Sugar-Specific Inhibitory Effects of Wheat Germ Agglutinin and Phytohemagglutinin-E4 on Histamine Release Induced by Basic Secretagogues from Rat Peritoneal Mast Cells and Their Possible Action Sites.
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概要
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The histamine release induced by compound 48/80, bradykinin or polyethylenimine with a molecular weight of 600 (PEI<SUB>6</SUB>) was inhibited by wheat germ agglutinin (WGA) and phytohemagglutinin E-subunits (PHA-E<SUB>4</SUB>), and the inhibition was specifically reversed by N-acetyl glucosamine and N-acetyl galactosamine, respectively. Concanavalin A (Con A) and phytohemagglutinin L-subunits (PHA-L<SUB>4</SUB>) did not inhibit the histamine release induced by compound 48/80, bradykinin or PEI<SUB>6</SUB>. The histamine release induced by substance P was also inhibited sugar-specifically by WGA and PHA-E<SUB>4</SUB>. The binding sites for compound 48/80, bradykinin, PEI<SUB>6</SUB> and substance P, therefore, seemed to especially overlap each other. These binding sites were found to be glycoproteins having affinities to WGA and PHA-E<SUB>4</SUB>, but not to Con A and PHA-L<SUB>4</SUB>. The binding of WGA and PHA-E<SUB>4</SUB> to the glycoproteins resulted in inhibition of the interaction between the basic secretagogues including bradykinin and substance P and their binding sites on the mast cells. The bindings of five lectins to mast cell glycoproteins were examined by lectin-blotting. Several glycoproteins, which had specific affinities to WGA and PHA-E<SUB>4</SUB>, but not to Con A and PHA-L<SUB>4</SUB> were detected. We assumed that the binding sites for basic secretagogues which are coupled with histamine-releasing mechanisms exist among these glycoproteins. A 41-kDa protein (α-subunit of pertussis toxin-sensitive G protein) was not detected by WGA, suggesting that the binding sites for the basic secretagogues were not G proteins.
- 公益社団法人 日本薬理学会の論文
著者
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Umeda Masato
Department Of Functional Materials Science Saitama University
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Aoki Junken
Department Of Health Chemistry Faculty Of Pharmaceutical Sciences The University Of Tokyo
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Inoue Keizo
Department Of Biochemistry And Molecular Biology Indiana University
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Matsuda Koji
Department Of Endoscopy Jikei University
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UCHIDA Masaatsu
Department of Chemical Pharmacology, Faculty of Pharmaceutical Sciences, University of Tokyo
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NAGAYA Kohi
Department of Molecular Pharmacology, Meiji College of Pharmacy
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Inoue Keizo
Department of Health Chemistry, Faculty of Pharmaceutical Sciences, Tokyo University
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SUZUKI-NISHIMURA Tamiko
Department of Molecular Pharmacology, Meiji College of Pharmacy
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Umeda Masato
Department of Health Chemistry, Faculty of Pharmaceutical Sciences, Tokyo University
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Matsuda Koji
Department of Molecular Pharmacology, Meiji College of Pharmacy
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