To investigate the roles of calcium-binding proteins in degranulation, we used three anti-allergic drugs, amlexanox, cromolyn and tranilast, which inhibit IgE-mediated degranulation of mast cells, as molecular probes in affinity chromatography. All of these drugs, which have different structures but similar function, scarcely bound to calmodulin in bovine lung extract, but bound to the same kinds of calcium-binding proteins, such as the 10-kDa proteins isolated in this study, calcyphosine and annexins I–V. The 10-kDa proteins obtained on three drug-coupled resins and on phenyl-Sepharose were analysed by reversed-phase HPLC. It was found that two characteristic 10-kDa proteins, one polar and one less polar, were bound with all three drugs, although S100A2 (S100L), of the S100 family, was bound with phenyl-Sepharose. The cDNA and deduced amino acid sequence proved our major polar protein to be identical with the calcium-binding protein in bovine amniotic fluid (CAAF1, S100A12). The cDNA and deduced amino acid sequence of the less-polar protein shared 95% homology with human and mouse S100A13. In addition, it was demonstrated that the native S100A12 and recombinant S100A12 and S100A13 bind to immobilized amlexanox. On the basis of these findings, we speculate that the three anti-allergic drugs might inhibit degranulation by binding with S100A12 and S100A13.
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Research Article|
March 08 1999
Three distinct anti-allergic drugs, amlexanox, cromolyn and tranilast, bind to S100A12 and S100A13 of the S100 protein family
Tsuyoshi SHISHIBORI;
Tsuyoshi SHISHIBORI
*Department of Chemistry, Kagawa Medical University, 1750–1, Miki-cho, Kita-gun, 761–0793 Kagawa, Japan
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Yuhta OYAMA;
Yuhta OYAMA
*Department of Chemistry, Kagawa Medical University, 1750–1, Miki-cho, Kita-gun, 761–0793 Kagawa, Japan
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Osamu MATSUSHITA;
Osamu MATSUSHITA
†Department of Microbiology, Kagawa Medical University, 1750–1, Miki-cho, Kita-gun, 761–0793 Kagawa, Japan
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Kayoko YAMASHITA;
Kayoko YAMASHITA
*Department of Chemistry, Kagawa Medical University, 1750–1, Miki-cho, Kita-gun, 761–0793 Kagawa, Japan
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Hiromi FURUICHI;
Hiromi FURUICHI
‡Department of Plastic Surgery, Kagawa Medical University, 1750–1, Miki-cho, Kita-gun, 761–0793 Kagawa, Japan
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Akinobu OKABE;
Akinobu OKABE
†Department of Microbiology, Kagawa Medical University, 1750–1, Miki-cho, Kita-gun, 761–0793 Kagawa, Japan
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Hajime MAETA;
Hajime MAETA
§Department of Surgery1, Kagawa Medical University, 1750–1, Miki-cho, Kita-gun, 761–0793 Kagawa, Japan
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Yuiro HATA;
Yuiro HATA
‡Department of Plastic Surgery, Kagawa Medical University, 1750–1, Miki-cho, Kita-gun, 761–0793 Kagawa, Japan
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Ryoji KOBAYASHI
Ryoji KOBAYASHI
1
*Department of Chemistry, Kagawa Medical University, 1750–1, Miki-cho, Kita-gun, 761–0793 Kagawa, Japan
1To whom correspondence should be addressed (e-mail ryoji@kms.ac.jp).
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Publisher: Portland Press Ltd
Received:
September 28 1998
Revision Received:
December 07 1998
Accepted:
January 11 1999
Online ISSN: 1470-8728
Print ISSN: 0264-6021
The Biochemical Society, London © 1999
1999
Biochem J (1999) 338 (3): 583–589.
Article history
Received:
September 28 1998
Revision Received:
December 07 1998
Accepted:
January 11 1999
Citation
Tsuyoshi SHISHIBORI, Yuhta OYAMA, Osamu MATSUSHITA, Kayoko YAMASHITA, Hiromi FURUICHI, Akinobu OKABE, Hajime MAETA, Yuiro HATA, Ryoji KOBAYASHI; Three distinct anti-allergic drugs, amlexanox, cromolyn and tranilast, bind to S100A12 and S100A13 of the S100 protein family. Biochem J 15 March 1999; 338 (3): 583–589. doi: https://doi.org/10.1042/bj3380583
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