acid via an interaction between the 5- and 15-lipoxygenases. Preincubation of [3H] myo-inositol labeled PMN with 10-7M and 10-5M LXA4 for 1 minute at 37°C resulted in a concentration dependent inhibition of the generation of [3H] IP3 and [3H] IP in cells subsequently stimulated by increasing doses of LTB4 or FMLP for 1 minute at 37°C. Preincubation of PMN with LXA4 did not inhibit specific binding of [3H] LTB4 to PMN. These results indicate that LXA4 inhibits chemotactic factor-induced phosphoinositide hydrolysis at a post-receptor level.

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JO - Biochemical and Biophysical Research Communications

JF - Biochemical and Biophysical Research Communications

IS - 3

ER -

Lipoxin A₄ inhibits phosphoinositide hydrolysis in human neutrophils

Abstract

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