The presence of Ca2+-independent phospholipase A1 highly specific for phosphatidylinositol in bovine brain

Hiroshi Ueda; Tetsuyuki Kobayashi; Masaaki Kishimoto; Tomonari Tsutsumi; Shiro Watanabe; Harumi Okuyama

doi:10.1006/bbrc.1993.2181

The presence of Ca²⁺-independent phospholipase A1 highly specific for phosphatidylinositol in bovine brain

Hiroshi Ueda, Tetsuyuki Kobayashi^*, Masaaki Kishimoto, Tomonari Tsutsumi, Shiro Watanabe, Harumi Okuyama

^*Corresponding author for this work

Section of Host Defences, Division of Bioscience, Institute of Natural Medicine

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

22 Scopus citations

Abstract

EDTA-insensitive phospholipase A activity hydrolyzing phosphatidylinositol was detected in a bovine brain soluble fraction. This phospholipase A was purified 25-fold by sequential chromatographies of DEAE-Toyopearl, Phenyl-Toyopearl, and Ultrahydrogel 1000. The partially purified EDTA-insensitive phospholipase A showed an apparent molecular mass of 230kDa on an Ultrahydrogel 1000 column in the presence of 0.05% Triton X-100 and a pH optimum at 7.0. The enzyme was highly specific for phosphatidylinositol; phosphatidylethanolamine and phosphatidylcholine were not hydrolyzed significantly. The enzyme activity was characterized as phospholipase A1, and Ca²⁺ and Mg²⁺ were not required for its activity. These results indicate the existence of Ca²⁺-independent, phosphatidylinositol-specific metabolism besides those catalyzed by Ca²⁺-dependent phospholipase A2 and Ca²⁺-dependent, phosphatidylinositol-specific phospholipase C.

Original language	English
Pages (from-to)	1272-1279
Number of pages	8
Journal	Biochemical and Biophysical Research Communications
Volume	195
Issue number	3
DOIs	https://doi.org/10.1006/bbrc.1993.2181
State	Published - 1993/09/30

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology
Cell Biology

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10.1006/bbrc.1993.2181

Cite this

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title = "The presence of Ca2+-independent phospholipase A1 highly specific for phosphatidylinositol in bovine brain",

abstract = "EDTA-insensitive phospholipase A activity hydrolyzing phosphatidylinositol was detected in a bovine brain soluble fraction. This phospholipase A was purified 25-fold by sequential chromatographies of DEAE-Toyopearl, Phenyl-Toyopearl, and Ultrahydrogel 1000. The partially purified EDTA-insensitive phospholipase A showed an apparent molecular mass of 230kDa on an Ultrahydrogel 1000 column in the presence of 0.05% Triton X-100 and a pH optimum at 7.0. The enzyme was highly specific for phosphatidylinositol; phosphatidylethanolamine and phosphatidylcholine were not hydrolyzed significantly. The enzyme activity was characterized as phospholipase A1, and Ca2+ and Mg2+ were not required for its activity. These results indicate the existence of Ca2+-independent, phosphatidylinositol-specific metabolism besides those catalyzed by Ca2+-dependent phospholipase A2 and Ca2+-dependent, phosphatidylinositol-specific phospholipase C.",

author = "Hiroshi Ueda and Tetsuyuki Kobayashi and Masaaki Kishimoto and Tomonari Tsutsumi and Shiro Watanabe and Harumi Okuyama",

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AU - Ueda, Hiroshi

AU - Kobayashi, Tetsuyuki

AU - Kishimoto, Masaaki

AU - Tsutsumi, Tomonari

AU - Watanabe, Shiro

AU - Okuyama, Harumi

PY - 1993/9/30

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N2 - EDTA-insensitive phospholipase A activity hydrolyzing phosphatidylinositol was detected in a bovine brain soluble fraction. This phospholipase A was purified 25-fold by sequential chromatographies of DEAE-Toyopearl, Phenyl-Toyopearl, and Ultrahydrogel 1000. The partially purified EDTA-insensitive phospholipase A showed an apparent molecular mass of 230kDa on an Ultrahydrogel 1000 column in the presence of 0.05% Triton X-100 and a pH optimum at 7.0. The enzyme was highly specific for phosphatidylinositol; phosphatidylethanolamine and phosphatidylcholine were not hydrolyzed significantly. The enzyme activity was characterized as phospholipase A1, and Ca2+ and Mg2+ were not required for its activity. These results indicate the existence of Ca2+-independent, phosphatidylinositol-specific metabolism besides those catalyzed by Ca2+-dependent phospholipase A2 and Ca2+-dependent, phosphatidylinositol-specific phospholipase C.

AB - EDTA-insensitive phospholipase A activity hydrolyzing phosphatidylinositol was detected in a bovine brain soluble fraction. This phospholipase A was purified 25-fold by sequential chromatographies of DEAE-Toyopearl, Phenyl-Toyopearl, and Ultrahydrogel 1000. The partially purified EDTA-insensitive phospholipase A showed an apparent molecular mass of 230kDa on an Ultrahydrogel 1000 column in the presence of 0.05% Triton X-100 and a pH optimum at 7.0. The enzyme was highly specific for phosphatidylinositol; phosphatidylethanolamine and phosphatidylcholine were not hydrolyzed significantly. The enzyme activity was characterized as phospholipase A1, and Ca2+ and Mg2+ were not required for its activity. These results indicate the existence of Ca2+-independent, phosphatidylinositol-specific metabolism besides those catalyzed by Ca2+-dependent phospholipase A2 and Ca2+-dependent, phosphatidylinositol-specific phospholipase C.

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