Photoactivated inhibition of superoxide generation and protein kinase C activity in neutrophils by blepharismin, a protozoan photodynamically active pigment

Yoshiya Watanabe; Keisuke E-ige; Hirotsugu Kobuchi; Yoji Kato; Tatsuomi Matsuoka; Toshihiko Utsumi; Tamotsu Yoshioka; Alan A. Horton; Kozo Utsumi

doi:10.1016/0006-2952(94)00409-F

Photoactivated inhibition of superoxide generation and protein kinase C activity in neutrophils by blepharismin, a protozoan photodynamically active pigment

Yoshiya Watanabe, Keisuke E-ige, Hirotsugu Kobuchi, Yoji Kato, Tatsuomi Matsuoka, Toshihiko Utsumi, Tamotsu Yoshioka, Alan A. Horton, Kozo Utsumi

Research output: Contribution to journal › Article › peer-review

8 Citations (Scopus)

Abstract

Blepharismin is an endogenous photosensitizing pigment found in the protozoan Blepharisma. This pigment inhibited the generation of Superoxide anion (O₂^-) in neutrophils not only via a diacylglycerol-induced protein kinase C (PKC)-dependent reaction but also by an arachidonate-induced PKC-independent reaction. The inhibition was light and concentration dependent for both reactions. Light-activated inhibition was strong at wavelengths between 520 and 570nm but not above 610nm. PKC activity in neutrophils and from rat brain was inhibited by blepharismin in a light- and concentration dependent manner. Moreover, arachidonate-activated NADPH oxidase activity in a cell-free system was also inhibited by the pigment in a light- and concentration-dependent manner. These results suggest that blepharismin inhibits NADPH oxidase activation through the non-specific inhibition of various membrane-bound enzymes and that this inhibition may also be correlated with that of PKC.

Original language	English
Pages (from-to)	529-536
Number of pages	8
Journal	Biochemical Pharmacology
Volume	49
Issue number	4
DOIs	https://doi.org/10.1016/0006-2952(94)00409-F
Publication status	Published - Feb 14 1995
Externally published	Yes

Keywords

NADPH-oxida se
active oxygen generation
enzyme inhibition
fluorescence of pigment
perylenequinones
tyrosine kinase

ASJC Scopus subject areas

Biochemistry
Pharmacology

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Photoactivated inhibition of superoxide generation and protein kinase C activity in neutrophils by blepharismin, a protozoan photodynamically active pigment. / Watanabe, Yoshiya; E-ige, Keisuke; Kobuchi, Hirotsugu; Kato, Yoji; Matsuoka, Tatsuomi; Utsumi, Toshihiko; Yoshioka, Tamotsu; Horton, Alan A.; Utsumi, Kozo.

In: Biochemical Pharmacology, Vol. 49, No. 4, 14.02.1995, p. 529-536.

Research output: Contribution to journal › Article › peer-review

Watanabe, Yoshiya ; E-ige, Keisuke ; Kobuchi, Hirotsugu ; Kato, Yoji ; Matsuoka, Tatsuomi ; Utsumi, Toshihiko ; Yoshioka, Tamotsu ; Horton, Alan A. ; Utsumi, Kozo. / Photoactivated inhibition of superoxide generation and protein kinase C activity in neutrophils by blepharismin, a protozoan photodynamically active pigment. In: Biochemical Pharmacology. 1995 ; Vol. 49, No. 4. pp. 529-536.

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title = "Photoactivated inhibition of superoxide generation and protein kinase C activity in neutrophils by blepharismin, a protozoan photodynamically active pigment",

abstract = "Blepharismin is an endogenous photosensitizing pigment found in the protozoan Blepharisma. This pigment inhibited the generation of Superoxide anion (O2-) in neutrophils not only via a diacylglycerol-induced protein kinase C (PKC)-dependent reaction but also by an arachidonate-induced PKC-independent reaction. The inhibition was light and concentration dependent for both reactions. Light-activated inhibition was strong at wavelengths between 520 and 570nm but not above 610nm. PKC activity in neutrophils and from rat brain was inhibited by blepharismin in a light- and concentration dependent manner. Moreover, arachidonate-activated NADPH oxidase activity in a cell-free system was also inhibited by the pigment in a light- and concentration-dependent manner. These results suggest that blepharismin inhibits NADPH oxidase activation through the non-specific inhibition of various membrane-bound enzymes and that this inhibition may also be correlated with that of PKC.",

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author = "Yoshiya Watanabe and Keisuke E-ige and Hirotsugu Kobuchi and Yoji Kato and Tatsuomi Matsuoka and Toshihiko Utsumi and Tamotsu Yoshioka and Horton, {Alan A.} and Kozo Utsumi",

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AU - E-ige, Keisuke

AU - Kobuchi, Hirotsugu

AU - Kato, Yoji

AU - Matsuoka, Tatsuomi

AU - Utsumi, Toshihiko

AU - Yoshioka, Tamotsu

AU - Horton, Alan A.

AU - Utsumi, Kozo

PY - 1995/2/14

Y1 - 1995/2/14

N2 - Blepharismin is an endogenous photosensitizing pigment found in the protozoan Blepharisma. This pigment inhibited the generation of Superoxide anion (O2-) in neutrophils not only via a diacylglycerol-induced protein kinase C (PKC)-dependent reaction but also by an arachidonate-induced PKC-independent reaction. The inhibition was light and concentration dependent for both reactions. Light-activated inhibition was strong at wavelengths between 520 and 570nm but not above 610nm. PKC activity in neutrophils and from rat brain was inhibited by blepharismin in a light- and concentration dependent manner. Moreover, arachidonate-activated NADPH oxidase activity in a cell-free system was also inhibited by the pigment in a light- and concentration-dependent manner. These results suggest that blepharismin inhibits NADPH oxidase activation through the non-specific inhibition of various membrane-bound enzymes and that this inhibition may also be correlated with that of PKC.

AB - Blepharismin is an endogenous photosensitizing pigment found in the protozoan Blepharisma. This pigment inhibited the generation of Superoxide anion (O2-) in neutrophils not only via a diacylglycerol-induced protein kinase C (PKC)-dependent reaction but also by an arachidonate-induced PKC-independent reaction. The inhibition was light and concentration dependent for both reactions. Light-activated inhibition was strong at wavelengths between 520 and 570nm but not above 610nm. PKC activity in neutrophils and from rat brain was inhibited by blepharismin in a light- and concentration dependent manner. Moreover, arachidonate-activated NADPH oxidase activity in a cell-free system was also inhibited by the pigment in a light- and concentration-dependent manner. These results suggest that blepharismin inhibits NADPH oxidase activation through the non-specific inhibition of various membrane-bound enzymes and that this inhibition may also be correlated with that of PKC.

KW - NADPH-oxida se

KW - active oxygen generation

KW - enzyme inhibition

KW - fluorescence of pigment

KW - perylenequinones

KW - tyrosine kinase

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Photoactivated inhibition of superoxide generation and protein kinase C activity in neutrophils by blepharismin, a protozoan photodynamically active pigment

Abstract

Keywords

ASJC Scopus subject areas

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