Purification of a heat‐stable activator protein for ADP‐ribosylation factor‐dependent phospholipase D<sup>1</sup>

Akisue, Toshihiro; Jinnai, Hitoshi; Hitomi, Tomohiro; Miwa, Noriko; Yoshida, Kohsuke; Nakamura, Shun‐ichi

doi:10.1016/s0014-5793(97)01611-6

Cited by 4 publications

(5 citation statements)

References 30 publications

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“…Sci. USA 95 (1998) 12251 4) and RhoA (26), PKC (9, 10), unidentified cytosolic proteins with 50 kDa (11,12) and 23 kDa (14). PtdIns-4,5-P 2 (3) and PtdEtn (27) also are involved in the reaction, although these lipids do not serve as the substrates.…”

Section: Discussionmentioning

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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Section: Discussionmentioning

confidence: 99%

“…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). Sequence analysis now reveals that this protein is highly homologous to previously known G M2 ganglioside activator.…”

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confidence: 95%

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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“…Nakamura et al found from their experiment in cell free system (26) that 1.6 M AS could unmask the PLD activity from inhibitory agents in the tissue extract. Since then, they have included 1.6 M of AS in the reaction mixture to examine the rat kidney PLD activity in vitro (25)(26)(27). They, however, did not examine the effect of GM2AP in the absence of AS except on one occasion in which the PLD activity was assayed in the absence of AS using streptolysin-O-permeabilized HL-60 cells (25).…”

Section: Discussionmentioning

confidence: 99%

“…Recently, additional activities for GM2AP have been described. a ) GM2AP enhanced the ADP-ribosylation factor-dependent phospholipase D (PLD) activity in vitro (25)(26)(27). b ) GM2AP inhibited the stimulatory activity of platelet activating factor (PAF) to release intracellular Ca 2 ϩ pools (28).…”

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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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“…The immunoprecipitated proteins were eluted with a FLAG peptide (100 µg\ml) and subjected to SDS\PAGE using 12.5 % gels [21] followed by immunoblot analysis [22]. In some experiments (see Figure 5 below) FLAGtagged PLD2 immunoprecipitated with anti-FLAG M2 affinity gels was incubated with the heat-treated supernatant fractions (100 µg of protein each) prepared from rat kidney [23], purified recombinant G M# activator (3 µg) or ARF (3 µg) in the presence of 5 µM PtdCho, 80 µM PtdEtn, 7 µM PtdIns(4,5)P # and 1 mM MgCl # for 2 h. The immunoprecipitated proteins were eluted from the gels and analysed as above.…”

Section: Immunoprecipitation and Immunoblot Analysesmentioning

confidence: 99%

Regulation of mammalian phospholipase D2: interaction with and stimulation by GM2 activator

et al. 2001

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Purification of a heat‐stable activator protein for ADP‐ribosylation factor‐dependent phospholipase D¹

Cited by 4 publications

References 30 publications

Requirement of G _M2 ganglioside activator for phospholipase D activation

Requirement of G _M2 ganglioside activator for phospholipase D activation

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

Regulation of mammalian phospholipase D2: interaction with and stimulation by GM2 activator

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Purification of a heat‐stable activator protein for ADP‐ribosylation factor‐dependent phospholipase D1

Cited by 4 publications

References 30 publications

Requirement of G M2 ganglioside activator for phospholipase D activation

Requirement of G M2 ganglioside activator for phospholipase D activation

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

Regulation of mammalian phospholipase D2: interaction with and stimulation by GM2 activator

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Purification of a heat‐stable activator protein for ADP‐ribosylation factor‐dependent phospholipase D¹

Requirement of G _M2 ganglioside activator for phospholipase D activation

Requirement of G _M2 ganglioside activator for phospholipase D activation