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 journalArticle

7 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 languageEnglish
Pages (from-to)529-536
Number of pages8
JournalBiochemical Pharmacology
Volume49
Issue number4
DOIs
Publication statusPublished - Feb 14 1995
Externally publishedYes

Fingerprint

Pigments
Superoxides
Protein Kinase C
Neutrophils
Light
NADPH Oxidase
Cell-Free System
Diglycerides
Rats
Brain
Chemical activation
Membranes
Wavelength
blepharismin
Enzymes

Keywords

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

ASJC Scopus subject areas

  • Biochemistry
  • Pharmacology

Cite this

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 journalArticle

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.
@article{956ca5e5169e4a14a926c68476c0ddaa,
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.",
keywords = "active oxygen generation, enzyme inhibition, fluorescence of pigment, NADPH-oxida se, perylenequinones, tyrosine kinase",
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",
year = "1995",
month = "2",
day = "14",
doi = "10.1016/0006-2952(94)00409-F",
language = "English",
volume = "49",
pages = "529--536",
journal = "Biochemical Pharmacology",
issn = "0006-2952",
publisher = "Elsevier Inc.",
number = "4",

}

TY - JOUR

T1 - Photoactivated inhibition of superoxide generation and protein kinase C activity in neutrophils by blepharismin, a protozoan photodynamically active pigment

AU - Watanabe, Yoshiya

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 - active oxygen generation

KW - enzyme inhibition

KW - fluorescence of pigment

KW - NADPH-oxida se

KW - perylenequinones

KW - tyrosine kinase

UR - http://www.scopus.com/inward/record.url?scp=0028815821&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0028815821&partnerID=8YFLogxK

U2 - 10.1016/0006-2952(94)00409-F

DO - 10.1016/0006-2952(94)00409-F

M3 - Article

C2 - 7872958

AN - SCOPUS:0028815821

VL - 49

SP - 529

EP - 536

JO - Biochemical Pharmacology

JF - Biochemical Pharmacology

SN - 0006-2952

IS - 4

ER -