Reconstitution of GTP‐γ‐S‐dependent phospholipase D activity with ARF, RhoA, and a soluble 36‐kDa protein

Shimooku, Kiyoshi; Akisue, Toshihiro; Jinnai, Hitoshi; Hitomi, Tomohiro; Ogino, Chiaki; Yoshida, Kohsuke; Nakamura, Shun‐ichi; Nishizuka, Yasutomi

doi:10.1016/0014-5793(96)00483-8

Cited by 14 publications

(19 citation statements)

References 29 publications

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“…4A). This level of stimulation is comparable to the results of Shimooku et al (41), but lower than that reported by Nakamura et al (26). This stimulation might be the result of an assay condition containing unusually high AS concentration.…”

Section: Discussionsupporting

confidence: 85%

Effect of GM2 activator protein on the enzymatic hydrolysis of phospholipids and sphingomyelin

Shimada

2003

Journal of Lipid Research

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GM2 activator protein (GM2AP) is a specific protein cofactor that stimulates the enzymatic hydrolysis of the GalNAc from GM2, a sialic acid containing glycosphingolipid, both in vitro and in lysosomes. While phospholipids together with glycosphingolipids are important membrane constituents, little is known about the possible effect of GM2AP on the hydrolysis of phospholipids. Several recent reports suggest that GM2AP might have functions other than stimulating the conversion of GM2 into GM3 by ␤ -hexosaminidase A, such as inhibiting the activity of platelet activating factor and enhancing the degradation of phosphatidylcholine by phospholipase D (PLD). We therefore examined the effect of GM2AP on the in vitro hydrolyses of a number of phospholipids and sphingomyelin by microbial ( Streptomyces chromofuscus ) and plant (cabbage) PLD. GM2AP, at the concentration as low as 1.08 M (1 g/50 l) was found to inhibit about 70% of the hydrolyses of phosphatidylcholine, phosphatidylethanolamine, and phosphatidylinositol by PLD, whereas the same concentration of GM2AP only inhibited about 20-25% of the hydrolysis of sphingomyelin by sphingomyelinase and had no effect on the hydrolysis of sphingosylphosphorylcholine by PLD. Thus, GM2AP exerts strong and broad inhibitory effects on the hydrolysis of phospholipids carried out by plant and microbial PLDs. High ammonium sulfate concentration (1.6 M or 21.1%) masks this inhibitory effect, possibly due to the alteration of the ionic property of GM2AP. -Shimada, Y., Y-T. Li, and S-C. Li. Effect of GM2 activator protein on the enzymatic hydrolysis of phospholipids and sphingomyelin.

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Section: Discussionsupporting

confidence: 85%

Effect of GM2 activator protein on the enzymatic hydrolysis of phospholipids and sphingomyelin

Shimada

2003

Journal of Lipid Research

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“…15). The kidney PLD enzyme used in this study is ARF-dependent and shows properties similar to PLD1 (13). The enzymatic activity obtained in the presence of both PKC and PtdIns-4,5-P 2 disappears by the addition of higher concentrations of ammonium sulfate (Fig.…”

Section: Discussionmentioning

confidence: 97%

“…PLD was purified Ϸ200-fold as described (13) except that the rat kidney was used instead of the bovine kidney as enzyme source and that hydroxyapatite column chromatography was omitted from the purification procedure.…”

Section: Methodsmentioning

confidence: 99%

“…In earlier reports from this laboratory, cytosol from the rat kidney was essential for the activation of ARF-dependent PLD purified partially from the same tissue (13). The kidney PLD is an ARF-dependent enzyme resembling PLD1.…”

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confidence: 99%

“…The kidney PLD is an ARF-dependent enzyme resembling PLD1. The active components in the cytosol consist of at least three protein factors; ARF, RhoA, and a heat-stable protein (13). The heat-stable protein shows a molecular size of 23 kDa upon SDS͞PAGE (14).…”

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confidence: 99%

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Requirement of G _M2 ganglioside activator for phospholipase D activation

Nakamura

Akisue²,

Jinnai³

et al. 1998

Proc. Natl. Acad. Sci. U.S.A.

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authors request that the following corrections be noted. It was accidentally stated that the studies by Kajita et al. (1) and Lee et al. (2) dealt with cinnamoyl-CoA reductase modified plants when in fact they concerned 4-coumarate:coenzyme A ligase (4CL) transgenic plants. Lignin concentration was reduced by down-regulation of 4CL activity in both studies (1, 2). In a subsequent article, Kajita et al. (3) reported a negligible decrease in lignin concentration and a decreased syringyl-toguaiacyl ratio for lignin composition of a sense-suppressed 4CL transgenic tobacco line. Kajita et al. (1) rather than Kajita et al. (3) was inadvertently cited when this later report was contrasted with the large decreases in lignin concentration and an increased syringyl-to-guaiacyl lignin ratio for anti-sense suppressed 4CL Arabidopsis transgenics (2). The authors apologize for the confusion these errors have created for readers of their Commentary and to the authors of the cited work for misrepresenting their research. November 10, 1998, of Proc. Natl. Acad. Sci. USA (95, 13612-13617), the authors request that the following correction be noted: In Fig. 2 appearing on page 13614, the genotype identification for testicular histology in panels C and D were shown reversed. The correct identification is Ϫ͞Ϫ for panel C and ϩ͞ϩ for panel D. The fifth sentence of the figure legend should read as follows: "Histological sections at lower (E) and higher (D) magnification of the seminiferous tubuli from a wild-type and mutant (F and C) mouse."Cell Biology. In the article "Efficient construction of a large nonimmune phage antibody library: The production of highaffinity human single-chain antibodies to protein antigens" by

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Phospholipase D

Exton

1998

Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biolog

113

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Reconstitution of GTP‐γ‐S‐dependent phospholipase D activity with ARF, RhoA, and a soluble 36‐kDa protein

Cited by 14 publications

References 29 publications

Effect of GM2 activator protein on the enzymatic hydrolysis of phospholipids and sphingomyelin

Effect of GM2 activator protein on the enzymatic hydrolysis of phospholipids and sphingomyelin

Requirement of G _M2 ganglioside activator for phospholipase D activation

Phospholipase D

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Reconstitution of GTP‐γ‐S‐dependent phospholipase D activity with ARF, RhoA, and a soluble 36‐kDa protein

Cited by 14 publications

References 29 publications

Effect of GM2 activator protein on the enzymatic hydrolysis of phospholipids and sphingomyelin

Effect of GM2 activator protein on the enzymatic hydrolysis of phospholipids and sphingomyelin

Requirement of G M2 ganglioside activator for phospholipase D activation

Phospholipase D

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Requirement of G _M2 ganglioside activator for phospholipase D activation