Characterization of meFucoidan as a Selective Inhibitor for Secretory Phospholipase A(2)-IIA and the Phosphorylation of meFucoidan-Binding Proteins by A-Kinase in Vitro.

Characterization of meFucoidan as a Selective Inhibitor for Secretory Phospholipase A(2)-IIA and the Phosphorylation of meFucoidan-Binding Proteins by A-Kinase in Vitro. Research Abstract Details 

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Characterization of meFucoidan as a Selective Inhibitor for Secretory Phospholipase A(2)-IIA and the Phosphorylation of meFucoidan-Binding Proteins by A-Kinase in Vitro. Abstract Text:

Hiroko Maruyama,Kanzo Suzuki,Sayaka Miyai,Kenzo Ohtsuki,

The direct interaction of Mekabu fucoidan (meFucoidan) with four functional basic proteins (sPLA(2)-IIA, bFGF, histone H2B and HBV core protein) and three synthetic FGF-BP peptides (sp5, GE13 and RS6) was characterized in vitro. It was found that (i) meFucoidan inhibited dose-dependently the activity of sPLA(2)-IIA, but not pPLA(2), through its direct binding to the enzyme; (ii) sPLA(2)-IIA activity was sensitive to meFucoidan rather than heparin, but significantly stimulated by sulfatide; (iii) the A-kinase-mediated phosphorylation of these basic proteins, except sPLA(2)-IIA, and synthetic peptides, containing potent phosphorylation sites for A-kinase, was inhibited dose-dependently by meFucoidan; and (iv) two consensus meFucoidan-binding motifs (B-B-B-B-X and B-X-B-B-X; B, basic amino acid) in these basic proteins and synthetic peptides could be overlapping to the potent phosphorylation site (B-B-X-S/T) for the kinase in vitro. These results presented here suggest that meFucoidan functions as a selective inhibitor for sPLA(2)-IIA and the A-kinase-mediated phosphorylation of cellular meFucoidan-binding functional basic proteins in vitro.

Characterization of meFucoidan as a Selective Inhibitor for Secretory Phospholipase A(2)-IIA and the Phosphorylation of meFucoidan-Binding Proteins by A-Kinase in Vitro. Publishing Authors By Initials

H Maruyama,K Suzuki,S Miyai,K Ohtsuki,

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Characterization of meFucoidan as a Selective Inhibitor for Secretory Phospholipase A(2)-IIA and the Phosphorylation of meFucoidan-Binding Proteins by A-Kinase in Vitro. Journal Published:

PUBLICATION TYPE: Journal Article

Journal: Biological & pharmaceutical bulletin

VOLUME: 31

Page Numbers: 714-8

Journal Abbreviation: Biol. Pharm. Bull.

ISSN: 0918-6158

DAY: 1

MONTH: Apr

YEAR: 2008

Characterization of meFucoidan as a Selective Inhibitor for Secretory Phospholipase A(2)-IIA and the Phosphorylation of meFucoidan-Binding Proteins by A-Kinase in Vitro. Information

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LANGUAGE: eng

NlmUniqueID: 9311984

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Grant and Affiliation Information for Characterization of meFucoidan as a Selective Inhibitor for Secretory Phospholipase A(2)-IIA and the Phosphorylation of meFucoidan-Binding Proteins by A-Kinase in Vitro.

AFFILIATION: Laboratory of Pathology, Graduate School of Medical Sciences, Kitasato University.

Country: Japan

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MEDLINETA: Biol Pharm Bull

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